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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.
13-FEB-2019, entry version 86.
RecName: Full=Bifunctional dethiobiotin synthetase/7,8-diamino-pelargonic acid aminotransferase, mitochondrial;
AltName: Full=Bifunctional BIO3-BIO1 protein {ECO:0000303|PubMed:17993549};
Includes:
RecName: Full=Dethiobiotin synthetase;
EC=6.3.3.3 {ECO:0000269|PubMed:22547782};
AltName: Full=DTB synthetase;
Short=DTBS;
AltName: Full=Protein BIOTIN AUXOTROPH 3 {ECO:0000303|PubMed:17993549};
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 {ECO:0000269|PubMed:22547782};
AltName: Full=Diaminopelargonic acid synthase;
AltName: Full=Protein BIOTIN AUXOTROPH 1 {ECO:0000303|PubMed:17993549};
Flags: Precursor;
Name=BIO3-BIO1 {ECO:0000303|PubMed:17993549};
Synonyms=BIO1 {ECO:0000303|PubMed:17993549},
BIO3 {ECO:0000303|PubMed:17993549};
OrderedLocusNames=At5g57590 {ECO:0000312|Araport:AT5G57590};
ORFNames=MUA2.17/MUA2.18 {ECO:0000312|EMBL:BAB08794.1};
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).
[11]
DISRUPTION PHENOTYPE.
PubMed=11779812;
McElver J., Tzafrir I., Aux G., Rogers R., Ashby C., Smith K.,
Thomas C., Schetter A., Zhou Q., Cushman M.A., Tossberg J., Nickle T.,
Levin J.Z., Law M., Meinke D., Patton D.;
"Insertional mutagenesis of genes required for seed development in
Arabidopsis thaliana.";
Genetics 159:1751-1763(2001).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12644697; DOI=10.1104/pp.013243;
Che P., Weaver L.M., Wurtele E.S., Nikolau B.J.;
"The role of biotin in regulating 3-methylcrotonyl-coenzyme a
carboxylase expression in Arabidopsis.";
Plant Physiol. 131:1479-1486(2003).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23031218; DOI=10.1111/tpj.12037;
Pommerrenig B., Popko J., Heilmann M., Schulmeister S., Dietel K.,
Schmitt B., Stadler R., Feussner I., Sauer N.;
"SUCROSE TRANSPORTER 5 supplies Arabidopsis embryos with biotin and
affects triacylglycerol accumulation.";
Plant J. 73:392-404(2013).
[14]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 23-833 IN COMPLEX WITH
(4R,5S)-DETHIOBIOTIN; 7-KETO-8-AMINOPELARGONIC ACID; L-TARTARIC ACID
AND PYRIDOXAL PHOSPHATE, FUNCTION, MUTAGENESIS OF PHE-348; SER-382 AND
ILE-815, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PATHWAY, COFACTOR,
ALTERNATIVE SPLICING, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=cv. Columbia;
PubMed=22547782; DOI=10.1105/TPC.112.097675;
Cobessi D., Dumas R., Pautre V., Meinguet C., Ferrer J.-L., Alban C.;
"Biochemical and structural characterization of the Arabidopsis
bifunctional enzyme dethiobiotin synthetase-diaminopelargonic acid
aminotransferase: evidence for substrate channeling in biotin
synthesis.";
Plant Cell 24:1608-1625(2012).
-!- FUNCTION: Bifunctional enzyme that catalyzes two different
reactions involved in the biotin biosynthesis.
{ECO:0000269|PubMed:12644697, ECO:0000269|PubMed:17993549,
ECO:0000269|PubMed:22547782, ECO:0000269|PubMed:23031218}.
-!- 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:22547782,
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.
{ECO:0000269|PubMed:22547782}.
