ID A0A076NQX8_9CORY Unreviewed; 429 AA.
AC A0A076NQX8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 ECO:0000313|EMBL:SNV79975.1};
GN ORFNames=CIMIT_09420 {ECO:0000313|EMBL:AIJ34090.1}, SAMEA4535761_01947
GN {ECO:0000313|EMBL:SNV79975.1};
OS Corynebacterium imitans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=156978 {ECO:0000313|EMBL:AIJ34090.1, ECO:0000313|Proteomes:UP000028780};
RN [1] {ECO:0000313|EMBL:AIJ34090.1, ECO:0000313|Proteomes:UP000028780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44264 {ECO:0000313|EMBL:AIJ34090.1,
RC ECO:0000313|Proteomes:UP000028780};
RA Mollmann S., Albersmeier A., Ruckert C., Tauch A.;
RT "Complete genome sequence of Corynebacterium imitans DSM 44264, isolated
RT from a five-month-old boy with suspected pharyngeal diphtheria.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SNV79975.1, ECO:0000313|Proteomes:UP000215374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13015 {ECO:0000313|EMBL:SNV79975.1,
RC ECO:0000313|Proteomes:UP000215374};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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}.
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DR EMBL; CP009211; AIJ34090.1; -; Genomic_DNA.
DR EMBL; LT906467; SNV79975.1; -; Genomic_DNA.
DR RefSeq; WP_038592084.1; NZ_LT906467.1.
DR AlphaFoldDB; A0A076NQX8; -.
DR STRING; 156978.CIMIT_09420; -.
DR KEGG; cii:CIMIT_09420; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_3_11; -.
DR OrthoDB; 9801052at2; -.
DR UniPathway; UPA00078; UER00160.
DR Proteomes; UP000028780; Chromosome.
DR Proteomes; UP000215374; Chromosome 1.
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:UP000028780};
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 51
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 115..116
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 247
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 307..308
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
FT SITE 18
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 276
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00834"
SQ SEQUENCE 429 AA; 45898 MW; 727B2FBE8FD373D1 CRC64;
MTPETLAAID TAHIWHPYAA PGSGNLPVAA THGVYLELAD GRLLIDAMSS WWAAAHGHGH
PRLIRAAHEQ IDAMSHVMFG GLTHEPAARL TQNLLELTSG EAGPNYSRVF LADSGSVSVE
VAIKMTLQYA RGTGHPERNR LLTWRSGYHG DTFAAMSVCD PDGGMHSMWQ GVLAEQYFAP
APPVRGASDK ERAAYLAEFE KLITDDVAAV IIEPVVQGAG GMRFHDAELV RGVRELCTTH
GVLLLADEIA TGFGRTGQLF TTLDNGVVPD ILCVGKAITG GFMTLAAVLT TDEVAAGMEP
AAIMHGPTFM GNPLACAVAA EATAMIKEGD WREQTRNIEG WLTEELAPAR EIQGVADVRI
LGAIGVVEMA FDVDMAATTQ AAVDQGVWIR PFGRNIYTMP PFICTEDQTR QIGRAVVAAA
QAASKEQYQ
//
