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Serine--pyruvate aminotransferase (SPT) (EC 2.6.1.51) (Alanine--glyoxylate aminotransferase) (AGT) (EC 2.6.1.44)

 SPYA_HUMAN              Reviewed;         392 AA.
P21549; Q53QU6;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
22-NOV-2017, entry version 175.
RecName: Full=Serine--pyruvate aminotransferase;
Short=SPT;
EC=2.6.1.51;
AltName: Full=Alanine--glyoxylate aminotransferase;
Short=AGT;
EC=2.6.1.44;
Name=AGXT; Synonyms=AGT1, SPAT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2253628; DOI=10.1111/j.1432-1033.1990.tb19420.x;
Nishiyama K., Berstein G., Oda T., Ichiyama A.;
"Cloning and nucleotide sequence of cDNA encoding human liver serine-
pyruvate aminotransferase.";
Eur. J. Biochem. 194:9-18(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-11 AND MET-340, VARIANT HP1
ARG-170, AND SUBCELLULAR LOCATION.
PubMed=1703535; DOI=10.1083/jcb.111.6.2341;
Purdue P.E., Takada Y., Danpure C.J.;
"Identification of mutations associated with peroxisome-to-
mitochondrion mistargeting of alanine/glyoxylate aminotransferase in
primary hyperoxaluria type 1.";
J. Cell Biol. 111:2341-2351(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2363689; DOI=10.1042/bj2680517;
Takada Y., Kaneko N., Esumi H., Purdue P.E., Danpure C.J.;
"Human peroxisomal L-alanine: glyoxylate aminotransferase.
Evolutionary loss of a mitochondrial targeting signal by point
mutation of the initiation codon.";
Biochem. J. 268:517-520(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2045108; DOI=10.1016/0888-7543(91)90481-S;
Purdue P.E., Lumb M.J., Fox M., Griffo G., Hamon-Benais C., Povey S.,
Danpure C.J.;
"Characterization and chromosomal mapping of a genomic clone encoding
human alanine:glyoxylate aminotransferase.";
Genomics 10:34-42(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL
PHOSPHATE AND AMINO-OXYACETIC ACID, SUBUNIT, AND PYRIDOXAL PHOSPHATE
AT LYS-209.
PubMed=12899834; DOI=10.1016/S0022-2836(03)00791-5;
Zhang X., Roe S.M., Hou Y., Bartlam M., Rao Z., Pearl L.H.,
Danpure C.J.;
"Crystal structure of alanine:glyoxylate aminotransferase and the
relationship between genotype and enzymatic phenotype in primary
hyperoxaluria type 1.";
J. Mol. Biol. 331:643-652(2003).
[11]
VARIANT HP1 PRO-205.
PubMed=2039493; DOI=10.1016/0006-291X(91)90396-O;
Nishiyama K., Funai T., Katafuchi R., Hattori F., Onoyama K.,
Ichiyama A.;
"Primary hyperoxaluria type I due to a point mutation of T to C in the
coding region of the serine:pyruvate aminotransferase gene.";
Biochem. Biophys. Res. Commun. 176:1093-1099(1991).
[12]
VARIANT HP1 GLU-82.
PubMed=1349575; DOI=10.1016/0888-7543(92)90225-H;
Purdue P.E., Lumb M.J., Allsop J., Minatogawa Y., Danpure C.J.;
"A glycine-to-glutamate substitution abolishes alanine:glyoxylate
aminotransferase catalytic activity in a subset of patients with
primary hyperoxaluria type 1.";
Genomics 13:215-218(1992).
[13]
VARIANT HP1 PHE-187.
PubMed=1301173; DOI=10.1093/hmg/1.8.643;
Minatogawa Y., Tone S., Allsop J., Purdue P.E., Takada Y.,
Danpure C.J., Kido R.;
"A serine-to-phenylalanine substitution leads to loss of
alanine:glyoxylate aminotransferase catalytic activity and
immunoreactivity in a patient with primary hyperoxaluria type 1.";
Hum. Mol. Genet. 1:643-644(1992).
[14]
VARIANTS HP1 ARG-41 AND ILE-152.
PubMed=8101040;
Danpure C.J., Purdue P.E., Fryer P., Griffiths S., Allsop J.,
Lumb M.J., Guttridge K.M., Jennings P.R., Scheinman J.I., Mauer S.M.,
Davidson N.O.;
"Enzymological and mutational analysis of a complex primary
hyperoxaluria type 1 phenotype involving alanine:glyoxylate
aminotransferase peroxisome-to-mitochondrion mistargeting and
intraperoxisomal aggregation.";
Am. J. Hum. Genet. 53:417-432(1993).
[15]
REVIEW ON HP1.
PubMed=8507692; DOI=10.1016/0300-9084(93)90091-6;
Danpure C.J.;
"Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion
mistargeting of alanine:glyoxylate aminotransferase.";
Biochimie 75:309-315(1993).
[16]
VARIANTS HP1 CYS-233; HIS-233 AND THR-244.
PubMed=9192270; DOI=10.1136/jmg.34.6.489;
von Schnakenburg C., Rumsby G.;
"Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of
the AGXT gene.";
J. Med. Genet. 34:489-492(1997).
[17]
VARIANTS HP1 ARG-108; TYR-173; ARG-190; ALA-296 DEL AND ASP-350.
