ID D8MUW7_ERWBE Unreviewed; 419 AA.
AC D8MUW7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:CAX60624.1};
GN Name=goaG {ECO:0000313|EMBL:CAX60624.1};
GN OrderedLocusNames=EbC_30930 {ECO:0000313|EMBL:CAX60624.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX60624.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX60624.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
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; FP236843; CAX60624.1; -; Genomic_DNA.
DR RefSeq; WP_013203109.1; NC_014306.1.
DR AlphaFoldDB; D8MUW7; -.
DR STRING; 634500.EbC_30930; -.
DR KEGG; ebi:EbC_30930; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OMA; KPGWDTI; -.
DR Proteomes; UP000008793; 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; 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:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 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:CAX60624.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW Transferase {ECO:0000313|EMBL:CAX60624.1}.
SQ SEQUENCE 419 AA; 44932 MW; 4DF4F8F8BFDF964E CRC64;
MNSEVQQRRL AATPRGVGVM CDFYAVRAEN ATLWDHQGRE YTDFTAGIAV LNTGHRHPKV
VEAVRNQLDC FTHTAFQVIP YENYLLLAER LNQRVPIAGP AKTTFFSSGA EAVENAVKIA
RAATGRPGVI AFTGAFHGRT MMTMGLTGKV VPYKTGFGPF PGSVFHARYP NALHGHSIDD
AMESLESLFR CDISPQQVAA IIFEPIQGEG GFNIAPVEFV SKLRTLCDQH GILLIADEIQ
TGFARTGKLF ACEYYPDAKP DLITMAKSLG GGLPISAVSG RAEVMDAPLP GGLGGTYAGN
PLAIASSLAV LEVIDEEALC DRALRLGAEL VETLNGCGNP ALVEVRARGS MVAAEFNDPA
TGKPSAEIAK NIQQKALEHG LILLTCGVHG NVIRFLYPLT IPDAQFKQAL TLLDTLLRA
//