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Database: UniProt
Entry: A0A068QRL0_9GAMM
LinkDB: A0A068QRL0_9GAMM
Original site: A0A068QRL0_9GAMM 
ID   A0A068QRL0_9GAMM        Unreviewed;       428 AA.
AC   A0A068QRL0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:CDG17623.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:CDG17623.1};
GN   Name=puuE {ECO:0000313|EMBL:CDG17623.1};
GN   ORFNames=XDD1_1924 {ECO:0000313|EMBL:CDG17623.1};
OS   Xenorhabdus doucetiae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG17623.1, ECO:0000313|Proteomes:UP000032721};
RN   [1] {ECO:0000313|EMBL:CDG17623.1, ECO:0000313|Proteomes:UP000032721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA   Genoscope - CEA;
RL   Submitted (JUL-2013) 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; FO704550; CDG17623.1; -; Genomic_DNA.
DR   RefSeq; WP_045970470.1; NZ_VNHN01000068.1.
DR   AlphaFoldDB; A0A068QRL0; -.
DR   STRING; 351671.XDD1_1924; -.
DR   KEGG; xdo:XDD1_1924; -.
DR   HOGENOM; CLU_016922_10_0_6; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000032721; 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:CDG17623.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:CDG17623.1}.
SQ   SEQUENCE   428 AA;  46148 MW;  AFCC0D8832D7BEB2 CRC64;
     MTESMLAKRR SAAIAKGVGV TTQVYVERAE NAEIWDAQGQ RYIDFAAGIA VVNTGHCHPR
     VIAAAREQLE QFTHTCHQVV PYENYVALAE RLNRLVPGHF VKKTVFVTTG AEAVENAVKI
     ARAATGRSGV VAFSGAFHGR TFLGMSLTGK VAPYKMGFGP LVSDVYHVPF PVELHGISVE
     QTLNALENLF RTDIEPTRVA AIIIEPVQGE GGFYPAPAEL LESLRDIADR YGIVLIADEI
     QTGFARTGKL FAMEHHQVAA DLTTMAKGLA GGFPLAAVTG RAELMDAVVP GGLGGTYGGN
     PVAIAASHAV LDVIEEEKLA ARATQLGERL TQYLHELRPR VPQIADVRGF GLMIAVEFHR
     AGSQEPDADF TNAVRQKALE RGLILLTCGV HSNVIRFLPP LTIQDDVFDE ALNILKSVLL
     DLNGKEGK
//
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