ID G8N7H8_GEOTH Unreviewed; 459 AA.
AC G8N7H8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE EC=2.6.1.62 {ECO:0000256|HAMAP-Rule:MF_00834};
DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE Short=DAPA AT {ECO:0000256|HAMAP-Rule:MF_00834};
DE Short=DAPA aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE AltName: Full=7,8-diaminononanoate synthase {ECO:0000256|HAMAP-Rule:MF_00834};
DE Short=DANS {ECO:0000256|HAMAP-Rule:MF_00834};
DE AltName: Full=Diaminopelargonic acid synthase {ECO:0000256|HAMAP-Rule:MF_00834};
GN Name=bioA {ECO:0000256|HAMAP-Rule:MF_00834};
GN ORFNames=GTCCBUS3UF5_33750 {ECO:0000313|EMBL:AEV20676.1};
OS Geobacillus thermoleovorans CCB_US3_UF5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=1111068 {ECO:0000313|EMBL:AEV20676.1, ECO:0000313|Proteomes:UP000005636};
RN [1] {ECO:0000313|EMBL:AEV20676.1, ECO:0000313|Proteomes:UP000005636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB_US3_UF5 {ECO:0000313|EMBL:AEV20676.1,
RC ECO:0000313|Proteomes:UP000005636};
RA Muhd Sakaff M.K.L., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.;
RT "Complete genome sequence of thermophilic Geobacillus thermoleovorans
RT CCB_US3_UF5.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S-
CC adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to
CC form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase
CC known to utilize SAM as an amino donor. {ECO:0000256|HAMAP-
CC Rule:MF_00834}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine =
CC (7R,8S)-7,8-diammoniononanoate + S-adenosyl-4-methylsulfanyl-2-
CC oxobutanoate; Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:149468, ChEBI:CHEBI:149469;
CC EC=2.6.1.62; Evidence={ECO:0000256|HAMAP-Rule:MF_00834};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00834};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
CC {ECO:0000256|HAMAP-Rule:MF_00834}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00834}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. BioA subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_00834}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00834}.
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DR EMBL; CP003125; AEV20676.1; -; Genomic_DNA.
DR RefSeq; WP_011232486.1; NC_016593.1.
DR AlphaFoldDB; G8N7H8; -.
DR KEGG; gte:GTCCBUS3UF5_33750; -.
DR PATRIC; fig|1111068.3.peg.3283; -.
DR HOGENOM; CLU_016922_4_3_9; -.
DR UniPathway; UPA00078; UER00160.
DR Proteomes; UP000005636; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00834; BioA; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR005815; BioA.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00508; bioA; 1.
DR PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF21; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_00834}; Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00834};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00834};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00834};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00834}.
FT BINDING 116..117
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 258
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 323..324
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT SITE 20
FT /note="Participates in the substrate recognition with KAPA
FT and in a stacking interaction with the adenine ring of SAM"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT MOD_RES 287
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
SQ SEQUENCE 459 AA; 52277 MW; 1191E3AF301F8E6D CRC64;
MAYSYEQLEQ WDKQYVWHPF TQMKQYAKER PLIIERGQGS YLYDVDGNRY LDGYASLWVN
VHGHNDPELN AALREQLEKI AHSTLLGSAN VPSILLAKRL LEYWPHMSKV FYSDTGAAAV
EIALKIAYQY WKNIDPVQYA KKNKFVSLKE AYHGDTVGAV SVGGMETFHR IFAPLLFERI
EVPSPYVYRM DEYGSEQEIV GYCLRELERV LEEQHDQIAA VVIEPLVQGA AGIIVHPRGF
LKGVERLCRR YGVLFICDEV AVGFGRTGTM FACEQEEVKP DLVCLGKGIT GGYLPLAATL
VTEEIYAAFL GDVDEDKTFY HGHTYTGNQL TCSVALKNIE LIEKRSLIDS VKRKARRLAE
WLERLYEIPI VGDIRQKGLM CGIEIVKDRR TKEVFPRAAM VEHRIILEAR RRGLVIRPLG
PVLTFIPVLS MSEDEMAEAV RILFDSLACL YEQARAELL
//
