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2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain) (BCKDE1A) (BCKDH E1-alpha)

 ODBA_HUMAN              Reviewed;         445 AA.
P12694; B4DP47; E7EW46; Q16034; Q16472;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 2.
12-SEP-2018, entry version 215.
RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial;
EC=1.2.4.4;
AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain;
Short=BCKDE1A;
Short=BCKDH E1-alpha;
Flags: Precursor;
Name=BCKDHA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1420356; DOI=10.1016/0167-4781(92)90149-T;
McKean M.C., Winkeler K.A., Danner D.J.;
"Nucleotide sequence of the 5' end including the initiation codon of
cDNA for the E1 alpha subunit of the human branched chain alpha-
ketoacid dehydrogenase complex.";
Biochim. Biophys. Acta 1171:109-112(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow, and Lung;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-445 (ISOFORM 1).
PubMed=2914958;
Fisher C.W., Chuang J.L., Griffin T.A., Lau K.S., Cox R.P.,
Chuang D.T.;
"Molecular phenotypes in cultured maple syrup urine disease cells.
Complete E1 alpha cDNA sequence and mRNA and subunit contents of the
human branched chain alpha-keto acid dehydrogenase complex.";
J. Biol. Chem. 264:3448-3453(1989).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-445, AND VARIANT MSUD1A
ASN-438.
PubMed=2060625; DOI=10.1016/0014-5793(91)80755-R;
Dariush N., Fisher C.W., Cox R.P., Chuang D.T.;
"Structure of the gene encoding the entire mature E1 alpha subunit of
human branched-chain alpha-keto acid dehydrogenase complex.";
FEBS Lett. 284:34-38(1991).
[7]
ERRATUM.
PubMed=1682165; DOI=10.1016/0014-5793(91)81324-2;
Dariush N., Fisher C.W., Cox R.P., Chuang D.T.;
FEBS Lett. 291:376-377(1991).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 68-445 (ISOFORM 1).
TISSUE=Liver;
PubMed=3224821; DOI=10.1016/0378-1119(88)90390-3;
Zhang B., Crabb D.W., Harris R.A.;
"Nucleotide and deduced amino acid sequence of the E1 alpha subunit of
human liver branched-chain alpha-ketoacid dehydrogenase.";
Gene 69:159-164(1988).
[9]
PROTEIN SEQUENCE OF 46-57.
PubMed=7918575; DOI=10.1016/0304-4165(94)90161-9;
Wynn R.M., Kochi H., Cox R.P., Chuang D.T.;
"Differential processing of human and rat E1 alpha precursors of the
branched-chain alpha-keto acid dehydrogenase complex caused by an N-
terminal proline in the rat sequence.";
Biochim. Biophys. Acta 1201:125-128(1994).
[10]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 46-445 IN COMPLEX WITH
THIAMINE PYROPHOSPHATE AND POTASSIUM IONS, COFACTOR, AND SUBUNIT
STRUCTURE.
PubMed=10745006; DOI=10.1016/S0969-2126(00)00105-2;
Aevarsson A., Chuang J.L., Wynn R.M., Turley S., Chuang D.T.,
Hol W.G.J.;
"Crystal structure of human branched-chain alpha-ketoacid
dehydrogenase and the molecular basis of multienzyme complex
deficiency in maple syrup urine disease.";
Structure 8:277-291(2000).
[11]
VARIANT MSUD1A CYS-413.
PubMed=8037208;
Chuang J.L., Fisher C.R., Cox R.P., Chuang D.T.;
"Molecular basis of maple syrup urine disease: novel mutations at the
E1 alpha locus that impair E1(alpha 2 beta 2) assembly or decrease
steady-state E1 alpha mRNA levels of branched-chain alpha-keto acid
dehydrogenase complex.";
Am. J. Hum. Genet. 55:297-304(1994).
[12]
VARIANT MSUD1A ASN-438.
PubMed=2703538; DOI=10.1172/JCI114033;
Zhang B., Edenberg H.J., Crabb D.W., Harris R.A.;
"Evidence for both a regulatory mutation and a structural mutation in
a family with maple syrup urine disease.";
J. Clin. Invest. 83:1425-1429(1989).
[13]
VARIANT MSUD1A ASN-438.
