ID H2FTM5_OCESG Unreviewed; 426 AA.
AC H2FTM5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AEY02583.1};
GN OrderedLocusNames=GU3_14150 {ECO:0000313|EMBL:AEY02583.1};
OS Oceanimonas sp. (strain GK1 / IBRC-M 10197).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Oceanimonas.
OX NCBI_TaxID=511062 {ECO:0000313|EMBL:AEY02583.1, ECO:0000313|Proteomes:UP000007742};
RN [1] {ECO:0000313|EMBL:AEY02583.1, ECO:0000313|Proteomes:UP000007742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GK1 {ECO:0000313|EMBL:AEY02583.1,
RC ECO:0000313|Proteomes:UP000007742};
RX PubMed=22461556; DOI=10.1128/JB.00023-12;
RA Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., Ramezani M.,
RA Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.;
RT "Complete genome sequence of Oceanimonas sp. GK1, a halotolerant bacterium
RT from Gavkhouni Wetland in Iran.";
RL J. Bacteriol. 194:2123-2124(2012).
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|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP003171; AEY02583.1; -; Genomic_DNA.
DR RefSeq; WP_014293290.1; NC_016745.1.
DR AlphaFoldDB; H2FTM5; -.
DR STRING; 511062.GU3_14150; -.
DR KEGG; oce:GU3_14150; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000007742; Chromosome.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic 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; IPR004632; 4NH2But_aminotransferase_bac.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00700; GABAtrnsam; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
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,
KW ECO:0000313|EMBL:AEY02583.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000007742};
KW Transferase {ECO:0000313|EMBL:AEY02583.1}.
SQ SEQUENCE 426 AA; 45462 MW; D82BAE537AF841F6 CRC64;
MSKNQQLQQR KDAVFARGMG NMAPVYVDHA KNNEIWDVEG NRFIDFAAGI AVVNTGHSHP
RIVAAVSEQL QRFSHTCAMV TPYESAVALA ERLVKLAPGN SPKKAIFVTT GAEAVENAVK
IARAHTKRSG VIAFNGGFHG RTNLAMGLTG KVAPYKAGFG PFPGEIYHLP YPNAYHGVTE
AQSLKALDEL FHCDIEPGRV AALIIEPVQG EGGFYPAPPS FLQKLRALCD QHGIVLICDE
IQTGFARTGR LFATEYAGIE PDLMTMAKGI AGGFPLSAVV GKADIMDAAN PGGLGGTYAA
FPLACAAGLE VLNIIEEEQL CDKALALGEL MNKRLSELQA KYPHHIGQVR NLGAMVAMEL
VHNGDVDQPN PELTKAVVAK GIEKGVILLS CGVRGNVIRF LPALTSPLEV VSEGLDLLEQ
VLAELV
//
