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Bifunctional dethiobiotin synthetase/7,8-diamino-pelargonic acid aminotransferase, mitochondrial (Bifunctional BIO3-BIO1 protein) [Includes: Dethiobiotin synthetase (EC 6.3.3.3) (DTB synthetase) (DTBS) (Protein BIOTIN AUXOTROPH 3); 7,8-diamino-pelargonic acid aminotransferase (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Adenosylmethionine-8-amino-7-oxononanoate aminotransferase) (EC 2.6.1.62) (Diaminopelargonic acid synthase) (Protein BIOTIN AUXOTROPH 1)]

 BIODA_ARATH             Reviewed;         833 AA.
B0F481; B0F482; Q681L5; Q6NQL9; Q9FKL4; Q9FKL5;
13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 1.
25-APR-2018, entry version 82.
RecName: Full=Bifunctional dethiobiotin synthetase/7,8-diamino-pelargonic acid aminotransferase, mitochondrial;
AltName: Full=Bifunctional BIO3-BIO1 protein;
Includes:
RecName: Full=Dethiobiotin synthetase;
EC=6.3.3.3;
AltName: Full=DTB synthetase;
Short=DTBS;
AltName: Full=Protein BIOTIN AUXOTROPH 3;
Includes:
RecName: Full=7,8-diamino-pelargonic acid aminotransferase;
Short=DAPA AT;
Short=DAPA aminotransferase;
AltName: Full=7,8-diaminononanoate synthase;
Short=DANS;
AltName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase;
EC=2.6.1.62;
AltName: Full=Diaminopelargonic acid synthase;
AltName: Full=Protein BIOTIN AUXOTROPH 1;
Flags: Precursor;
Name=BIO3-BIO1; Synonyms=BIO1, BIO3;
OrderedLocusNames=At5g57590/At5g57600; ORFNames=MUA2.17/MUA2.18;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE
SPLICING, FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=17993549; DOI=10.1104/pp.107.107409;
Muralla R., Chen E., Sweeney C., Gray J.A., Dickerman A.,
Nikolau B.J., Meinke D.;
"A bifunctional locus (BIO3-BIO1) required for biotin biosynthesis in
Arabidopsis.";
Plant Physiol. 146:60-73(2008).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
STRAIN=cv. Columbia;
Alban C., Pinon V.;
"Arabidopsis thaliana 7,8-diaminopelargonic acid aminotransferase
(AtbioA) mRNA.";
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
STRAIN=cv. Columbia;
Alban C., Pautre V.;
"cDNA sequences for BIO3-BIO1 from Arabidopsis.";
Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9679202; DOI=10.1093/dnares/5.2.131;
Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
features of the regions of 1,381,565 bp covered by twenty one
physically assigned P1 and TAC clones.";
DNA Res. 5:131-145(1998).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, AND MUTAGENESIS OF 777-TYR--THR-833.
PubMed=2909401; DOI=10.1016/S0012-1606(89)80047-8;
Schneider T., Dinkins R., Robinson K., Shellhammer J., Meinke D.W.;
"An embryo-lethal mutant of Arabidopsis thaliana is a biotin
auxotroph.";
Dev. Biol. 131:161-167(1989).
[9]
FUNCTION.
PubMed=16667573; DOI=10.1104/pp.93.3.1162;
Shellhammer J., Meinke D.;
"Arrested embryos from the bio1 auxotroph of Arabidopsis thaliana
contain reduced levels of biotin.";
Plant Physiol. 93:1162-1167(1990).
[10]
FUNCTION.
PubMed=8676868; DOI=10.1007/BF02172516;
Patton D.A., Volrath S., Ward E.R.;
"Complementation of an Arabidopsis thaliana biotin auxotroph with an
Escherichia coli biotin biosynthetic gene.";
Mol. Gen. Genet. 251:261-266(1996).
-!- FUNCTION: Bifunctional enzyme that catalyzes two different
reactions involved in the biotin biosynthesis.