PubMed=9604803;
von Schnakenburg C., Rumsby G.;
"Identification of new mutations in primary hyperoxaluria type 1
(PH1).";
J. Nephrol. 11:15-17(1998).
[18]
VARIANTS HP1 VAL-41; GLU-95 INS; ARG-116 AND ARG-156.
PubMed=10394939; DOI=10.1007/s004390050984;
Amoroso A., Pirulli D., Puzzer D., Ferri L., Crovella S.,
Ferrettini C., Marangella M., Mazzola G., Florian F.;
"Gene symbol: AGXT. Disease: primary hyperoxaluria type I.";
Hum. Genet. 104:441-441(1999).
[19]
VARIANTS HP1 VAL-41; GLU-95 INS; ARG-116 AND ARG-156.
PubMed=10453743; DOI=10.1007/s004390050998;
Pirulli D., Puzzer D., Ferri L., Crovella S., Amoroso A.,
Ferrettini C., Marangella M., Mazzola G., Florian F.;
"Molecular analysis of hyperoxaluria type 1 in Italian patients
reveals eight new mutations in the alanine: glyoxylate
aminotransferase gene.";
Hum. Genet. 104:523-525(1999).
[20]
VARIANTS HP1 ARG-41; ARG-156; ARG-190; THR-244; CYS-289 AND PRO-298.
PubMed=10541294;
Rinat C., Wanders R.J.A., Drukker A., Halle D., Frishberg Y.;
"Primary hyperoxaluria type I: a model for multiple mutations in a
monogenic disease within a distinct ethnic group.";
J. Am. Soc. Nephrol. 10:2352-2358(1999).
[21]
VARIANTS HP1 ILE-152; ARG-170; ASN-183; CYS-233 AND THR-244.
PubMed=10862087;
DOI=10.1002/1098-1004(200006)15:6<577::AID-HUMU9>3.0.CO;2-#;
Basmaison O., Rolland M.-O., Cochat P., Bozon D.;
"Identification of 5 novel mutations in the AGXT gene.";
Hum. Mutat. 15:577-577(2000).
[22]
CHARACTERIZATION OF VARIANTS HP1 ARG-41; GLU-82; ILE-152; ARG-170 AND
THR-244, CHARACTERIZATION OF VARIANT LEU-11, AND MUTAGENESIS OF
LYS-209.
PubMed=10960483; DOI=10.1074/jbc.M006693200;
Lumb M.J., Danpure C.J.;
"Functional synergism between the most common polymorphism in human
alanine:glyoxylate aminotransferase and four of the most common
disease-causing mutations.";
J. Biol. Chem. 275:36415-36422(2000).
[23]
VARIANT HP1 ASP-112, AND VARIANT ILE-326.
PubMed=12559847; DOI=10.1016/S1096-7192(02)00204-4;
Coulter-Mackie M.B., Tung A., Henderson H.E., Toone J.R.,
Applegarth D.A.;
"The AGT gene in Africa: a distinctive minor allele haplotype, a
polymorphism (V326I), and a novel PH1 mutation (A112D) in Black
Africans.";
Mol. Genet. Metab. 78:44-50(2003).
[24]
CHARACTERIZATION OF VARIANT HP1 THR-244.
PubMed=12777626; DOI=10.1073/pnas.1131968100;
Santana A., Salido E., Torres A., Shapiro L.J.;
"Primary hyperoxaluria type 1 in the Canary Islands: a conformational
disease due to I244T mutation in the P11L-containing
alanine:glyoxylate aminotransferase.";
Proc. Natl. Acad. Sci. U.S.A. 100:7277-7282(2003).
[25]
VARIANTS HP1 ARG-82; ILE-152; VAL-153; ARG-170 AND ASP-336.
PubMed=15253729; DOI=10.1111/j.1523-1755.2004.00796.x;
van Woerden C.S., Groothoff J.W., Wijburg F.A., Annink C.,
Wanders R.J.A., Waterham H.R.;
"Clinical implications of mutation analysis in primary hyperoxaluria
type 1.";
Kidney Int. 66:746-752(2004).
[26]
VARIANTS HP1 VAL-139 DEL; ARG-156; LEU-158; ARG-190; GLU-201; LEU-233;
THR-244 AND ARG-253, AND VARIANT ASN-9.
PubMed=15849466; DOI=10.1159/000085411;
Monico C.G., Olson J.B., Milliner D.S.;
"Implications of genotype and enzyme phenotype in pyridoxine response
of patients with type I primary hyperoxaluria.";
Am. J. Nephrol. 25:183-188(2005).
[27]
VARIANTS HP1 ARG-41; ARG-108; ARG-156; ARG-190; ARG-195; HIS-243;
THR-244; MET-279; THR-287; CYS-289 AND PRO-298, AND VARIANT ASN-9.
PubMed=15961946; DOI=10.1159/000086357;
Frishberg Y., Rinat C., Shalata A., Khatib I., Feinstein S.,
Becker-Cohen R., Weismann I., Wanders R.J.A., Rumsby G., Roels F.,
Mandel H.;
"Intra-familial clinical heterogeneity: absence of genotype-phenotype
correlation in primary hyperoxaluria type 1 in Israel.";
Am. J. Nephrol. 25:269-275(2005).
[28]
VARIANTS HP1 ARG-161 AND LEU-218, AND VARIANTS THR-279 AND VAL-280.
PubMed=15963748; DOI=10.1016/j.ymgme.2005.05.005;
Coulter-Mackie M.B., Lian Q., Applegarth D., Toone J.;
"The major allele of the alanine:glyoxylate aminotransferase gene:
nine novel mutations and polymorphisms associated with primary
hyperoxaluria type 1.";
Mol. Genet. Metab. 86:172-178(2005).
