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Database: UniProt/TrEMBL
Entry: A4SQ50_AERS4
LinkDB: A4SQ50_AERS4
Original site: A4SQ50_AERS4 
ID   A4SQ50_AERS4            Unreviewed;       434 AA.
AC   A4SQ50;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   07-JUN-2017, entry version 60.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ABO91022.1};
GN   Name=gabT {ECO:0000313|EMBL:ABO91022.1};
GN   OrderedLocusNames=ASA_3021 {ECO:0000313|EMBL:ABO91022.1};
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245 {ECO:0000313|EMBL:ABO91022.1, ECO:0000313|Proteomes:UP000000225};
RN   [1] {ECO:0000313|Proteomes:UP000000225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449 {ECO:0000313|Proteomes:UP000000225};
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A.,
RA   Kimball J., Munholland J., Murphy C., Sarty D., Williams J.,
RA   Nash J.H., Johnson S.C., Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights
RT   into the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(2008).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000644; ABO91022.1; -; Genomic_DNA.
DR   RefSeq; WP_005312492.1; NC_009348.1.
DR   ProteinModelPortal; A4SQ50; -.
DR   STRING; 382245.ASA_3021; -.
DR   EnsemblBacteria; ABO91022; ABO91022; ASA_3021.
DR   GeneID; 4996444; -.
DR   KEGG; asa:ASA_3021; -.
DR   PATRIC; fig|382245.13.peg.3001; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K07250; -.
DR   OMA; PYRWPSG; -.
DR   Proteomes; UP000000225; 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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00700; GABAtrnsam; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ABO91022.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000225};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:ABO91022.1}.
SQ   SEQUENCE   434 AA;  45698 MW;  E663BE9F78EA9FCC CRC64;
     MSHSDSHADN NRAWQARGEA AVVNGVGTLL PVFIDKTLNA ELWDVEGNRY IDFASGIAVL
     NTGHNHPKVV AAVREQLEKF SHTCFQVTPY PGYIELAEKL NALVPGPTPK RTLFLSTGAE
     AVENAIKIAR AHTGRSGTIA FKGGFHGRTM MGMALTGKVV PYKTGFGPFP GEVYHLPFPS
     DYLGVSEADA LAALDLCFSS DIEPARVAAI ILEPVQGEGG FYSASPSFMQ SLRKLCDQHG
     IVLICDEIQS GFCRTGKTFA TEYSGIEPDI MTLAKSLAGG FPLSAVVGKA AIMNAAKPGG
     LGGTYAGSPI ACAAALAVLE VIEEEQLNQK ALAQGAQIKA RLHQLAEGFD CIGDIRGPGA
     MVAMELVKGR DASQPDPDLT KRLVAEAGKR GLVLLSCGVR ANVIRFLAPL TATPALIEEG
     LALLEQALTA ASQG
//
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