-!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-
dependent insertion of CO2 between the N7 and N8 nitrogen atoms of
7,8-diaminopelargonic acid (DAPA) to form an ureido ring.
{ECO:0000250, ECO:0000269|PubMed:16667573,
ECO:0000269|PubMed:17993549, ECO:0000269|PubMed:2909401,
ECO:0000269|PubMed:8676868}.
-!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S-
adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid
(KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only
animotransferase known to utilize SAM as an amino donor.
-!- CATALYTIC ACTIVITY: ATP + 7,8-diaminononanoate + CO(2) = ADP +
phosphate + dethiobiotin.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7-
oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-
diaminononanoate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250};
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
7,8-diaminononanoate: step 1/2.
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
1/1.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=BIO3-BIO1;
IsoId=B0F481-1; Sequence=Displayed;
Name=2; Synonyms=BIO3 long;
IsoId=B0F481-2; Sequence=VSP_043888, VSP_043889;
Note=May be due to a competing acceptor splice site.;
Name=3; Synonyms=BIO1 short;
IsoId=B0F481-3; Sequence=VSP_043884, VSP_043887;
Note=May be due to a competing acceptor splice site.;
Name=4; Synonyms=BIO3 short;
IsoId=B0F481-4; Sequence=VSP_043886;
Note=May be due to an intron retention.;
Name=5; Synonyms=BIO1 long;
IsoId=B0F481-5; Sequence=VSP_043885;
-!- DISRUPTION PHENOTYPE: Arrested embryos at the transition to
cotyledon stages of development. {ECO:0000269|PubMed:17993549}.
-!- SIMILARITY: In the N-terminal section; belongs to the dethiobiotin
synthetase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the class-III
pyridoxal-phosphate-dependent aminotransferase family. BioA
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB08794.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g57590 and At5g57600.; Evidence={ECO:0000305};
Sequence=BAB08795.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g57590 and At5g57600.; Evidence={ECO:0000305};
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EMBL; EU089963; ABW80569.1; -; mRNA.
EMBL; EU090805; ABU50828.1; -; mRNA.
EMBL; EU090805; ABU50829.1; -; mRNA.
EMBL; EF081156; ABN80998.1; -; mRNA.
EMBL; HQ857557; AEW48251.1; -; mRNA.
EMBL; HQ857558; AEW48252.1; -; mRNA.
EMBL; AB011482; BAB08794.1; ALT_SEQ; Genomic_DNA.
EMBL; AB011482; BAB08795.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED96924.1; -; Genomic_DNA.
EMBL; BT010433; AAQ62434.1; -; mRNA.
EMBL; AK175602; BAD43365.1; -; mRNA.
RefSeq; NP_200567.2; NM_125140.4. [B0F481-1]
UniGene; At.29327; -.
PDB; 4A0F; X-ray; 2.71 A; A/B=23-833.
PDB; 4A0G; X-ray; 2.50 A; A/B/C/D=23-833.
PDB; 4A0H; X-ray; 2.81 A; A/B=23-833.
PDB; 4A0R; X-ray; 2.68 A; A/B=23-833.
PDBsum; 4A0F; -.
PDBsum; 4A0G; -.
PDBsum; 4A0H; -.
PDBsum; 4A0R; -.
ProteinModelPortal; B0F481; -.
SMR; B0F481; -.
STRING; 3702.AT5G57590.1; -.
PaxDb; B0F481; -.
PRIDE; B0F481; -.
EnsemblPlants; AT5G57590.1; AT5G57590.1; AT5G57590. [B0F481-1]
GeneID; 835863; -.
Gramene; AT5G57590.1; AT5G57590.1; AT5G57590. [B0F481-1]
KEGG; ath:AT5G57590; -.
Araport; AT5G57590; -.
