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Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (Diaminopelargonic acid synthase)

 BIOA_YEAST              Reviewed;         480 AA.
P50277; D6W1N3; E9P967; Q4R1J0;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 156.
RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase;
EC=2.6.1.62;
AltName: Full=7,8-diamino-pelargonic acid aminotransferase;
Short=DAPA AT;
Short=DAPA aminotransferase;
AltName: Full=Diaminopelargonic acid synthase;
Name=BIO3; OrderedLocusNames=YNR058W; ORFNames=N3510;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC 28383 / FL100 / VTT C-80102;
PubMed=10333520; DOI=10.1016/S0378-1119(99)00117-1;
Phalip V., Kuhn I., Lemoine Y., Jeltsch J.-M.;
"Characterization of the biotin biosynthesis pathway in Saccharomyces
cerevisiae and evidence for a cluster containing BIO5, a novel gene
involved in vitamer uptake.";
Gene 232:43-51(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-229; ARG-295 AND
ASP-384.
STRAIN=ATCC 204626 / S288c / A364A;
PubMed=16269718; DOI=10.1128/AEM.71.11.6845-6855.2005;
Wu H., Ito K., Shimoi H.;
"Identification and characterization of a novel biotin biosynthesis
gene in Saccharomyces cerevisiae.";
Appl. Environ. Microbiol. 71:6845-6855(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
-!- 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:10333520}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7-
oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-
diaminononanoate.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250};
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
1/1.
-!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
aminotransferase family. BioA subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U47112; AAA88905.1; -; Genomic_DNA.
EMBL; U53467; AAB63970.1; -; Genomic_DNA.
EMBL; AB200248; BAE00005.1; -; Genomic_DNA.
EMBL; Z71673; CAA96340.1; -; Genomic_DNA.
EMBL; AY723862; AAU09779.1; -; Genomic_DNA.
EMBL; BK006947; DAA10599.1; -; Genomic_DNA.
PIR; S63390; S63390.
RefSeq; NP_014456.1; NM_001183235.1.
ProteinModelPortal; P50277; -.
SMR; P50277; -.
BioGrid; 35884; 18.
DIP; DIP-4822N; -.
IntAct; P50277; 5.
MINT; MINT-562496; -.
STRING; 4932.YNR058W; -.
PRIDE; P50277; -.
EnsemblFungi; YNR058W; YNR058W; YNR058W.
GeneID; 855795; -.
KEGG; sce:YNR058W; -.
EuPathDB; FungiDB:YNR058W; -.
SGD; S000005341; BIO3.
HOGENOM; HOG000020209; -.
InParanoid; P50277; -.
KO; K00833; -.
OMA; FGGITHD; -.
OrthoDB; EOG092C26XW; -.
BioCyc; YEAST:YNR058W-MONOMER; -.
UniPathway; UPA00078; UER00160.
PRO; PR:P50277; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0005737; C:cytoplasm; ISS:SGD.
GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IDA:SGD.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0009102; P:biotin biosynthetic process; IDA:SGD.
CDD; cd00610; OAT_like; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR005814; Aminotrans_3.
InterPro; IPR005815; BioA.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF00202; Aminotran_3; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR00508; bioA; 1.
3: Inferred from homology;
Aminotransferase; Biotin biosynthesis; Complete proteome;
Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine;
Transferase.
CHAIN 1 480 Adenosylmethionine-8-amino-7-oxononanoate
aminotransferase.
/FTId=PRO_0000120378.
REGION 65 66 7-keto-8-aminopelargonic acid binding.
{ECO:0000250}.
REGION 126 127 Pyridoxal phosphate binding.
{ECO:0000250}.
BINDING 26 26 7-keto-8-aminopelargonic acid.
{ECO:0000250}.
BINDING 270 270 Pyridoxal phosphate. {ECO:0000250}.
BINDING 314 314 7-keto-8-aminopelargonic acid.
{ECO:0000250}.
BINDING 350 350 7-keto-8-aminopelargonic acid; via
carbonyl oxygen. {ECO:0000250}.
BINDING 352 352 Pyridoxal phosphate. {ECO:0000250}.
BINDING 441 441 7-keto-8-aminopelargonic acid.
{ECO:0000250}.
MOD_RES 314 314 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
VARIANT 229 229 K -> E (in strain: ATCC 28383 and ATCC
204626). {ECO:0000269|PubMed:16269718}.
VARIANT 295 295 H -> R (in strain: ATCC 28383 and ATCC
204626). {ECO:0000269|PubMed:16269718}.
VARIANT 384 384 N -> D (in strain: ATCC 28383 and ATCC
204626). {ECO:0000269|PubMed:16269718}.
CONFLICT 140 140 S -> P (in Ref. 5; AAU09779).
{ECO:0000305}.
SEQUENCE 480 AA; 53709 MW; 00A8BC42DCBED19A CRC64;
MSQEISYTPD VAELLDFDKK HIWHPYTSLS SPLNVYPVKS AHGCKLVLDT DSPVDVEVID
AMSSWWCVIH GYNNPELNEA LTKQMLKFSH VLLGGFTHKG AVNLVQKLLK VIDEPSLQYC
FLADSGSVAV EVALKMALQS NMSGEATKNR TKFLTIKNGY HGDTFGAMSV CDPENSMHHI
YNDRLSENIF AQAPSIVDGL PTSQNGFEDH WNAEEVTDLK KQFELHSDKI CAVILEPILQ
GAGGLRPYHP QFLIEVQKLC NQYDVLFIMD EIATGFGRTG EIFAFKHCQK YQDQHGISPS
DQIKVVPDIL CVGKGLTSGY MTMSAVVVND KVASRISSPN SPTGGCFMHG PTFMGNALAC
SVAEKSMDIL LRGEWRKQVS AIENQIYREL YQYIKNPDNG LIGTVVKRVS VIGAVGIVEL
YKKTDPEWFQ KKFISKGVHI RPFNCLCYIM PPYVITTEEL TKVNQVLIEV LHEWKSHINQ


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