ID N9F507_ACIHA Unreviewed; 456 AA.
AC N9F507;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Diaminobutyrate-2-oxoglutarate aminotransferase {ECO:0000313|EMBL:ENW17572.1};
GN ORFNames=F927_01926 {ECO:0000313|EMBL:ENW17572.1};
OS Acinetobacter haemolyticus CIP 64.3 = MTCC 9819.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217659 {ECO:0000313|EMBL:ENW17572.1, ECO:0000313|Proteomes:UP000017667};
RN [1] {ECO:0000313|EMBL:ENW17572.1, ECO:0000313|Proteomes:UP000017667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 64.3 {ECO:0000313|EMBL:ENW17572.1,
RC ECO:0000313|Proteomes:UP000017667};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter haemolyticus CIP 64.3.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:ENW17572.1}.
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DR EMBL; APQQ01000022; ENW17572.1; -; Genomic_DNA.
DR RefSeq; WP_004638380.1; NZ_KB849800.1.
DR AlphaFoldDB; N9F507; -.
DR GeneID; 56329778; -.
DR PATRIC; fig|1217659.3.peg.1891; -.
DR HOGENOM; CLU_016922_10_0_6; -.
DR Proteomes; UP000017667; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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 InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR004637; Dat.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00709; dat; 1.
DR PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43552:SF1; DIAMINOBUTYRATE--2-OXOGLUTARATE 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:0000313|EMBL:ENW17572.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ENW17572.1}.
SQ SEQUENCE 456 AA; 48689 MW; 1909994601C8BD5E CRC64;
MSVTSVNPAA NATNEYYLTR QSQMESNVRS YPRKLPLAIA KAQGCWVTDV EGTEYLDCLA
GAGTLALGHN HPAVIQSIQD TLASGLPLHT LDLTTPLKDA FTEALLAHLP GGKEEYCLQF
CGPSGADATE AAIKLAKTFT GRSSVISFSG GYHGMTHGSL AMTGNLSAKN AVNGLMPGVQ
FMPYPHEYRC PLGLGGEAGV DALTYFFENF IEDVESGVTK PAAVILEAIQ GEGGVVTAPA
KWLQKIREVT EKHNIVLILD EVQAGFARSG KMFAFEHAGI EPDVVVMSKA VGGGLPLAVL
GIKRKFDAWQ PAGHTGTFRG NQLAMGTGLM VLKTIKEQNL AQNAQERGDF LQAEFKKLAQ
EFPCIGNVRG RGLMIGVEIV DERKPADHMG SLPADAQLAA AIQTACFNNK LLLEKGGRNG
TVIRLLCPLI INQDECVEVI ARFKKAVAEA LKAVRG
//
