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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) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)

 J8AFL7_BACCE            Unreviewed;       477 AA.
J8AFL7;
31-OCT-2012, integrated into UniProtKB/TrEMBL.
31-OCT-2012, sequence version 1.
28-MAR-2018, entry version 34.
RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
EC=2.6.1.62 {ECO:0000256|HAMAP-Rule:MF_00834};
AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
Short=DAPA AT {ECO:0000256|HAMAP-Rule:MF_00834};
Short=DAPA aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
AltName: Full=7,8-diaminononanoate synthase {ECO:0000256|HAMAP-Rule:MF_00834};
Short=DANS {ECO:0000256|HAMAP-Rule:MF_00834};
AltName: Full=Diaminopelargonic acid synthase {ECO:0000256|HAMAP-Rule:MF_00834};
Name=bioA {ECO:0000256|HAMAP-Rule:MF_00834};
ORFNames=IEE_01315 {ECO:0000313|EMBL:EJQ47311.1};
Bacillus cereus BAG5X1-1.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus cereus group.
NCBI_TaxID=1053189 {ECO:0000313|EMBL:EJQ47311.1, ECO:0000313|Proteomes:UP000006600};
[1] {ECO:0000313|EMBL:EJQ47311.1, ECO:0000313|Proteomes:UP000006600}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BAG5X1-1 {ECO:0000313|EMBL:EJQ47311.1,
ECO:0000313|Proteomes:UP000006600};
The Broad Institute Genome Sequencing Platform;
The Broad Institute Genome Sequencing Center for Infectious Disease;
Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V.,
Timmery S., Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X.,
Shank E.B., Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q.,
Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A.,
Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C.,
Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
Nusbaum C., Birren B.;
"The Genome Sequence of Bacillus cereus BAG5X1-1.";
Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
-!- 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:0000256|HAMAP-Rule:MF_00834}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7-
oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-
diaminononanoate. {ECO:0000256|HAMAP-Rule:MF_00834}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000256|HAMAP-Rule:MF_00834};
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
1/1. {ECO:0000256|HAMAP-Rule:MF_00834}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00834}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834}.
-!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
aminotransferase family. BioA subfamily. {ECO:0000256|HAMAP-
Rule:MF_00834}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00834}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EJQ47311.1}.
-----------------------------------------------------------------------
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EMBL; AHDJ01000018; EJQ47311.1; -; Genomic_DNA.
RefSeq; WP_002199416.1; NZ_JH791996.1.
ProteinModelPortal; J8AFL7; -.
EnsemblBacteria; EJQ47311; EJQ47311; IEE_01315.
PATRIC; fig|1053189.3.peg.1337; -.
UniPathway; UPA00078; UER00160.
Proteomes; UP000006600; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-UniRule.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd00610; OAT_like; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
HAMAP; MF_00834; BioA; 1.
InterPro; IPR005814; Aminotrans_3.
InterPro; IPR005815; BioA.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
Pfam; PF00202; Aminotran_3; 1.
PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR00508; bioA; 1.
PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
3: Inferred from homology;
Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00834};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000006600};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834};
Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00834,
ECO:0000256|RuleBase:RU003560};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00834};
Transferase {ECO:0000256|HAMAP-Rule:MF_00834}.
REGION 142 143 Pyridoxal phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_00834}.
COILED 216 247 {ECO:0000256|SAM:Coils}.
BINDING 175 175 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00834}.
BINDING 281 281 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00834}.
BINDING 310 310 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00834}.
BINDING 345 345 Substrate; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00834}.
BINDING 440 440 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00834}.
SITE 45 45 Participates in the substrate recognition
with KAPA and in a stacking interaction
with the adenine ring of SAM.
{ECO:0000256|HAMAP-Rule:MF_00834}.
MOD_RES 310 310 N6-(pyridoxal phosphate)lysine.
{ECO:0000256|HAMAP-Rule:MF_00834}.
SEQUENCE 477 AA; 53878 MW; 3E48BBA49D0D48A3 CRC64;
MLTIFINKLT LGVTIVAVNS NTSEKSSYTY EELSKKNKDY VWHPFTQMKD YLEEDPVIIE
RGEGRKLYDV NGNEYWDGVS SIWLNVHGHQ VPELDEAIRE QLNKIAHSTM LGLANVPSIL
LAEKIIDVVP EGLKKVFYSD SGSTAVEIAI KMAFQYWQHK GKPRKQRFVT LKEAYHGDTI
GAVSVGAIDL FHQVYSSLLF EAIKMPYPYT YRSPYGDNKE QIVKKHLEEM EELLKEKHEE
IAAIIVEPLM QGAGGMITMP KGYLKGLRNL CTKYNVLFIT DEVATGFGRT GKMFACEHEN
VTPDILTAGK GLTGGYLPIA VTVTKDEIYN AFLGEYEEQK TFFHGHSYTG NPLGCAVAIA
NLELYEKTNL IESVAHKTEY VAGQLEALNE YKHVGDIRQC GLMIGIELVK NKEMKESYEW
TERVGVQVCK RSRELGMILR PLGNTIVFMP PLASTMAEID EMLRILYKAI SDITEEE


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