PubMed=2241958; DOI=10.1016/0006-291X(90)90723-Z;
Matsuda I., Nobukuni Y., Mitsubuchi H., Indo Y., Endo F., Asaka J.,
Harada A.;
"A T-to-A substitution in the E1 alpha subunit gene of the branched-
chain alpha-ketoacid dehydrogenase complex in two cell lines derived
from Menonite maple syrup urine disease patients.";
Biochem. Biophys. Res. Commun. 172:646-651(1990).
[14]
VARIANT MSUD1A ASN-438.
PubMed=1867199;
Fisher C.R., Fisher C.W., Chuang D.T., Cox R.P.;
"Occurrence of a Tyr393-->Asn (Y393N) mutation in the E1 alpha gene of
the branched-chain alpha-keto acid dehydrogenase complex in maple
syrup urine disease patients from a Mennonite population.";
Am. J. Hum. Genet. 49:429-434(1991).
[15]
VARIANT MSUD1A ASN-438.
PubMed=1885764; DOI=10.1172/JCI115363;
Fisher C.R., Chuang J.L., Cox R.P., Fisher C.W., Star R.A.,
Chuang D.T.;
"Maple syrup urine disease in Mennonites. Evidence that the Y393N
mutation in E1 alpha impedes assembly of the E1 component of branched-
chain alpha-keto acid dehydrogenase complex.";
J. Clin. Invest. 88:1034-1037(1991).
[16]
VARIANTS MSUD1A TRP-159; LYS-190; THR-253 AND THR-326.
PubMed=8161368;
Nobukuni Y., Mitsubuchi H., Hayashida Y., Ohta K., Indo Y., Ichiba Y.,
Endo F., Matsuda I.;
"Heterogeneity of mutations in maple syrup urine disease (MSUD):
screening and identification of affected E1 alpha and E1 beta subunits
of the branched-chain alpha-keto-acid dehydrogenase multienzyme
complex.";
Biochim. Biophys. Acta 1225:64-70(1993).
[17]
VARIANTS MSUD1A ARG-290 AND CYS-409.
PubMed=7883996; DOI=10.1172/JCI117804;
Chuang J.L., Davie J.R., Chinsky J.M., Wynn R.M., Cox R.P.,
Chuang D.T.;
"Molecular and biochemical basis of intermediate maple syrup urine
disease: occurrence of homozygous G245R and F364C mutations at the E1-
alpha locus of Hispanic-Mexican patients.";
J. Clin. Invest. 95:954-963(1995).
[18]
VARIANTS MSUD1A MET-211; VAL-220; CYS-346; LYS-PRO-403 INS AND
427-LEU-ALA-428 DELINS PRO.
PubMed=21844576;
Park H.D., Lee D.H., Hong Y.H., Kang D.H., Lee Y.K., Song J.,
Lee S.Y., Kim J.W., Ki C.S., Lee Y.W.;
"Three Korean patients with maple syrup urine disease: four novel
mutations in the BCKDHA gene.";
Ann. Clin. Lab. Sci. 41:167-173(2011).
-!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex
catalyzes the overall conversion of alpha-keto acids to acyl-CoA
and CO(2). It contains multiple copies of three enzymatic
components: branched-chain alpha-keto acid decarboxylase (E1),
lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
-!- CATALYTIC ACTIVITY: 3-methyl-2-oxobutanoate +
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]
lipoyllysine = [dihydrolipoyllysine-residue (2-
methylpropanoyl)transferase] S-(2-
methylpropanoyl)dihydrolipoyllysine + CO(2).
-!- COFACTOR:
Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
Evidence={ECO:0000269|PubMed:10745006};
-!- SUBUNIT: Heterotetramer of alpha and beta chains.
{ECO:0000269|PubMed:10745006}.
