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Database: UniProt
Entry: D4GJ65_PANAM
LinkDB: D4GJ65_PANAM
Original site: D4GJ65_PANAM 
ID   D4GJ65_PANAM            Unreviewed;       420 AA.
AC   D4GJ65;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   SubName: Full=PuuE {ECO:0000313|EMBL:ADD77815.1};
GN   Name=puuE {ECO:0000313|EMBL:ADD77815.1};
GN   OrderedLocusNames=PANA_2648 {ECO:0000313|EMBL:ADD77815.1};
OS   Pantoea ananatis (strain LMG 20103).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD77815.1, ECO:0000313|Proteomes:UP000001702};
RN   [1] {ECO:0000313|EMBL:ADD77815.1, ECO:0000313|Proteomes:UP000001702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD77815.1,
RC   ECO:0000313|Proteomes:UP000001702};
RX   PubMed=20348253; DOI=10.1128/JB.00060-10;
RA   De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA   Coutinho T.A.;
RT   "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT   Eucalyptus blight and dieback.";
RL   J. Bacteriol. 192:2936-2937(2010).
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; CP001875; ADD77815.1; -; Genomic_DNA.
DR   RefSeq; WP_013026526.1; NC_013956.2.
DR   AlphaFoldDB; D4GJ65; -.
DR   STRING; 706191.PANA_2648; -.
DR   GeneID; 57267457; -.
DR   KEGG; pam:PANA_2648; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_6; -.
DR   OMA; VMCGFYA; -.
DR   Proteomes; UP000001702; 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; 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:0000256|ARBA:ARBA00022576};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001702};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ   SEQUENCE   420 AA;  44584 MW;  0409B87D80AD8717 CRC64;
     MSNSEVQVRR LNATPRGVGV MCDFYAVKAE NATLWDHQGR EIIDFSAGIA VLNTGHRHPK
     VIAAIKEQLD HFTHTAFQVV PYENYIALAE KLNALVPVSG PAKTTFFSTG AEAVENAVKI
     ARAATGRPGV IAFTGAFHGR TNMTMSLTGK VVPYKTGFGP FASSVFHARY PNALHGCSVD
     DALESLQTIF RCDISPQQVA AIIYEPIQGE GGFNVAPPAF VTALRTLCDQ HGILLIADEI
     QSGFARTGKL FASEYYPDVQ PDLITMAKSL AGGMPLSAVS GRADVMDAPL PGGLGGTYAG
     SPPAIAAALA VLEVIRDENL CERALLLGGQ LTETLQGAGC SALAEVRGRG SMIAAEFTNS
     EGQPSADIAK AIQQEALDEG LLLLTCGVHG NVIRFLYPLT IPDAQFRTAL NLLNRILGKY
//
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