ID N9T0E8_9GAMM Unreviewed; 456 AA.
AC N9T0E8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Diaminobutyrate-2-oxoglutarate aminotransferase {ECO:0000313|EMBL:ENX56825.1};
GN ORFNames=F901_00150 {ECO:0000313|EMBL:ENX56825.1};
OS Acinetobacter dispersus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=70348 {ECO:0000313|EMBL:ENX56825.1, ECO:0000313|Proteomes:UP000013195};
RN [1] {ECO:0000313|EMBL:ENX56825.1, ECO:0000313|Proteomes:UP000013195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 1867 {ECO:0000313|EMBL:ENX56825.1,
RC ECO:0000313|Proteomes:UP000013195};
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 sp. NIPH 1867.";
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:ENX56825.1}.
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DR EMBL; APRO01000001; ENX56825.1; -; Genomic_DNA.
DR RefSeq; WP_005208276.1; NZ_KB850085.1.
DR AlphaFoldDB; N9T0E8; -.
DR PATRIC; fig|1217702.3.peg.145; -.
DR HOGENOM; CLU_016922_10_0_6; -.
DR Proteomes; UP000013195; 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; 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:ENX56825.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ENX56825.1}.
SQ SEQUENCE 456 AA; 48734 MW; 9246E800A9F798A0 CRC64;
MSVTSVNPAT NSTNEYYLTR QSQMESNVRS YPRKLPLAIA KALGCWVTDV EGTEYLDCLA
GAGTLALGHN HPAVIQSIQD TLASGLPLHT LDLTTPLKDA FTEALLEQLP GGKEEYCLQF
CGPSGADGTE AAIKLAKTYT GRSTVISFSG GYHGMTHGAL AMTGNLSAKN AVNGLMPGVQ
FMPYPHEYRC PLGLGGEAGV DALTYFFENF IEDVESGVTK PAAVILEAIQ GEGGVVTAPV
KWLQKIREVT EKHNIVLILD EVQAGFARSG KMFAFEHAGI EPDVVVMSKA VGGSLPLAVL
GIKRKFDAWQ PAGHTGTFRG NQLAMGTGLA SLKVIKEQNL AQNAQERGDF LQAEFKKLAQ
EFPCIGNVRG RGLMIGVEIV DERKPADHMG SLPADAQLAA AIQTACFNNK LLLEKGGRNG
TVIRLLCPLI INHEECVEAV ARFKKAVAEA LKAVRG
//