ID B2GGI0_KOCRD Unreviewed; 447 AA.
AC B2GGI0;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:BAG30296.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:BAG30296.1};
GN Name=gabT {ECO:0000313|EMBL:BAG30296.1};
GN OrderedLocusNames=KRH_19490 {ECO:0000313|EMBL:BAG30296.1};
OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG30296.1, ECO:0000313|Proteomes:UP000008838};
RN [1] {ECO:0000313|EMBL:BAG30296.1, ECO:0000313|Proteomes:UP000008838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC {ECO:0000313|Proteomes:UP000008838};
RX PubMed=18408034; DOI=10.1128/JB.01853-07;
RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL J. Bacteriol. 190:4139-4146(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009152; BAG30296.1; -; Genomic_DNA.
DR RefSeq; WP_012399017.1; NC_010617.1.
DR AlphaFoldDB; B2GGI0; -.
DR STRING; 378753.KRH_19490; -.
DR KEGG; krh:KRH_19490; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_11; -.
DR OMA; GAIETMK; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000008838; Chromosome.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
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; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; ORNITHINE AMINOTRANSFERASE; 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:0000313|EMBL:BAG30296.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000008838};
KW Transferase {ECO:0000313|EMBL:BAG30296.1}.
SQ SEQUENCE 447 AA; 47075 MW; 0D251D8642406D8D CRC64;
MAEIEYRLPQ KRELVTSIPG PKSQSLAERR AQTVAAGVAS SLPVFADELD GGVIKDVDGN
QMVDLGSGIA VTSVGASNPK VVARVQDAVA KFTHTCFMVT PYEDYVAVGE KMAQLTPGSF
DKRTALFTSG SEAVENAVKI ARVRTKRQAV VVFDHAYHGR TNLTMAMTAK VMPYKQGFGP
FANEVYRVPM SYPFRDPEGM TGTEAAKRAL TMVEKQVGAE NVAAVVIEPI QGEGGFIVPA
EGFLPALSSW CRENGAVFVA DEVQAGIART GAWFASEHEG VEPDLVTFAK GIAGGMPLSG
VVGRAEIMDA VHPGGLGGTY GGNPVACAAA LGALEAIEEW DLVARAQEIE KVIREELGSV
AESSPVVGDL RGRGAMIALE FVKPGTTEPN PDAAKQIAAR CLEQGVAILT CGTYGNIVRL
LPPLVIDMDL LRDALGVFAA AIQEVGA
//