[29]
CHARACTERIZATION OF VARIANTS HP1 ARG-41; VAL-41; GLU-82; ARG-108;
ASP-112; ARG-156; ARG-161; ARG-170; TYR-173; ASN-183; PHE-187; PRO-205
AND LEU-218, MUTAGENESIS OF LYS-209, AND SUBUNIT.
PubMed=16971151; DOI=10.1016/j.ymgme.2006.07.013;
Coulter-Mackie M.B., Lian Q.;
"Consequences of missense mutations for dimerization and turnover of
alanine:glyoxylate aminotransferase: study of a spectrum of
mutations.";
Mol. Genet. Metab. 89:349-359(2006).
[30]
VARIANTS HP1 CYS-36; ARG-41; GLU-41; PRO-150; ILE-152; ARG-156;
LEU-158; CYS-161; SER-161; PRO-166; ARG-170; TYR-173; CYS-233;
HIS-233; THR-244 AND ARG-253, VARIANT ASN-9, CHARACTERIZATION OF
VARIANTS HP1 CYS-36; GLU-41; PRO-150; ARG-156; LEU-158; CYS-161;
SER-161; PRO-166; TYR-173; CYS-233; HIS-233 AND ARG-253, AND
CHARACTERIZATION OF VARIANT ASN-9.
PubMed=17495019; DOI=10.1373/clinchem.2006.084434;
Williams E., Rumsby G.;
"Selected exonic sequencing of the AGXT gene provides a genetic
diagnosis in 50% of patients with primary hyperoxaluria type 1.";
Clin. Chem. 53:1216-1221(2007).
[31]
CHARACTERIZATION OF VARIANTS HP1 ARG-161; CYS-161 AND SER-161, AND
SUBCELLULAR LOCATION.
PubMed=24055001; DOI=10.1016/j.bbadis.2013.09.002;
Oppici E., Roncador A., Montioli R., Bianconi S., Cellini B.;
"Gly161 mutations associated with primary hyperoxaluria type I induce
the cytosolic aggregation and the intracellular degradation of the
apo-form of alanine:glyoxylate aminotransferase.";
Biochim. Biophys. Acta 1832:2277-2288(2013).
[32]
CHARACTERIZATION OF VARIANTS HP1 ARG-41; ILE-152; ARG-170 AND THR-244,
SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=23229545; DOI=10.1074/jbc.M112.432617;
Fargue S., Lewin J., Rumsby G., Danpure C.J.;
"Four of the most common mutations in primary hyperoxaluria type 1
unmask the cryptic mitochondrial targeting sequence of
alanine:glyoxylate aminotransferase encoded by the polymorphic minor
allele.";
J. Biol. Chem. 288:2475-2484(2013).
[33]
VARIANT HP1 ASN-202.
PubMed=24934730; DOI=10.1186/1471-2369-15-92;
Li G.M., Xu H., Shen Q., Gong Y.N., Fang X.Y., Sun L., Liu H.M.,
An Y.;
"Mutational analysis of AGXT in two Chinese families with primary
hyperoxaluria type 1.";
BMC Nephrol. 15:92-92(2014).
[34]
CHARACTERIZATION OF VARIANT HP1 ARG-47, AND SUBCELLULAR LOCATION.
PubMed=26149463; DOI=10.1016/j.bbapap.2015.07.002;
Montioli R., Oppici E., Dindo M., Roncador A., Gotte G., Cellini B.,
Borri Voltattorni C.;
"Misfolding caused by the pathogenic mutation G47R on the minor allele
of alanine:glyoxylate aminotransferase and chaperoning activity of
pyridoxine.";
Biochim. Biophys. Acta 1854:1280-1289(2015).
-!- CATALYTIC ACTIVITY: L-serine + pyruvate = 3-hydroxypyruvate + L-
alanine.
-!- CATALYTIC ACTIVITY: L-alanine + glyoxylate = pyruvate + glycine.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12899834,
ECO:0000269|PubMed:16971151, ECO:0000269|PubMed:23229545}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-727098, EBI-727098;
P50542-1:PEX5; NbExp=4; IntAct=EBI-727098, EBI-15982193;
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:1703535,
ECO:0000269|PubMed:23229545, ECO:0000269|PubMed:24055001,
ECO:0000269|PubMed:26149463}. Mitochondrion
{ECO:0000269|PubMed:1703535, ECO:0000269|PubMed:23229545}.
Note=Predominantly localized in the peroxisomes. Mitochondrial
mistargeting occurs in variant proteins Arg-41, Arg-47, Ile-152,
Arg-170 and Thr-244 associated with the disease HP1.
{ECO:0000269|PubMed:23229545}.
-!- TISSUE SPECIFICITY: Liver.
-!- POLYMORPHISM: Polymorphism at position 11 acts synergistically
with different mutations in AGXT producing specific enzymic
phenotypes in HP1 patients. The combined presence of Leu-11 and
Met-340 polymorphisms defines the minor AGXT allele, whereas their
absence defines the major allele. The minor allele has frequencies
of 20% in normal European and North American populations, and 50%
in HP1 patients. {ECO:0000269|PubMed:1703535}.