-!- INTERACTION:
P21953:BCKDHB; NbExp=13; IntAct=EBI-1029053, EBI-1029067;
P21953-1:BCKDHB; NbExp=3; IntAct=EBI-15489562, EBI-15489569;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P12694-1; Sequence=Displayed;
Name=2;
IsoId=P12694-2; Sequence=VSP_056156, VSP_056157;
Note=No experimental confirmation available.;
-!- DISEASE: Maple syrup urine disease 1A (MSUD1A) [MIM:248600]: A
metabolic disorder due to an enzyme defect in the catabolic
pathway of the branched-chain amino acids leucine, isoleucine, and
valine. Accumulation of these 3 amino acids and their
corresponding keto acids leads to encephalopathy and progressive
neurodegeneration. Clinical features include mental and physical
retardation, feeding problems, and a maple syrup odor to the
urine. The keto acids of the branched-chain amino acids are
present in the urine. If untreated, maple syrup urine disease can
lead to seizures, coma, and death. The disease is often classified
by its pattern of signs and symptoms. The most common and severe
form of the disease is the classic type, which becomes apparent
soon after birth. Variant forms of the disorder become apparent
later in infancy or childhood and are typically milder, but they
still involve developmental delay and other medical problems if
not treated. {ECO:0000269|PubMed:1867199,
ECO:0000269|PubMed:1885764, ECO:0000269|PubMed:2060625,
ECO:0000269|PubMed:21844576, ECO:0000269|PubMed:2241958,
ECO:0000269|PubMed:2703538, ECO:0000269|PubMed:7883996,
ECO:0000269|PubMed:8037208, ECO:0000269|PubMed:8161368}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- MISCELLANEOUS: Bound potassium ions stabilize the protein
structure.
-!- SIMILARITY: Belongs to the BCKDHA family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB59549.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; Z14093; CAA78475.1; -; mRNA.
EMBL; AK298188; BAG60459.1; -; mRNA.
EMBL; AC011462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007878; AAH07878.1; -; mRNA.
EMBL; BC008933; AAH08933.1; -; mRNA.
EMBL; BC023983; AAH23983.1; -; mRNA.
EMBL; J04474; AAB59549.1; ALT_INIT; mRNA.
EMBL; AH003771; AAB20222.2; -; Genomic_DNA.
EMBL; AH003707; AAB19268.2; -; Genomic_DNA.
EMBL; M22221; AAA35590.1; -; mRNA.
CCDS; CCDS12581.1; -. [P12694-1]
PIR; S27156; DEHUXA.
RefSeq; NP_000700.1; NM_000709.3. [P12694-1]
RefSeq; NP_001158255.1; NM_001164783.1.
UniGene; Hs.433307; -.
PDB; 1DTW; X-ray; 2.70 A; A=46-445.
PDB; 1OLS; X-ray; 1.85 A; A=46-445.
PDB; 1OLU; X-ray; 1.90 A; A=46-445.
PDB; 1OLX; X-ray; 2.25 A; A=46-445.
PDB; 1U5B; X-ray; 1.83 A; A=46-445.
PDB; 1V11; X-ray; 1.95 A; A=46-445.
PDB; 1V16; X-ray; 1.90 A; A=46-445.
PDB; 1V1M; X-ray; 2.00 A; A=46-445.
PDB; 1V1R; X-ray; 1.80 A; A=46-445.
PDB; 1WCI; X-ray; 1.84 A; A=46-445.
PDB; 1X7W; X-ray; 1.73 A; A=46-445.
PDB; 1X7X; X-ray; 2.10 A; A=46-445.
PDB; 1X7Y; X-ray; 1.57 A; A=46-445.
PDB; 1X7Z; X-ray; 1.72 A; A=46-445.
PDB; 1X80; X-ray; 2.00 A; A=46-445.
PDB; 2BEU; X-ray; 1.89 A; A=46-445.
PDB; 2BEV; X-ray; 1.80 A; A=46-445.
PDB; 2BEW; X-ray; 1.79 A; A=46-445.
PDB; 2BFB; X-ray; 1.77 A; A=46-445.
PDB; 2BFC; X-ray; 1.64 A; A=46-445.
PDB; 2BFD; X-ray; 1.39 A; A=46-445.
PDB; 2BFE; X-ray; 1.69 A; A=46-445.
PDB; 2BFF; X-ray; 1.46 A; A=46-445.
