ID A9WMI0_RENSM Unreviewed; 461 AA.
AC A9WMI0;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ABY23535.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:ABY23535.1};
GN OrderedLocusNames=RSal33209_1802 {ECO:0000313|EMBL:ABY23535.1};
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Renibacterium.
OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY23535.1, ECO:0000313|Proteomes:UP000002007};
RN [1] {ECO:0000313|Proteomes:UP000002007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC {ECO:0000313|Proteomes:UP000002007};
RX PubMed=18723615; DOI=10.1128/JB.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
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; CP000910; ABY23535.1; -; Genomic_DNA.
DR RefSeq; WP_012245206.1; NC_010168.1.
DR AlphaFoldDB; A9WMI0; -.
DR SMR; A9WMI0; -.
DR STRING; 288705.RSal33209_1802; -.
DR KEGG; rsa:RSal33209_1802; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_4_0_11; -.
DR Proteomes; UP000002007; 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 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; 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 PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
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:ABY23535.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000002007};
KW Transferase {ECO:0000313|EMBL:ABY23535.1}.
SQ SEQUENCE 461 AA; 50183 MW; 3C96C0171D5B8849 CRC64;
MSTSTQKPED QQLAKAQVKA DDRNHVFHSW SAQAKIDPLP VAGGSGATFW DYDGKHYLDF
SSQLVNLNLG HQHPRLIEAI KRQADKLVTI QPAFANDVRG ELARLLAERA PGSLNQVFFT
NGGADANEHA VRMARQHTGK RKILAAYRSY HGGTTTAMSL TGEPRRWAND PGDASVVHFF
GPYPYRSAFH SSSLEEETQR ALEHLESVIQ LEGPGTVAGI ILETVVGTNG VFIPPPGYLQ
GVREICDRYG MVYIADEVMV GFGRIGEWFA VDAFDVVPDL LTFAKGINSG YVPLGGVLIS
DAIAETFAER AYPGGLTYSG HPLACAVGVE TMHIFAGDQI PERVRDLGER VVRPELERWA
QVHPSVGEVR GLGLFWAIEL VRDRSSGEPL VPFNASGEAA APMNAIAAAC KAAGLWPFTH
FNRVHVAPPL IISEEDLRRG LAIIDEALLV ADSYAEPAEE Q
//