-!- DISEASE: Hyperoxaluria primary 1 (HP1) [MIM:259900]: An inborn
error of glyoxylate metabolism characterized by increased
excretion of oxalate and glycolate, and progressive tissue
accumulation of insoluble calcium oxalate. Affected individuals
are at risk for nephrolithiasis, nephrocalcinosis and early onset
end-stage renal disease. {ECO:0000269|PubMed:10394939,
ECO:0000269|PubMed:10453743, ECO:0000269|PubMed:10541294,
ECO:0000269|PubMed:10862087, ECO:0000269|PubMed:10960483,
ECO:0000269|PubMed:12559847, ECO:0000269|PubMed:12777626,
ECO:0000269|PubMed:1301173, ECO:0000269|PubMed:1349575,
ECO:0000269|PubMed:15253729, ECO:0000269|PubMed:15849466,
ECO:0000269|PubMed:15961946, ECO:0000269|PubMed:15963748,
ECO:0000269|PubMed:16971151, ECO:0000269|PubMed:1703535,
ECO:0000269|PubMed:17495019, ECO:0000269|PubMed:2039493,
ECO:0000269|PubMed:23229545, ECO:0000269|PubMed:24055001,
ECO:0000269|PubMed:24934730, ECO:0000269|PubMed:26149463,
ECO:0000269|PubMed:8101040, ECO:0000269|PubMed:9192270,
ECO:0000269|PubMed:9604803}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
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EMBL; X56092; CAA39572.1; -; mRNA.
EMBL; X53414; CAA37493.1; -; mRNA.
EMBL; D13368; BAA02632.1; -; mRNA.
EMBL; M61763; AAA51680.1; -; Genomic_DNA.
EMBL; AK292754; BAF85443.1; -; mRNA.
EMBL; AC104809; AAY24168.1; -; Genomic_DNA.
EMBL; CH471063; EAW71222.1; -; Genomic_DNA.
EMBL; BC132819; AAI32820.1; -; mRNA.
CCDS; CCDS2543.1; -.
PIR; I39419; XNHUSP.
RefSeq; NP_000021.1; NM_000030.2.
UniGene; Hs.144567; -.
PDB; 1H0C; X-ray; 2.50 A; A=1-392.
PDB; 1J04; X-ray; 2.60 A; A=1-392.
PDB; 2YOB; X-ray; 1.90 A; A/B=1-388.
PDB; 3R9A; X-ray; 2.35 A; A/C=1-392.
PDB; 4CBR; X-ray; 2.30 A; A=1-392.
PDB; 4CBS; X-ray; 2.30 A; A=1-392.
PDB; 4I8A; X-ray; 2.90 A; A/B/C/D=1-392.
PDB; 4KXK; X-ray; 2.90 A; A/C=1-392.
PDB; 4KYO; X-ray; 2.20 A; A/C=1-392.
PDB; 5F9S; X-ray; 1.70 A; A/B=6-391.
PDB; 5HHY; X-ray; 1.70 A; A/B=6-391.
PDB; 5LUC; X-ray; 1.80 A; A/B/E/G/M/N/S/T=1-392.
PDB; 5OFY; X-ray; 2.80 A; A=1-392.
PDB; 5OG0; X-ray; 2.50 A; A=1-392.
PDBsum; 1H0C; -.
PDBsum; 1J04; -.
PDBsum; 2YOB; -.
PDBsum; 3R9A; -.
PDBsum; 4CBR; -.
PDBsum; 4CBS; -.
PDBsum; 4I8A; -.
PDBsum; 4KXK; -.
PDBsum; 4KYO; -.
PDBsum; 5F9S; -.
PDBsum; 5HHY; -.
PDBsum; 5LUC; -.
PDBsum; 5OFY; -.
PDBsum; 5OG0; -.
ProteinModelPortal; P21549; -.
SMR; P21549; -.
BioGrid; 106694; 4.
DIP; DIP-59650N; -.
IntAct; P21549; 28.
MINT; MINT-1419187; -.
STRING; 9606.ENSP00000302620; -.
DrugBank; DB08060; 4-(2-AMINOPHENYL)-4-OXOBUTANOIC ACID.
DrugBank; DB02079; Aminooxyacetic acid.
DrugBank; DB00145; Glycine.
DrugBank; DB00160; L-Alanine.
DrugBank; DB00133; L-Serine.
DrugBank; DB04083; N'-Pyridoxyl-Lysine-5'-Monophosphate.
DrugBank; DB00114; Pyridoxal Phosphate.
iPTMnet; P21549; -.
PhosphoSitePlus; P21549; -.
BioMuta; AGXT; -.
DMDM; 134855; -.
MaxQB; P21549; -.
PaxDb; P21549; -.
PeptideAtlas; P21549; -.
PRIDE; P21549; -.
Ensembl; ENST00000307503; ENSP00000302620; ENSG00000172482.
GeneID; 189; -.
KEGG; hsa:189; -.
UCSC; uc002waa.5; human.
CTD; 189; -.
DisGeNET; 189; -.
EuPathDB; HostDB:ENSG00000172482.4; -.
GeneCards; AGXT; -.
GeneReviews; AGXT; -.
HGNC; HGNC:341; AGXT.
HPA; HPA035370; -.
HPA; HPA035371; -.
MalaCards; AGXT; -.
MIM; 259900; phenotype.
MIM; 604285; gene.
neXtProt; NX_P21549; -.
OpenTargets; ENSG00000172482; -.
Orphanet; 93598; Primary hyperoxaluria type 1.
PharmGKB; PA24633; -.
eggNOG; KOG2862; Eukaryota.
eggNOG; COG0075; LUCA.