-!- CATALYTIC ACTIVITY:
Reaction=7,8-diaminononanoate + ATP + CO2 = ADP + dethiobiotin + 3
H(+) + phosphate; Xref=Rhea:RHEA:15805, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57861, ChEBI:CHEBI:58500, ChEBI:CHEBI:456216;
EC=6.3.3.3; Evidence={ECO:0000269|PubMed:22547782};
-!- CATALYTIC ACTIVITY:
Reaction=8-amino-7-oxononanoate + S-adenosyl-L-methionine = 7,8-
diaminononanoate + S-adenosyl-4-methylsulfanyl-2-oxobutanoate;
Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490, ChEBI:CHEBI:57532,
ChEBI:CHEBI:58500, ChEBI:CHEBI:59789; EC=2.6.1.62;
Evidence={ECO:0000269|PubMed:22547782};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:22547782};
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:22547782};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=415 nm {ECO:0000269|PubMed:22547782};
Note=Shoulder at 335 nm (at pH 7.5 and 30 degrees Celsius).
{ECO:0000269|PubMed:22547782};
Kinetic parameters:
Note=kcat is 0.072 min(-1) for 7,8-diamino-pelargonic acid
aminotransferase + dethiobiotin synthetase activities, and 1.85
min(-1) for 7,8-diamino-pelargonic acid aminotransferase
activity only (at pH 7.5 and 30 degrees Celsius).
{ECO:0000269|PubMed:22547782};
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from
7,8-diaminononanoate: step 1/2. {ECO:0000269|PubMed:22547782}.
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
1/1. {ECO:0000269|PubMed:22547782}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22547782}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:22547782}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Only the isoform BIO3-BIO1 is detected at protein level
in mitochondria. {ECO:0000269|PubMed:22547782};
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 (PubMed:11779812,
PubMed:17993549). Biotin depletion leading to lethality; this
phenotype is rescued by exogenous supply of biotin
(PubMed:12644697, PubMed:23031218). {ECO:0000269|PubMed:11779812,
ECO:0000269|PubMed:12644697, ECO:0000269|PubMed:17993549,
ECO:0000269|PubMed:23031218}.
-!- 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};
-!- WEB RESOURCE: Name=Seed defective Arabidopsis mutants;
URL="http://seedgenes.org/MutantList";
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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; 289012at2759; -.
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.
Genevisible; B0F481; AT.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
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:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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; 1.
SUPFAM; SSF53383; SSF53383; 1.
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|UniProtKB:P13000}.
NP_BIND 210 213 ATP. {ECO:0000250|UniProtKB:P13000}.
NP_BIND 270 271 ATP. {ECO:0000250|UniProtKB:P13000}.
NP_BIND 518 520 ATP. {ECO:0000250|UniProtKB:P13000}.
REGION 36 299 Dethiobiotin synthetase. {ECO:0000305}.
REGION 332 830 7,8-diamino-pelargonic acid
aminotransferase. {ECO:0000305}.
REGION 391 392 7-keto-8-aminopelargonic acid binding.
{ECO:0000244|PDB:4A0H,
ECO:0000269|PubMed:22547782}.
REGION 453 454 Pyridoxal phosphate binding.
{ECO:0000244|PDB:4A0G,
ECO:0000244|PDB:4A0H,
ECO:0000244|PDB:4A0R,
ECO:0000269|PubMed:22547782}.
REGION 701 702 Pyridoxal phosphate binding.
{ECO:0000244|PDB:4A0G,
ECO:0000244|PDB:4A0H,
ECO:0000244|PDB:4A0R,
ECO:0000269|PubMed:22547782}.
METAL 51 51 Magnesium. {ECO:0000244|PDB:4A0G,
ECO:0000269|PubMed:22547782}.
METAL 88 88 Magnesium. {ECO:0000244|PDB:4A0G,
ECO:0000269|PubMed:22547782}.
METAL 210 210 Magnesium. {ECO:0000244|PDB:4A0G,
ECO:0000269|PubMed:22547782}.
BINDING 81 81 Substrate. {ECO:0000244|PDB:4A0R,
ECO:0000269|PubMed:22547782}.
BINDING 97 97 ATP. {ECO:0000250|UniProtKB:P13000}.
BINDING 495 495 7-keto-8-aminopelargonic acid.
{ECO:0000244|PDB:4A0H,
ECO:0000269|PubMed:22547782}.
BINDING 545 545 ATP. {ECO:0000250|UniProtKB:P13000}.
BINDING 637 637 Pyridoxal phosphate.
