ID C0ZNN8_RHOE4 Unreviewed; 454 AA.
AC C0ZNN8;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:BAH31290.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:BAH31290.1};
GN Name=gabT {ECO:0000313|EMBL:BAH31290.1};
GN OrderedLocusNames=RER_05820 {ECO:0000313|EMBL:BAH31290.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31290.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH31290.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
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; AP008957; BAH31290.1; -; Genomic_DNA.
DR RefSeq; WP_020906042.1; NC_012490.1.
DR AlphaFoldDB; C0ZNN8; -.
DR KEGG; rer:RER_05820; -.
DR PATRIC; fig|234621.6.peg.1027; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_11; -.
DR OMA; GAIETMK; -.
DR Proteomes; UP000002204; 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 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:BAH31290.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:BAH31290.1}.
SQ SEQUENCE 454 AA; 47437 MW; 8D35C35CA0604500 CRC64;
MSAIEYRLPQ ERRIVTEFPG PRSAALAERR KKVVGAGVAS TLPVYVADAD GGVIVDVDGN
SLIDLGAGIA VTSVGASNPA VVSAVQDQVA HFTHTCFMVA PYEGYVEVAE RLAELTPGDH
EKRSVLFNSG AEAVENAVKI ARHATGRDAV VVFDHAYHGR TNLTMALTSK SMPYKSGFGP
FAPEVYRVPM SYPYREGLNV DGSKITGEQA AQRAITMIEK QVGAANTAAI LIEPIQGEGG
FIVPAEGFLP TLVAWAKENG VVFIADEVQA GFARTGAWFA SDHEGIVPDL VTLAKGIAGG
MPLAAVTGRA ELIDAVHPGG LGGTYGGNPV ACAAALASID QMRELDLCGR ARTIETTVVG
RMNALAKELD VIGDVRGRGA MLAIELVKPG GQEPDADITK KIAAECLAAG VVILTCGTYG
NVIRLLPPLV ISEELLDDAL TVLETAIRTA AQGN
//