GeneTree; ENSGT00390000006648; -.
HOGENOM; HOG000171815; -.
HOVERGEN; HBG006907; -.
InParanoid; P21549; -.
KO; K00830; -.
OMA; WGCDDKP; -.
OrthoDB; EOG091G0EMK; -.
PhylomeDB; P21549; -.
TreeFam; TF313234; -.
BioCyc; MetaCyc:HS10525-MONOMER; -.
BRENDA; 2.6.1.44; 2681.
Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
EvolutionaryTrace; P21549; -.
GeneWiki; AGXT; -.
GenomeRNAi; 189; -.
PRO; PR:P21549; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000172482; -.
CleanEx; HS_AGXT; -.
Genevisible; P21549; HS.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:UniProtKB.
GO; GO:0016597; F:amino acid binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0004760; F:serine-pyruvate transaminase activity; IBA:GO_Central.
GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IDA:UniProtKB.
GO; GO:0009436; P:glyoxylate catabolic process; IDA:UniProtKB.
GO; GO:0046487; P:glyoxylate metabolic process; IMP:HGNC.
GO; GO:0042853; P:L-alanine catabolic process; IDA:UniProtKB.
GO; GO:0019448; P:L-cysteine catabolic process; IDA:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:0046724; P:oxalic acid secretion; IEA:Ensembl.
GO; GO:0042866; P:pyruvate biosynthetic process; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR000192; Aminotrans_V_dom.
InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
Pfam; PF00266; Aminotran_5; 1.
PIRSF; PIRSF000524; SPT; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Aminotransferase; Complete proteome;
Disease mutation; Mitochondrion; Peroxisome; Phosphoprotein;
Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase.
CHAIN 1 392 Serine--pyruvate aminotransferase.
/FTId=PRO_0000150237.
BINDING 360 360 Substrate.
MOD_RES 9 9 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 209 209 N6-(pyridoxal phosphate)lysine.
MOD_RES 225 225 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O35423}.
MOD_RES 225 225 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O35423}.
MOD_RES 234 234 N6-acetyllysine.
{ECO:0000250|UniProtKB:O35423}.
MOD_RES 312 312 N6-acetyllysine.
{ECO:0000250|UniProtKB:O35423}.
VARIANT 9 9 T -> N (polymorphism; no loss of
alanine--glyoxylate aminotransferase
activity; dbSNP:rs115014558).
{ECO:0000269|PubMed:15849466,
ECO:0000269|PubMed:15961946,
ECO:0000269|PubMed:17495019}.
/FTId=VAR_060547.
VARIANT 11 11 P -> L (common polymorphism; reduction of
specific alanine--glyoxylate
aminotransferase activity in vitro;
causes mitochondrial mistargeting when
associated with R-170; dbSNP:rs34116584).
{ECO:0000269|PubMed:10960483,
ECO:0000269|PubMed:1703535}.
/FTId=VAR_000587.
VARIANT 22 22 N -> S (in dbSNP:rs34885252).
/FTId=VAR_048236.
VARIANT 36 36 R -> C (in HP1; when associated with L-11
and M-340 on the minor AGXT allele;
results in loss of alanine--glyoxylate
aminotransferase activity;
dbSNP:rs180177157).
{ECO:0000269|PubMed:17495019}.
/FTId=VAR_074582.
VARIANT 41 41 G -> E (in HP1; loss of alanine--
glyoxylate aminotransferase activity;
dbSNP:rs180177168).
{ECO:0000269|PubMed:17495019}.
/FTId=VAR_074583.
VARIANT 41 41 G -> R (in HP1; when associated with L-11
and M-340 on the minor AGXT allele;
results in loss of protein stability;
loss of alanine--glyoxylate
aminotransferase activity; loss of
dimerization; partial mitochondrial
mistargeting; intraperoxisomal protein
aggregation seen; dbSNP:rs121908523).
{ECO:0000269|PubMed:10541294,
ECO:0000269|PubMed:10960483,
ECO:0000269|PubMed:15961946,
ECO:0000269|PubMed:16971151,
ECO:0000269|PubMed:17495019,
ECO:0000269|PubMed:23229545,
ECO:0000269|PubMed:8101040}.
/FTId=VAR_000588.
VARIANT 41 41 G -> V (in HP1; reduced alanine--
glyoxylate aminotransferase activity; no
loss of dimerization; no effect on
protein stability; dbSNP:rs180177168).
{ECO:0000269|PubMed:10394939,
ECO:0000269|PubMed:10453743,
ECO:0000269|PubMed:16971151}.
/FTId=VAR_010969.
VARIANT 47 47 G -> R (in HP1; when associated with L-11
and M-340 on the minor AGXT allele;
results in protein misfolding; decreased
alanine--glyoxylate aminotransferase
activity; reduced expression levels;
reduced pyridoxal phosphate binding;
reduced dimerization; reduced
thermostability; increased propensity to
aggregation; increased susceptibility to
proteolytic degradation within the N-
terminal region; mitochondrial
mistargeting; exposure to pyridoxine can
rescue the functionality by partially
preventing aggregation and degradation
and by redirecting all the protein to the
peroxisome; dbSNP:rs180177173).
{ECO:0000269|PubMed:26149463}.
/FTId=VAR_074584.
VARIANT 82 82 G -> E (in HP1; abolishes alanine--
glyoxylate aminotransferase activity by
interfering with pyridoxal phosphate
binding; dbSNP:rs121908522).