PDB; 2J9F; X-ray; 1.88 A; A/C=46-445.
PDBsum; 1DTW; -.
PDBsum; 1OLS; -.
PDBsum; 1OLU; -.
PDBsum; 1OLX; -.
PDBsum; 1U5B; -.
PDBsum; 1V11; -.
PDBsum; 1V16; -.
PDBsum; 1V1M; -.
PDBsum; 1V1R; -.
PDBsum; 1WCI; -.
PDBsum; 1X7W; -.
PDBsum; 1X7X; -.
PDBsum; 1X7Y; -.
PDBsum; 1X7Z; -.
PDBsum; 1X80; -.
PDBsum; 2BEU; -.
PDBsum; 2BEV; -.
PDBsum; 2BEW; -.
PDBsum; 2BFB; -.
PDBsum; 2BFC; -.
PDBsum; 2BFD; -.
PDBsum; 2BFE; -.
PDBsum; 2BFF; -.
PDBsum; 2J9F; -.
ProteinModelPortal; P12694; -.
SMR; P12694; -.
BioGrid; 107065; 29.
DIP; DIP-6146N; -.
IntAct; P12694; 14.
STRING; 9606.ENSP00000269980; -.
iPTMnet; P12694; -.
PhosphoSitePlus; P12694; -.
BioMuta; BCKDHA; -.
EPD; P12694; -.
MaxQB; P12694; -.
PaxDb; P12694; -.
PeptideAtlas; P12694; -.
PRIDE; P12694; -.
ProteomicsDB; 52863; -.
Ensembl; ENST00000269980; ENSP00000269980; ENSG00000248098. [P12694-1]
Ensembl; ENST00000457836; ENSP00000416000; ENSG00000248098. [P12694-2]
GeneID; 593; -.
KEGG; hsa:593; -.
UCSC; uc002oqq.4; human. [P12694-1]
CTD; 593; -.
DisGeNET; 593; -.
EuPathDB; HostDB:ENSG00000248098.10; -.
GeneCards; BCKDHA; -.
GeneReviews; BCKDHA; -.
HGNC; HGNC:986; BCKDHA.
HPA; HPA036640; -.
MalaCards; BCKDHA; -.
MIM; 248600; phenotype.
MIM; 608348; gene.
neXtProt; NX_P12694; -.
OpenTargets; ENSG00000248098; -.
Orphanet; 268145; Classic maple syrup urine disease.
Orphanet; 268162; Intermediate maple syrup urine disease.
Orphanet; 268173; Intermittent maple syrup urine disease.
Orphanet; 268184; Thiamine-responsive maple syrup urine disease.
PharmGKB; PA25297; -.
eggNOG; KOG1182; Eukaryota.
eggNOG; COG1071; LUCA.
GeneTree; ENSGT00530000063174; -.
HOGENOM; HOG000281337; -.
HOVERGEN; HBG002459; -.
InParanoid; P12694; -.
KO; K00166; -.
OrthoDB; EOG091G073F; -.
PhylomeDB; P12694; -.
TreeFam; TF300863; -.
BioCyc; MetaCyc:MONOMER-12005; -.
Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
SABIO-RK; P12694; -.
SIGNOR; P12694; -.
ChiTaRS; BCKDHA; human.
EvolutionaryTrace; P12694; -.
GeneWiki; BCKDHA; -.
GenomeRNAi; 593; -.
PRO; PR:P12694; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000248098; Expressed in 91 organ(s), highest expression level in heart.
CleanEx; HS_BCKDHA; -.
ExpressionAtlas; P12694; baseline and differential.
Genevisible; P12694; HS.
GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IDA:HGNC.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; TAS:ProtInc.
GO; GO:0003826; F:alpha-ketoacid dehydrogenase activity; IDA:HGNC.
GO; GO:0016831; F:carboxy-lyase activity; TAS:HGNC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009083; P:branched-chain amino acid catabolic process; IDA:HGNC.
InterPro; IPR034616; BCKDH_E1-a.
InterPro; IPR001017; DH_E1.
InterPro; IPR029061; THDP-binding.
PANTHER; PTHR43380:SF1; PTHR43380:SF1; 1.