TAIR; locus:2174532; AT5G57590.
eggNOG; ENOG410IPFW; Eukaryota.
eggNOG; COG0161; LUCA.
HOGENOM; HOG000201750; -.
InParanoid; B0F481; -.
KO; K19562; -.
OMA; KVEWYRG; -.
OrthoDB; EOG09360C74; -.
PhylomeDB; B0F481; -.
BioCyc; MetaCyc:MONOMER-8566; -.
BRENDA; 2.6.1.62; 399.
BRENDA; 6.3.3.3; 399.
UniPathway; UPA00078; UER00160.
UniPathway; UPA00078; UER00161.
PRO; PR:B0F481; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; B0F481; baseline and differential.
Genevisible; B0F481; AT.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004141; F:dethiobiotin synthase activity; IDA:TAIR.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0009102; P:biotin biosynthetic process; IDA:TAIR.
Gene3D; 3.40.640.10; -; 1.
HAMAP; MF_00336; BioD; 1.
InterPro; IPR005814; Aminotrans_3.
InterPro; IPR004472; DTB_synth_BioD.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
Pfam; PF00202; Aminotran_3; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53383; SSF53383; 2.
PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Aminotransferase; ATP-binding;
Biotin biosynthesis; Complete proteome; Ligase; Magnesium;
Metal-binding; Mitochondrion; Multifunctional enzyme;
Nucleotide-binding; Pyridoxal phosphate; Reference proteome;
S-adenosyl-L-methionine; Transferase; Transit peptide.
TRANSIT 1 23 Mitochondrion. {ECO:0000255}.
CHAIN 24 833 Bifunctional dethiobiotin synthetase/7,8-
diamino-pelargonic acid aminotransferase,
mitochondrial.
/FTId=PRO_0000417696.
NP_BIND 47 52 ATP. {ECO:0000250}.
NP_BIND 210 213 ATP. {ECO:0000250}.
REGION 36 299 Dethiobiotin synthetase.
REGION 332 830 7,8-diamino-pelargonic acid
aminotransferase.
REGION 391 392 7-keto-8-aminopelargonic acid binding.
{ECO:0000250}.
REGION 453 454 Pyridoxal phosphate binding.
{ECO:0000250}.
METAL 51 51 Magnesium. {ECO:0000250}.
METAL 97 97 Magnesium. {ECO:0000250}.
METAL 210 210 Magnesium. {ECO:0000250}.
BINDING 81 81 Substrate. {ECO:0000250}.
BINDING 97 97 ATP. {ECO:0000250}.
BINDING 495 495 7-keto-8-aminopelargonic acid.
{ECO:0000250}.
BINDING 637 637 Pyridoxal phosphate. {ECO:0000250}.
BINDING 666 666 7-keto-8-aminopelargonic acid.
{ECO:0000250}.
BINDING 700 700 7-keto-8-aminopelargonic acid; via
carbonyl oxygen. {ECO:0000250}.
BINDING 702 702 Pyridoxal phosphate. {ECO:0000250}.
BINDING 797 797 7-keto-8-aminopelargonic acid.
{ECO:0000250}.
SITE 348 348 Participates in the substrate recognition
with KAPA and in a stacking interaction
with the adenine ring of SAM.
{ECO:0000250}.
MOD_RES 666 666 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
VAR_SEQ 1 382 Missing (in isoform 3).
{ECO:0000303|PubMed:17993549,
ECO:0000303|Ref.2, ECO:0000303|Ref.7}.
/FTId=VSP_043884.
VAR_SEQ 1 321 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_043885.
VAR_SEQ 288 833 Missing (in isoform 4).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_043886.
VAR_SEQ 383 399 QQFDACASWWTQGPDPT -> MLVQAGGHRGQILLSRL
(in isoform 3).
{ECO:0000303|PubMed:17993549,
ECO:0000303|Ref.2, ECO:0000303|Ref.7}.
/FTId=VSP_043887.
VAR_SEQ 403 405 ELA -> VSG (in isoform 2).
