ID I2BC71_SHIBC Unreviewed; 427 AA.
AC I2BC71; K6VI99;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=4-aminobutyrate aminotransferase-like aminotransferase {ECO:0000313|EMBL:AFJ48125.1};
GN Name=gabT {ECO:0000313|EMBL:AFJ48125.1};
GN OrderedLocusNames=EBL_c30550 {ECO:0000313|EMBL:AFJ48125.1};
OS Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS CDC 9005-74) (Escherichia blattae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shimwellia.
OX NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ48125.1, ECO:0000313|Proteomes:UP000001955};
RN [1] {ECO:0000313|EMBL:AFJ48125.1, ECO:0000313|Proteomes:UP000001955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC {ECO:0000313|Proteomes:UP000001955};
RX PubMed=22843577; DOI=10.1128/JB.00829-12;
RA Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT DSM 4481, isolated from a cockroach.";
RL J. Bacteriol. 194:4436-4436(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; CP001560; AFJ48125.1; -; Genomic_DNA.
DR RefSeq; WP_002442793.1; NZ_BAHA01000018.1.
DR AlphaFoldDB; I2BC71; -.
DR STRING; 630626.EBL_c30550; -.
DR KEGG; ebt:EBL_c30550; -.
DR PATRIC; fig|630626.3.peg.2972; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000001955; 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:AFJ48125.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000001955};
KW Transferase {ECO:0000313|EMBL:AFJ48125.1}.
SQ SEQUENCE 427 AA; 45640 MW; 93D40B1E411C1232 CRC64;
MSTNKELMQR RTNAVPRGVG QIHPIFADRA QNCRVWDVEG REFLDFAGGI AVLNTGHLHP
KITAAVEAQL KKLSHTCFQV LAYEPYLELC EAMNQKVPGD FAKKTLLVTT GSEAVENAVK
IARAATRRSA TIAFSGAYHG RTHYTLSLTG KVNPYSAGMG LMPGHVYRAL YPCPLHGISD
DDAIASIERI FKNDAAPEDV AAIIIEPVQG EGGFYAASPA FMQRLRALCD THGIMLIADE
VQSGAGRTGT LFAMEQMGVA ADLTTFAKSI AGGFPLAGVT GRAEVMDAVV PGGLGGTYAG
SPISCAAALA VLETFEQENL LQKAKDLGKT LRNGLLAIAE RHREIGDVRG LGAMVAIELF
EDGDTSKPNA KLTADIVARA RDKGLILLSC GPYYNVLRIL VPLTIEADQI RQGLDIIAQC
FDEAKQG
//
