ID H3RF03_PANSE Unreviewed; 420 AA.
AC H3RF03;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=4-aminobutyrate transaminase {ECO:0000313|EMBL:ARF50886.1};
DE SubName: Full=GABA aminotransferase, PLP-dependent {ECO:0000313|EMBL:EHT99845.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:EHT99845.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:EHT99845.1};
GN Name=puuE {ECO:0000313|EMBL:EHT99845.1};
GN ORFNames=CKS_2065 {ECO:0000313|EMBL:EHT99845.1}, DSJ_17130
GN {ECO:0000313|EMBL:ARF50886.1};
OS Pantoea stewartii subsp. stewartii DC283.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=660596 {ECO:0000313|EMBL:EHT99845.1, ECO:0000313|Proteomes:UP000005050};
RN [1] {ECO:0000313|EMBL:EHT99845.1, ECO:0000313|Proteomes:UP000005050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC283 {ECO:0000313|EMBL:EHT99845.1,
RC ECO:0000313|Proteomes:UP000005050};
RX PubMed=22111898; DOI=10.1111/j.1365-2958.2011.07926.x;
RA Wang X., Yang F., von Bodman S.B.;
RT "The genetic and structural basis of two distinct terminal side branch
RT residues in stewartan and amylovoran exopolysaccharides and their potential
RT role in host adaptation.";
RL Mol. Microbiol. 83:195-207(2012).
RN [2] {ECO:0000313|EMBL:EHT99845.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DC283 {ECO:0000313|EMBL:EHT99845.1};
RA Biehl B.S., Ding Y., Dugan-Rocha S.P., Gibbs R.A., Glasner J.D., Kovar C.,
RA Muzny D.M., Neeno-Eckwall E.C., Perna N.T., Qin X., von Bodman S.B.,
RA Weinstock G.M.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ARF50886.1, ECO:0000313|Proteomes:UP000192380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC283 {ECO:0000313|EMBL:ARF50886.1,
RC ECO:0000313|Proteomes:UP000192380};
RA Duong D.A., Stevens A.M., Jensen R.V.;
RT "Complete Genome Assembly of Pantoea stewartii subsp. stewartii DC283, a
RT Corn Pathogen.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; CP017581; ARF50886.1; -; Genomic_DNA.
DR EMBL; AHIE01000020; EHT99845.1; -; Genomic_DNA.
DR RefSeq; WP_006120038.1; NZ_CP017581.1.
DR AlphaFoldDB; H3RF03; -.
DR STRING; 660596.DSJ_17130; -.
DR KEGG; pstw:DSJ_17130; -.
DR PATRIC; fig|660596.6.peg.2720; -.
DR eggNOG; COG0160; Bacteria.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000005050; Unassembled WGS sequence.
DR Proteomes; UP000192380; 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; 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:EHT99845.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:EHT99845.1}.
SQ SEQUENCE 420 AA; 44599 MW; 62DEB1EDE956E161 CRC64;
MSNSEVQVRR LNATPRGVGV MCDFYAVKAE NATLWDHEGR EIIDFSAGIA VLNTGHRHPK
VIAAIKEQLD CFTHTAFQIV PYENYIALAE KLNARVPVNG PAKTTFFSTG AEAVENAVKI
ARAATGRPGI IAFTGAFHGR TNMTMSLTGK VTPYKTGFGP FAGSVFHARY PNALHGCSVE
DALESVQTIF RCDISPQQVA AIIYEPIQGE GGFNVAPAGF VTALRKLCDE HGILLIADEI
QSGFARTGKL FASEYYSDVQ PDLITMAKSL AGGMPLSAVS GRAEIMDAPL PGGLGGTYAG
SPPAIAAALA VLEVIREENL CERALQLGGQ LAETLKGAGC NALADVRGRG SMIAAEFCDS
TGKPRADIAK AIQQAALDEG LLLLTCGVHG NVIRFLYPLT IPDAQFRTAL NLLNRILGQH
//