{ECO:0000303|PubMed:17993549,
ECO:0000303|Ref.3}.
/FTId=VSP_043888.
VAR_SEQ 406 833 Missing (in isoform 2).
{ECO:0000303|PubMed:17993549,
ECO:0000303|Ref.3}.
/FTId=VSP_043889.
MUTAGEN 777 833 Missing: In bio1-1: Arrested embryo.
{ECO:0000269|PubMed:2909401}.
CONFLICT 236 236 G -> E (in Ref. 6; AAQ62434).
{ECO:0000305}.
STRAND 31 33 {ECO:0000244|PDB:4A0G}.
STRAND 38 48 {ECO:0000244|PDB:4A0G}.
HELIX 50 62 {ECO:0000244|PDB:4A0G}.
STRAND 72 80 {ECO:0000244|PDB:4A0G}.
TURN 83 85 {ECO:0000244|PDB:4A0G}.
HELIX 88 103 {ECO:0000244|PDB:4A0G}.
STRAND 108 117 {ECO:0000244|PDB:4A0G}.
HELIX 118 124 {ECO:0000244|PDB:4A0G}.
STRAND 134 144 {ECO:0000244|PDB:4A0G}.
STRAND 151 159 {ECO:0000244|PDB:4A0G}.
STRAND 161 164 {ECO:0000244|PDB:4A0G}.
HELIX 166 172 {ECO:0000244|PDB:4A0G}.
HELIX 179 193 {ECO:0000244|PDB:4A0G}.
STRAND 205 210 {ECO:0000244|PDB:4A0G}.
STRAND 212 214 {ECO:0000244|PDB:4A0F}.
HELIX 225 228 {ECO:0000244|PDB:4A0G}.
HELIX 230 232 {ECO:0000244|PDB:4A0G}.
STRAND 236 239 {ECO:0000244|PDB:4A0G}.
STRAND 243 245 {ECO:0000244|PDB:4A0F}.
HELIX 246 258 {ECO:0000244|PDB:4A0G}.
TURN 259 261 {ECO:0000244|PDB:4A0G}.
STRAND 264 270 {ECO:0000244|PDB:4A0G}.
HELIX 277 283 {ECO:0000244|PDB:4A0G}.
TURN 284 286 {ECO:0000244|PDB:4A0G}.
STRAND 290 293 {ECO:0000244|PDB:4A0G}.
HELIX 305 310 {ECO:0000244|PDB:4A0G}.
HELIX 312 343 {ECO:0000244|PDB:4A0G}.
HELIX 351 353 {ECO:0000244|PDB:4A0G}.
HELIX 356 358 {ECO:0000244|PDB:4A0G}.
STRAND 360 366 {ECO:0000244|PDB:4A0G}.
STRAND 369 374 {ECO:0000244|PDB:4A0G}.
HELIX 375 378 {ECO:0000244|PDB:4A0G}.
STRAND 379 386 {ECO:0000244|PDB:4A0G}.
HELIX 389 392 {ECO:0000244|PDB:4A0G}.
HELIX 398 415 {ECO:0000244|PDB:4A0G}.
HELIX 426 437 {ECO:0000244|PDB:4A0G}.
TURN 438 443 {ECO:0000244|PDB:4A0G}.
STRAND 446 452 {ECO:0000244|PDB:4A0G}.
HELIX 453 470 {ECO:0000244|PDB:4A0G}.
TURN 471 473 {ECO:0000244|PDB:4A0G}.
STRAND 486 491 {ECO:0000244|PDB:4A0G}.
HELIX 500 504 {ECO:0000244|PDB:4A0G}.
HELIX 510 512 {ECO:0000244|PDB:4A0G}.
TURN 514 516 {ECO:0000244|PDB:4A0G}.
STRAND 524 527 {ECO:0000244|PDB:4A0G}.
STRAND 531 535 {ECO:0000244|PDB:4A0G}.
