ID K0I9W1_9BURK Unreviewed; 459 AA.
AC K0I9W1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AFU45901.1};
GN ORFNames=C380_11000 {ECO:0000313|EMBL:AFU45901.1};
OS Acidovorax sp. KKS102.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU45901.1, ECO:0000313|Proteomes:UP000006306};
RN [1] {ECO:0000313|EMBL:AFU45901.1, ECO:0000313|Proteomes:UP000006306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KKS102 {ECO:0000313|EMBL:AFU45901.1,
RC ECO:0000313|Proteomes:UP000006306};
RX PubMed=23209225; DOI=10.1128/JB.01848-12;
RA Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT Polychlorinated-Biphenyl Degrader.";
RL J. Bacteriol. 194:6970-6971(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; CP003872; AFU45901.1; -; Genomic_DNA.
DR AlphaFoldDB; K0I9W1; -.
DR STRING; 358220.C380_11000; -.
DR KEGG; ack:C380_11000; -.
DR PATRIC; fig|358220.3.peg.2238; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_4; -.
DR Proteomes; UP000006306; 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 PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 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:AFU45901.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AFU45901.1}.
SQ SEQUENCE 459 AA; 48412 MW; E99A4AB73D61A1A9 CRC64;
MDGVWRDFQN PLHSFISSST TTPTTMQQDR HFTNAALLTR RHAAVARGVG QAHDLFIQKA
RNAELWDVEG RRFIDFAGGI AVLNTGHLHA GVIAAVKAQL DLYTHTCFQV VAYEPYVEVC
ERLNTLAPGA FAKKSLLLTT GAEAVENAIK IARAYTKRPG VIAFTGGYHG RTNLTLGLTG
KVAPYKIGFG PFPGETYHAL FPNALHGVSV EQALHSVELI FKNDIEPERV AAFIVEPVQG
EGGFYVAPPE FISGLKALAD RYGILLIGDE VQTGAGRTGT WFASEQWPVA PDLITTAKSL
AGGFPLAGVV GRADVMDAPA PGGLGGTYAG SPVACAAALA VIEAFAQESL LARSQDMGAL
LVRGLKDIAA KVPAIGDVRG LGAMVAIELF ENGDLSRPDA ALTKQVVAEA ARRGLILLSC
GTHGNVIRIL VPLTASDELL HEGLAILADS LEAVAAATH
//