Pfam; PF00676; E1_dh; 1.
SUPFAM; SSF52518; SSF52518; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation;
Maple syrup urine disease; Metal-binding; Mitochondrion;
Oxidoreductase; Phosphoprotein; Polymorphism; Potassium;
Reference proteome; Thiamine pyrophosphate; Transit peptide.
TRANSIT 1 45 Mitochondrion.
{ECO:0000269|PubMed:7918575}.
CHAIN 46 445 2-oxoisovalerate dehydrogenase subunit
alpha, mitochondrial.
/FTId=PRO_0000020465.
REGION 157 159 Thiamine pyrophosphate binding.
{ECO:0000269|PubMed:10745006}.
METAL 206 206 Potassium. {ECO:0000269|PubMed:10745006}.
METAL 211 211 Potassium. {ECO:0000269|PubMed:10745006}.
METAL 212 212 Potassium. {ECO:0000269|PubMed:10745006}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000250|UniProtKB:P50136}.
MOD_RES 338 338 Phosphothreonine.
{ECO:0000250|UniProtKB:P50136}.
MOD_RES 339 339 Phosphoserine.
{ECO:0000250|UniProtKB:P50136}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000250|UniProtKB:P50136}.
MOD_RES 356 356 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P50136}.
MOD_RES 356 356 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P50136}.
MOD_RES 380 380 N6-succinyllysine.
{ECO:0000250|UniProtKB:P50136}.
VAR_SEQ 19 40 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056156.
VAR_SEQ 331 331 Y -> YSSSPILPPDPHSREPTLTWGPLPLC (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056157.
VARIANT 39 39 P -> H (in dbSNP:rs11549936).
/FTId=VAR_034360.
VARIANT 151 151 T -> M (in dbSNP:rs34442879).
/FTId=VAR_034361.
VARIANT 159 159 R -> W (in MSUD1A; dbSNP:rs769688327).
{ECO:0000269|PubMed:8161368}.
/FTId=VAR_004968.
VARIANT 190 190 Q -> K (in MSUD1A).
{ECO:0000269|PubMed:8161368}.
/FTId=VAR_004969.
VARIANT 211 211 T -> M (in MSUD1A; dbSNP:rs398123503).
{ECO:0000269|PubMed:21844576}.
/FTId=VAR_069748.
VARIANT 220 220 A -> V (in MSUD1A; dbSNP:rs375785084).
{ECO:0000269|PubMed:21844576}.
/FTId=VAR_069749.
VARIANT 253 253 A -> T (in MSUD1A; dbSNP:rs199599175).
{ECO:0000269|PubMed:8161368}.
/FTId=VAR_004970.
VARIANT 290 290 G -> R (in MSUD1A; dbSNP:rs137852871).
{ECO:0000269|PubMed:7883996}.
/FTId=VAR_015101.
VARIANT 326 326 I -> T (in MSUD1A).
{ECO:0000269|PubMed:8161368}.
/FTId=VAR_004971.
VARIANT 346 346 R -> C (in MSUD1A; dbSNP:rs182923857).
{ECO:0000269|PubMed:21844576}.
/FTId=VAR_069750.
VARIANT 403 403 P -> PKP (in MSUD1A).
/FTId=VAR_069751.
VARIANT 409 409 F -> C (in MSUD1A; dbSNP:rs137852872).
{ECO:0000269|PubMed:7883996}.
/FTId=VAR_015102.
VARIANT 413 413 Y -> C (in MSUD1A).
{ECO:0000269|PubMed:8037208}.
/FTId=VAR_004972.
VARIANT 427 428 LA -> P (in MSUD1A).
{ECO:0000269|PubMed:21844576}.
/FTId=VAR_069752.
VARIANT 438 438 Y -> N (in MSUD1A; impedes assembly of
the E1 component; dbSNP:rs137852870).
{ECO:0000269|PubMed:1867199,
ECO:0000269|PubMed:1885764,
ECO:0000269|PubMed:2060625,
ECO:0000269|PubMed:2241958,
ECO:0000269|PubMed:2703538}.
/FTId=VAR_004973.
CONFLICT 3 3 V -> G (in Ref. 6; AAB20222/AAB19268).