{ECO:0000269|PubMed:10960483,
ECO:0000269|PubMed:1349575,
ECO:0000269|PubMed:16971151}.
/FTId=VAR_008878.
VARIANT 82 82 G -> R (in HP1; dbSNP:rs180177185).
{ECO:0000269|PubMed:15253729}.
/FTId=VAR_060548.
VARIANT 95 95 E -> EE (in HP1).
{ECO:0000269|PubMed:10394939,
ECO:0000269|PubMed:10453743}.
/FTId=VAR_010970.
VARIANT 108 108 W -> R (in HP1; when associated with L-11
and M-340 on the minor AGXT allele;
results in loss of alanine--glyoxylate
aminotransferase activity; loss of
dimerization; decreased protein
stability; dbSNP:rs180177197).
{ECO:0000269|PubMed:15961946,
ECO:0000269|PubMed:16971151,
ECO:0000269|PubMed:9604803}.
/FTId=VAR_060549.
VARIANT 112 112 A -> D (in HP1; loss of alanine--
glyoxylate aminotransferase activity;
loss of dimerization; decreased protein
stability; causes protein aggregation;
dbSNP:rs796052061).
{ECO:0000269|PubMed:12559847,
ECO:0000269|PubMed:16971151}.
/FTId=VAR_060550.
VARIANT 116 116 G -> R (in HP1; dbSNP:rs180177207).
{ECO:0000269|PubMed:10394939,
ECO:0000269|PubMed:10453743}.
/FTId=VAR_010971.
VARIANT 139 139 Missing (in HP1).
{ECO:0000269|PubMed:15849466}.
/FTId=VAR_060551.
VARIANT 150 150 L -> P (in HP1; when associated with L-11
and M-340 on the minor AGXT allele;
results in loss of alanine--glyoxylate
aminotransferase activity;
dbSNP:rs180177222).
{ECO:0000269|PubMed:17495019}.
/FTId=VAR_074585.
VARIANT 152 152 F -> I (in HP1; when associated with L-11
and M-340 on the minor AGXT allele;
results in protein destabilization;
decreased alanine--glyoxylate
aminotransferase activity; no loss of
dimerization; mitochondrial mistargeting;
dbSNP:rs121908524).
{ECO:0000269|PubMed:10862087,
ECO:0000269|PubMed:10960483,
ECO:0000269|PubMed:15253729,
ECO:0000269|PubMed:17495019,
ECO:0000269|PubMed:23229545,
ECO:0000269|PubMed:8101040}.
/FTId=VAR_000589.
VARIANT 153 153 L -> V (in HP1; dbSNP:rs180177223).
{ECO:0000269|PubMed:15253729}.
/FTId=VAR_060552.
VARIANT 156 156 G -> R (in HP1; loss of alanine--
glyoxylate aminotransferase activity;
loss of dimerization; decreased protein
stability; dbSNP:rs121908530).
{ECO:0000269|PubMed:10394939,
ECO:0000269|PubMed:10453743,
ECO:0000269|PubMed:10541294,
ECO:0000269|PubMed:15849466,
ECO:0000269|PubMed:15961946,
ECO:0000269|PubMed:16971151,
ECO:0000269|PubMed:17495019}.
/FTId=VAR_010972.
VARIANT 158 158 S -> L (in HP1; loss of alanine--
glyoxylate aminotransferase activity;
dbSNP:rs180177225).
{ECO:0000269|PubMed:15849466,
ECO:0000269|PubMed:17495019}.
/FTId=VAR_060553.
VARIANT 161 161 G -> C (in HP1; when associated with L-11
and M-340 on the minor AGXT allele;
results in loss of alanine--glyoxylate
aminotransferase activity; reduced
expression levels; decreased protein
stability; protein aggregation seen in
the cytosol with a decreased aggregation
propensity in the presence of pyridoxal
phosphate; reduced peroxisomal
localization; dbSNP:rs180177227).
{ECO:0000269|PubMed:17495019,
ECO:0000269|PubMed:24055001}.
/FTId=VAR_074586.
VARIANT 161 161 G -> R (in HP1; loss of alanine--
glyoxylate aminotransferase activity;
reduced expression levels; decreased
protein stability; protein aggregation
seen in the cytosol with a decreased
aggregation propensity in the presence of
pyridoxal phosphate; loss of
dimerization; dbSNP:rs180177227).
{ECO:0000269|PubMed:15963748,
ECO:0000269|PubMed:16971151,
ECO:0000269|PubMed:24055001}.
/FTId=VAR_060554.
VARIANT 161 161 G -> S (in HP1; when associated with L-11
and M-340 on the minor AGXT allele;
results in loss of alanine--glyoxylate
aminotransferase activity; reduced
expression levels; decreased protein
stability; protein aggregation seen in
the cytosol with a decreased aggregation
propensity in the presence of pyridoxal
phosphate; reduced peroxisomal
localization; dbSNP:rs180177227).
{ECO:0000269|PubMed:17495019,
ECO:0000269|PubMed:24055001}.
/FTId=VAR_074587.
VARIANT 166 166 L -> P (in HP1; when associated with L-11
and M-340 on the minor AGXT allele;
results in loss of alanine--glyoxylate
aminotransferase activity;
dbSNP:rs180177230).
{ECO:0000269|PubMed:17495019}.
/FTId=VAR_074588.