STRAND 538 542 {ECO:0000244|PDB:4A0G}.
STRAND 556 558 {ECO:0000244|PDB:4A0G}.
HELIX 560 564 {ECO:0000244|PDB:4A0G}.
HELIX 566 570 {ECO:0000244|PDB:4A0G}.
HELIX 572 584 {ECO:0000244|PDB:4A0G}.
STRAND 596 602 {ECO:0000244|PDB:4A0G}.
STRAND 605 607 {ECO:0000244|PDB:4A0G}.
TURN 608 611 {ECO:0000244|PDB:4A0G}.
STRAND 612 615 {ECO:0000244|PDB:4A0G}.
HELIX 617 629 {ECO:0000244|PDB:4A0G}.
STRAND 634 637 {ECO:0000244|PDB:4A0G}.
TURN 639 646 {ECO:0000244|PDB:4A0G}.
STRAND 647 650 {ECO:0000244|PDB:4A0G}.
HELIX 652 655 {ECO:0000244|PDB:4A0G}.
STRAND 660 664 {ECO:0000244|PDB:4A0G}.
HELIX 666 669 {ECO:0000244|PDB:4A0G}.
STRAND 676 680 {ECO:0000244|PDB:4A0G}.
HELIX 682 686 {ECO:0000244|PDB:4A0G}.
STRAND 690 692 {ECO:0000244|PDB:4A0R}.
HELIX 693 695 {ECO:0000244|PDB:4A0G}.
TURN 702 705 {ECO:0000244|PDB:4A0G}.
HELIX 707 721 {ECO:0000244|PDB:4A0G}.
TURN 723 725 {ECO:0000244|PDB:4A0G}.
STRAND 733 736 {ECO:0000244|PDB:4A0G}.
HELIX 742 750 {ECO:0000244|PDB:4A0G}.
STRAND 751 753 {ECO:0000244|PDB:4A0F}.
STRAND 754 760 {ECO:0000244|PDB:4A0G}.
STRAND 763 768 {ECO:0000244|PDB:4A0G}.
HELIX 780 791 {ECO:0000244|PDB:4A0G}.
STRAND 802 806 {ECO:0000244|PDB:4A0G}.
HELIX 813 827 {ECO:0000244|PDB:4A0G}.
TURN 828 830 {ECO:0000244|PDB:4A0G}.
SEQUENCE 833 AA; 91935 MW; 87A5D5C624E19649 CRC64;
MIPVTATLIR HRLRHLRHRI RFKSTSVSPF HLPLNHPTYL IWSANTSLGK TLVSTGIAAS
FLLQQPSSSA TKLLYLKPIQ TGFPSDSDSR FVFSKLDSLS LRRQIPISIS NSVLHSSLPA
AKSLGLNVEV SESGMCSLNF RDEKTVTGAP ELLCKTLYAW EAAISPHLAA ERENATVEDS
VVLQMIEKCL KEEMECGVKS EKSDLLCLVE TAGGVASPGP SGTLQCDLYR PFRLPGILVG
DGRLGGISGT IAAYESLKLR GYDIAAVVFE DHGLVNEVPL TSYLRNKVPV LVLPPVPKDP
SDDLIEWFVE SDGVFKALKE TMVLANLERL ERLNGMAKLA GEVFWWPFTQ HKLVHQETVT
VIDSRCGENF SIYKASDNSS LSQQFDACAS WWTQGPDPTF QAELAREMGY TAARFGHVMF
PENVYEPALK CAELLLDGVG KGWASRVYFS DNGSTAIEIA LKMAFRKFCV DHNFCEATEE
EKHIVVKVIA LRGSYHGDTL GAMEAQAPSP YTGFLQQPWY TGRGLFLDPP TVFLSNGSWN
ISLPESFSEI APEYGTFTSR DEIFDKSRDA STLARIYSAY LSKHLQEHSG VRQSAHVGAL
IIEPVIHGAG GMHMVDPLFQ RVLVNECRNR KIPVIFDEVF TGFWRLGVET TTELLGCKPD
IACFAKLLTG GMVPLAVTLA TDAVFDSFSG DSKLKALLHG HSYSAHAMGC ATAAKAIQWF
KDPETNHNIT SQGKTLRELW DEELVQQISS HSAVQRVVVI GTLFALELKA DASNSGYASL
YAKSLLIMLR EDGIFTRPLG NVIYLMCGPC TSPEICRRLL TKLYKRLGEF NRT


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EIAAB28577 Mouse,Mus musculus,Oat,Ornithine aminotransferase, mitochondrial,Ornithine--oxo-acid aminotransferase
E1612p ELISA Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Pig,Plasma membrane-associated fatty acid-binding protein,Sus 96T
U1612p CLIA Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Pig,Plasma membrane-associated fatty acid-binding protein,Sus 96T
