ID L8XZ58_9GAMM Unreviewed; 451 AA.
AC L8XZ58;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=F387_01390 {ECO:0000313|EMBL:ELV07586.1};
OS Wohlfahrtiimonas chitiniclastica SH04.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Ignatzschineriaceae; Wohlfahrtiimonas.
OX NCBI_TaxID=1261130 {ECO:0000313|EMBL:ELV07586.1, ECO:0000313|Proteomes:UP000011617};
RN [1] {ECO:0000313|EMBL:ELV07586.1, ECO:0000313|Proteomes:UP000011617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH04 {ECO:0000313|EMBL:ELV07586.1,
RC ECO:0000313|Proteomes:UP000011617};
RX PubMed=23558531;
RA Cao X.M., Chen T., Xu L.Z., Yao L.S., Qi J., Zhang X.L., Yan Q.L.,
RA Deng Y.H., Guo T.Y., Wang J., Hu K.X., Xu B.L.;
RT "Complete Genome Sequence of Wohlfahrtiimonas chitiniclastica Strain SH04,
RT Isolated from Chrysomya megacephala Collected from Pudong International
RT Airport in China.";
RL Genome Announc. 1:E0011913-E0011913(2013).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELV07586.1}.
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DR EMBL; AOBV01000009; ELV07586.1; -; Genomic_DNA.
DR RefSeq; WP_008316171.1; NZ_KB372782.1.
DR AlphaFoldDB; L8XZ58; -.
DR PATRIC; fig|1261130.3.peg.1429; -.
DR HOGENOM; CLU_016922_4_3_6; -.
DR OrthoDB; 7052035at2; -.
DR UniPathway; UPA00078; UER00160.
DR Proteomes; UP000011617; Unassembled WGS sequence.
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 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}; Reference proteome {ECO:0000313|Proteomes:UP000011617};
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 56
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-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 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 255
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 320..321
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT SITE 19
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 284
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
SQ SEQUENCE 451 AA; 51375 MW; DE099E1C97CD1AD8 CRC64;
MTENQKWMQR DLSVVWHPCT QMKDHETYPL VPIKRGEGVW LYDFDDNKYL DGISSWWVNV
FGHANPKINQ AVKDQLDQLE HVIMAGFTHE PMIRLSEELV SITRDGLDYC FYADNGSSCI
ESALKMSMHY WRNVGEPTKN KFVTFTNSYH GETVGAMSVG DAPLYTQSYK SMLFDTFKVT
APDLYEKAED ETEEAYTLKR FAEMEALIHD HHHEIAAVII EPLVQCAGGM RMHSPLYLTK
LRALCDQYNV HIILDEIAVG FGRTGTMFAH EQADMVPDFL CLSKALTGGY LPMSVCMTSK
KVYDAFYREY HPESVFLHSH SYTGNALACS AALATLSIFR EDDVINNNQK LIQAFAKYTA
PLKDHPNVAQ VRQTGMITAI EVVKDKATRT PFSWESRIGL KMFDYAMKHG LLIRPLGGIV
YFNTPYIVTE EQIKWMVNIA TDAIDYALTQ V
//