VARIANT 170 170 G -> R (in HP1; when associated with L-11
and M-340 on the minor AGXT allele;
results in mitochondrial mistargeting;
slight decrease in alanine--glyoxylate
aminotransferase activity; loss of
dimerization; partial loss of protein
stability but protein stability increases
in the presence of pyridoxal phosphate;
causes protein aggregation;
dbSNP:rs121908529).
{ECO:0000269|PubMed:10862087,
ECO:0000269|PubMed:10960483,
ECO:0000269|PubMed:15253729,
ECO:0000269|PubMed:16971151,
ECO:0000269|PubMed:1703535,
ECO:0000269|PubMed:17495019,
ECO:0000269|PubMed:23229545}.
/FTId=VAR_000590.
VARIANT 173 173 C -> Y (in HP1; loss of alanine--
glyoxylate aminotransferase activity;
loss of dimerization; decreased protein
stability; causes protein aggregation;
dbSNP:rs180177231).
{ECO:0000269|PubMed:16971151,
ECO:0000269|PubMed:17495019,
ECO:0000269|PubMed:9604803}.
/FTId=VAR_060555.
VARIANT 183 183 D -> N (in HP1; loss of alanine--
glyoxylate aminotransferase activity; no
loss of dimerization; no effect on
protein stability; dbSNP:rs180177236).
{ECO:0000269|PubMed:10862087,
ECO:0000269|PubMed:16971151}.
/FTId=VAR_010973.
VARIANT 187 187 S -> F (in HP1; loss of alanine--
glyoxylate aminotransferase activity;
loss of dimerization but improved
dimerization in the presence of pyridoxal
phosphate; decreased protein stability;
dbSNP:rs180177238).
{ECO:0000269|PubMed:1301173,
ECO:0000269|PubMed:16971151}.
/FTId=VAR_000591.
VARIANT 190 190 G -> R (in HP1; dbSNP:rs180177239).
{ECO:0000269|PubMed:10541294,
ECO:0000269|PubMed:15849466,
ECO:0000269|PubMed:15961946,
ECO:0000269|PubMed:9604803}.
/FTId=VAR_060556.
VARIANT 195 195 M -> R (in HP1; dbSNP:rs180177244).
{ECO:0000269|PubMed:15961946}.
/FTId=VAR_060557.
VARIANT 201 201 D -> E (in HP1; dbSNP:rs180177246).
{ECO:0000269|PubMed:15849466}.
/FTId=VAR_060558.
VARIANT 202 202 I -> N (in HP1; unknown pathological
significance).
{ECO:0000269|PubMed:24934730}.
/FTId=VAR_074589.
VARIANT 205 205 S -> P (in HP1; loss of alanine--
glyoxylate aminotransferase activity;
decreased protein stability;
dbSNP:rs121908520).
{ECO:0000269|PubMed:16971151,
ECO:0000269|PubMed:2039493}.
/FTId=VAR_000592.
VARIANT 218 218 S -> L (in HP1; loss of alanine--
glyoxylate aminotransferase activity;
loss of dimerization; no effect on
protein stability; dbSNP:rs180177253).
{ECO:0000269|PubMed:15963748,
ECO:0000269|PubMed:16971151}.
/FTId=VAR_060559.
VARIANT 233 233 R -> C (in HP1; when associated with L-11
and M-340 on the minor AGXT allele;
results in loss of alanine--glyoxylate
aminotransferase activity;
dbSNP:rs121908526).
{ECO:0000269|PubMed:10862087,
ECO:0000269|PubMed:17495019,
ECO:0000269|PubMed:9192270}.
/FTId=VAR_008879.
VARIANT 233 233 R -> H (in HP1; when associated with L-11
and M-340 on the minor AGXT allele;
results in loss of alanine--glyoxylate
aminotransferase activity;
dbSNP:rs121908527).
{ECO:0000269|PubMed:17495019,
ECO:0000269|PubMed:9192270}.
/FTId=VAR_008880.
VARIANT 233 233 R -> L (in HP1; dbSNP:rs121908527).
{ECO:0000269|PubMed:15849466}.
/FTId=VAR_060560.
VARIANT 243 243 D -> H (in HP1; dbSNP:rs180177258).
{ECO:0000269|PubMed:15961946}.
/FTId=VAR_060561.
VARIANT 244 244 I -> T (in HP1; prevalent mutation in the
Canary islands; when associated with L-11
and M-340 on the minor AGXT allele;
results in protein misfolding; decreased
alanine--glyoxylate aminotransferase
activity; no loss of dimerization;
partial mitochondrial mistargeting;
dbSNP:rs121908525).
{ECO:0000269|PubMed:10541294,
ECO:0000269|PubMed:10862087,
ECO:0000269|PubMed:10960483,
ECO:0000269|PubMed:12777626,
ECO:0000269|PubMed:15849466,
ECO:0000269|PubMed:15961946,
ECO:0000269|PubMed:17495019,
ECO:0000269|PubMed:23229545,
ECO:0000269|PubMed:9192270}.
/FTId=VAR_008881.
VARIANT 253 253 C -> R (in HP1; when associated with L-11
and M-340 on the minor AGXT allele;
results in loss of alanine--glyoxylate
aminotransferase activity;
dbSNP:rs180177264).
{ECO:0000269|PubMed:15849466,
ECO:0000269|PubMed:17495019}.
/FTId=VAR_060562.
VARIANT 279 279 I -> M (in HP1; dbSNP:rs180177277).
{ECO:0000269|PubMed:15961946}.
/FTId=VAR_060563.
VARIANT 279 279 I -> T (in dbSNP:rs140992177).