{ECO:0000244|PDB:4A0G,
ECO:0000244|PDB:4A0H,
ECO:0000244|PDB:4A0R,
ECO:0000269|PubMed:22547782}.
BINDING 666 666 7-keto-8-aminopelargonic acid.
{ECO:0000244|PDB:4A0H,
ECO:0000269|PubMed:22547782}.
BINDING 700 700 7-keto-8-aminopelargonic acid; via
carbonyl oxygen. {ECO:0000244|PDB:4A0H,
ECO:0000269|PubMed:22547782}.
BINDING 797 797 7-keto-8-aminopelargonic acid.
{ECO:0000244|PDB:4A0H,
ECO:0000269|PubMed:22547782}.
SITE 348 348 Participates in the substrate recognition
with KAPA and in a stacking interaction
with the adenine ring of SAM.
{ECO:0000250|UniProtKB:P12995}.
MOD_RES 666 666 N6-(pyridoxal phosphate)lysine.
{ECO:0000244|PDB:4A0F,
ECO:0000244|PDB:4A0G,
ECO:0000244|PDB:4A0H,
ECO:0000244|PDB:4A0R,
ECO:0000269|PubMed:22547782}.
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 348 348 F->Y: No important impact on the enzyme
kinetic parameters.
{ECO:0000269|PubMed:22547782}.
MUTAGEN 382 382 S->Y: Reduced substrate channeling
leading to slower 7,8-diamino-pelargonic
acid aminotransferase + dethiobiotin
synthetase activities.
{ECO:0000269|PubMed:22547782}.
MUTAGEN 777 833 Missing: In bio1-1: Arrested embryo.
{ECO:0000269|PubMed:2909401}.
MUTAGEN 815 815 I->W: Reduced substrate channeling
leading to slower 7,8-diamino-pelargonic
acid aminotransferase + dethiobiotin
synthetase activities.
{ECO:0000269|PubMed:22547782}.
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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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP2199: Seed Development
WP1493: Carbon assimilation C4 pathway
WP1577: amino acid conjugation of benzoic acid
WP521: amino acid conjugation of benzoic acid
WP1621: Arginine and proline metabolism
WP1654: gamma-Hexachlorocyclohexane degradation
WP1700: Selenoamino acid metabolism
WP1689: Porphyrin and chlorophyll metabolism
WP1708: Terpenoid backbone biosynthesis
WP2211: Geranylgeranyldiphosphate biosynthesis II (plastidic)
WP626: Abscisic Acid Biosynthesis
WP668: Octadecanoid Pathway
WP1008: amino acid conjugation of benzoic acid
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1127: amino acid conjugation of benzoic acid
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1252: amino acid conjugation of benzoic acid
WP1287: amino acid conjugation of benzoic acid
WP1502: Mitochondrial biogenesis
WP2345: vitamin B7 (biotin) biosynthesis pathway
WP368: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP401: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP406: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP419: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP448: Mitochondrial LC-Fatty Acid Beta-Oxidation

Related Genes :
[TTHA1582] 8-amino-7-oxononanoate synthase/2-amino-3-ketobutyrate coenzyme A ligase (AONS/AKB ligase) (EC 2.3.1.29) (EC 2.3.1.47) (7-keto-8-amino-pelargonic acid synthase) (7-KAP synthase) (KAPA synthase) (8-amino-7-ketopelargonate synthase) (Alpha-oxoamine synthase) (Glycine acetyltransferase)
[bioA HPHPH6_1137] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPP62_1105] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA OR1_02255] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPP1_1246] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPA8_0903] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPH24_1299] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPP11_1335] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPH45_1063] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPH27_1641] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPH11_1220] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPH30_1221] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPP15_1336] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPP23_1384] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPP26_1687] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPH43_1034] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPNQ4216_1336] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPA4_1215] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPP41_1254] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPH34_0052] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPP74_1650] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPA20_1240] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPP4_1376] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPH16_1214] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPH23_0970] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPH19_1352] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA OUK_1268] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA OUG_1307] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPP13_1295] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)
[bioA HPHPP16_0550] Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)

Bibliography :
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