E1612r ELISA Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,Got2,Maat,mAspAT,Plasma membrane-associated fatty acid-binding protein,Ra 96T
U1612r CLIA Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,Got2,Maat,mAspAT,Plasma membrane-associated fatty acid-binding protein,Rat 96T
CSB-EL002601RA Rat Branched-chain-amino-acid aminotransferase, mitochondrial(BCAT2) ELISA kit 96T
BCAT2_HUMAN Human ELISA Kit FOR Branched-chain-amino-acid aminotransferase, mitochondrial 96T
BCAT2_MOUSE Mouse ELISA Kit FOR Branched-chain-amino-acid aminotransferase, mitochondrial 96T
E1612b ELISA kit Aspartate aminotransferase, mitochondrial,Bos taurus,Bovine,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Plasma membrane-associated fatty acid- 96T
U1612Rb CLIA Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Oryctolagus cuniculus,Plasma membrane-associated fatty acid-bi 96T
U1612m CLIA Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,Got2,Got-2,mAspAT,Mouse,Mus musculus,Plasma membrane-associated fatty acid 96T
E1612Rb ELISA Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Oryctolagus cuniculus,Plasma membrane-associated fatty acid-b 96T
CSB-EL002601RA Rat Branched-chain-amino-acid aminotransferase, mitochondrial(BCAT2) ELISA kit SpeciesRat 96T
CSB-EL002601PI Pig Branched-chain-amino-acid aminotransferase, mitochondrial(BCAT2) ELISA kit SpeciesPig 96T
CSB-EL002601BO Bovine Branched-chain-amino-acid aminotransferase, mitochondrial(BCAT2) ELISA kit 96T
CSB-EL002601HU Human Branched-chain-amino-acid aminotransferase, mitochondrial(BCAT2) ELISA kit 96T
CSB-EL002601MO Mouse Branched-chain-amino-acid aminotransferase, mitochondrial(BCAT2) ELISA kit 96T
AE54585BO Bovine Branched-chain-amino-acid aminotransferase, mitochondrial (BCAT2) ELISA Kit 48T
EIAAB37898 Endometrial progesterone-induced protein,EPIP,Oryctolagus cuniculus,Phosphohydroxythreonine aminotransferase,Phosphoserine aminotransferase,PSA,PSAT,PSAT1,Rabbit
E1612b ELISA Aspartate aminotransferase, mitochondrial,Bos taurus,Bovine,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Plasma membrane-associated fatty acid-bindi 96T
E1612h ELISA kit Aspartate aminotransferase, mitochondrial,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,Homo sapiens,Human,mAspAT,Plasma membrane-associated fatty acid 96T
U1612b CLIA Aspartate aminotransferase, mitochondrial,Bos taurus,Bovine,FABP-1,FABPpm,Fatty acid-binding protein,Glutamate oxaloacetate transaminase 2,GOT2,mAspAT,Plasma membrane-associated fatty acid-bindin 96T


 

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