{ECO:0000269|PubMed:15963748}.
/FTId=VAR_060564.
VARIANT 280 280 A -> V (in dbSNP:rs73106685).
{ECO:0000269|PubMed:15963748}.
/FTId=VAR_060565.
VARIANT 287 287 S -> T (in HP1; dbSNP:rs180177289).
{ECO:0000269|PubMed:15961946}.
/FTId=VAR_060566.
VARIANT 289 289 R -> C (in HP1; dbSNP:rs180177290).
{ECO:0000269|PubMed:10541294,
ECO:0000269|PubMed:15961946}.
/FTId=VAR_060567.
VARIANT 295 295 A -> T (in dbSNP:rs13408961).
/FTId=VAR_048237.
VARIANT 296 296 Missing (in HP1).
{ECO:0000269|PubMed:9604803}.
/FTId=VAR_060568.
VARIANT 298 298 L -> P (in HP1; dbSNP:rs180177293).
{ECO:0000269|PubMed:10541294,
ECO:0000269|PubMed:15961946}.
/FTId=VAR_060569.
VARIANT 326 326 V -> I (in dbSNP:rs115057148).
{ECO:0000269|PubMed:12559847}.
/FTId=VAR_060570.
VARIANT 336 336 V -> D (in HP1; dbSNP:rs180177155).
{ECO:0000269|PubMed:15253729}.
/FTId=VAR_060571.
VARIANT 340 340 I -> M (common polymorphism; associated
with hyperoxaluria; dbSNP:rs4426527).
{ECO:0000269|PubMed:1703535}.
/FTId=VAR_000593.
VARIANT 350 350 G -> D (in HP1; dbSNP:rs180177156).
{ECO:0000269|PubMed:9604803}.
/FTId=VAR_060572.
MUTAGEN 209 209 K->R: Affects pyridoxal phosphate
binding; loss of alanine--glyoxylate
aminotransferase activity.
{ECO:0000269|PubMed:10960483,
ECO:0000269|PubMed:16971151}.
HELIX 13 15 {ECO:0000244|PDB:5F9S}.
STRAND 27 29 {ECO:0000244|PDB:5F9S}.
HELIX 35 41 {ECO:0000244|PDB:5F9S}.
HELIX 51 68 {ECO:0000244|PDB:5F9S}.
STRAND 73 80 {ECO:0000244|PDB:5F9S}.
HELIX 82 93 {ECO:0000244|PDB:5F9S}.
STRAND 99 106 {ECO:0000244|PDB:5F9S}.
HELIX 107 118 {ECO:0000244|PDB:5F9S}.
STRAND 122 127 {ECO:0000244|PDB:5F9S}.
HELIX 136 146 {ECO:0000244|PDB:5F9S}.
STRAND 149 156 {ECO:0000244|PDB:5F9S}.
TURN 158 160 {ECO:0000244|PDB:5F9S}.
HELIX 169 175 {ECO:0000244|PDB:5F9S}.
STRAND 179 183 {ECO:0000244|PDB:5F9S}.
TURN 185 190 {ECO:0000244|PDB:5F9S}.
TURN 195 199 {ECO:0000244|PDB:5F9S}.
STRAND 201 209 {ECO:0000244|PDB:5F9S}.
STRAND 218 222 {ECO:0000244|PDB:5F9S}.
HELIX 224 231 {ECO:0000244|PDB:5F9S}.
HELIX 244 250 {ECO:0000244|PDB:5F9S}.
STRAND 254 256 {ECO:0000244|PDB:5F9S}.
HELIX 266 282 {ECO:0000244|PDB:5F9S}.
HELIX 284 304 {ECO:0000244|PDB:5F9S}.
STRAND 308 311 {ECO:0000244|PDB:5F9S}.
HELIX 314 316 {ECO:0000244|PDB:5F9S}.
STRAND 321 325 {ECO:0000244|PDB:5F9S}.
HELIX 332 343 {ECO:0000244|PDB:5F9S}.
STRAND 344 346 {ECO:0000244|PDB:4KYO}.
HELIX 352 354 {ECO:0000244|PDB:5F9S}.
TURN 355 357 {ECO:0000244|PDB:5F9S}.
STRAND 358 362 {ECO:0000244|PDB:5F9S}.
HELIX 365 367 {ECO:0000244|PDB:5F9S}.
HELIX 370 386 {ECO:0000244|PDB:5F9S}.
SEQUENCE 392 AA; 43010 MW; 2987DDE85B2470B4 CRC64;
MASHKLLVTP PKALLKPLSI PNQLLLGPGP SNLPPRIMAA GGLQMIGSMS KDMYQIMDEI
KEGIQYVFQT RNPLTLVISG SGHCALEAAL VNVLEPGDSF LVGANGIWGQ RAVDIGERIG
ARVHPMTKDP GGHYTLQEVE EGLAQHKPVL LFLTHGESST GVLQPLDGFG ELCHRYKCLL
LVDSVASLGG TPLYMDRQGI DILYSGSQKA LNAPPGTSLI SFSDKAKKKM YSRKTKPFSF
YLDIKWLANF WGCDDQPRMY HHTIPVISLY SLRESLALIA EQGLENSWRQ HREAAAYLHG
RLQALGLQLF VKDPALRLPT VTTVAVPAGY DWRDIVSYVI DHFDIEIMGG LGPSTGKVLR
IGLLGCNATR ENVDRVTEAL RAALQHCPKK KL


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