{ECO:0000305}.
CONFLICT 36 36 S -> A (in Ref. 5; AAB59549).
{ECO:0000305}.
CONFLICT 248 248 A -> D (in Ref. 8; AAA35590).
{ECO:0000305}.
STRAND 61 64 {ECO:0000244|PDB:2J9F}.
STRAND 88 90 {ECO:0000244|PDB:1DTW}.
HELIX 91 93 {ECO:0000244|PDB:2BFD}.
HELIX 99 124 {ECO:0000244|PDB:2BFD}.
STRAND 127 129 {ECO:0000244|PDB:2BFD}.
TURN 135 137 {ECO:0000244|PDB:2BFB}.
HELIX 138 146 {ECO:0000244|PDB:2BFD}.
STRAND 152 155 {ECO:0000244|PDB:2BFD}.
HELIX 161 166 {ECO:0000244|PDB:2BFD}.
HELIX 171 179 {ECO:0000244|PDB:2BFD}.
TURN 185 188 {ECO:0000244|PDB:2BFD}.
TURN 198 201 {ECO:0000244|PDB:2BFD}.
TURN 209 211 {ECO:0000244|PDB:2BFD}.
HELIX 212 226 {ECO:0000244|PDB:2BFD}.
STRAND 232 237 {ECO:0000244|PDB:2BFD}.
HELIX 240 242 {ECO:0000244|PDB:2BFD}.
HELIX 244 255 {ECO:0000244|PDB:2BFD}.
STRAND 260 266 {ECO:0000244|PDB:2BFD}.
STRAND 268 270 {ECO:0000244|PDB:2BFD}.
HELIX 275 277 {ECO:0000244|PDB:2BFD}.
STRAND 280 282 {ECO:0000244|PDB:2BFD}.
HELIX 285 287 {ECO:0000244|PDB:2BFD}.
HELIX 289 291 {ECO:0000244|PDB:2BFD}.
STRAND 294 299 {ECO:0000244|PDB:2BFD}.
HELIX 303 320 {ECO:0000244|PDB:2BFD}.
STRAND 324 329 {ECO:0000244|PDB:2BFD}.
HELIX 342 344 {ECO:0000244|PDB:2BFF}.
HELIX 351 357 {ECO:0000244|PDB:2BFF}.
HELIX 360 368 {ECO:0000244|PDB:2BFD}.
TURN 369 372 {ECO:0000244|PDB:2BFD}.
HELIX 376 399 {ECO:0000244|PDB:2BFD}.
HELIX 405 408 {ECO:0000244|PDB:2BFD}.
TURN 409 411 {ECO:0000244|PDB:2BEW}.
STRAND 412 415 {ECO:0000244|PDB:2BFD}.
HELIX 418 434 {ECO:0000244|PDB:2BFD}.
HELIX 435 437 {ECO:0000244|PDB:2BFD}.
HELIX 440 442 {ECO:0000244|PDB:2BFD}.
SEQUENCE 445 AA; 50471 MW; 2B4DD658924DB0C3 CRC64;
MAVAIAAARV WRLNRGLSQA ALLLLRQPGA RGLARSHPPR QQQQFSSLDD KPQFPGASAE
FIDKLEFIQP NVISGIPIYR VMDRQGQIIN PSEDPHLPKE KVLKLYKSMT LLNTMDRILY
ESQRQGRISF YMTNYGEEGT HVGSAAALDN TDLVFGQYRE AGVLMYRDYP LELFMAQCYG
NISDLGKGRQ MPVHYGCKER HFVTISSPLA TQIPQAVGAA YAAKRANANR VVICYFGEGA
ASEGDAHAGF NFAATLECPI IFFCRNNGYA ISTPTSEQYR GDGIAARGPG YGIMSIRVDG
NDVFAVYNAT KEARRRAVAE NQPFLIEAMT YRIGHHSTSD DSSAYRSVDE VNYWDKQDHP
ISRLRHYLLS QGWWDEEQEK AWRKQSRRKV MEAFEQAERK PKPNPNLLFS DVYQEMPAQL
RKQQESLARH LQTYGEHYPL DHFDK


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