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Database: UniProt
Entry: A0A132BRM5_9RHOB
LinkDB: A0A132BRM5_9RHOB
Original site: A0A132BRM5_9RHOB 
ID   A0A132BRM5_9RHOB        Unreviewed;       425 AA.
AC   A0A132BRM5;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=4-aminobutyrate aminotransferase PuuE {ECO:0000313|EMBL:KUP91021.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:KUP91021.1};
GN   Name=puuE {ECO:0000313|EMBL:KUP91021.1};
GN   ORFNames=TRIHO_41380 {ECO:0000313|EMBL:KUP91021.1};
OS   Tritonibacter horizontis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Tritonibacter.
OX   NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP91021.1, ECO:0000313|Proteomes:UP000068382};
RN   [1] {ECO:0000313|EMBL:KUP91021.1, ECO:0000313|Proteomes:UP000068382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O3.65 {ECO:0000313|EMBL:KUP91021.1,
RC   ECO:0000313|Proteomes:UP000068382};
RA   Poehlein A., Giebel H.A., Voget S., Brinkhoff T.;
RT   "Genome sequence of the marine Rhodobacteraceae strain O3.65, Candidatus
RT   Tritonibacter horizontis.";
RL   Submitted (DEC-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUP91021.1}.
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DR   EMBL; LPUY01000128; KUP91021.1; -; Genomic_DNA.
DR   RefSeq; WP_068248295.1; NZ_LPUY01000128.1.
DR   AlphaFoldDB; A0A132BRM5; -.
DR   PATRIC; fig|1768241.3.peg.4323; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000068382; Unassembled WGS sequence.
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:KUP91021.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068382};
KW   Transferase {ECO:0000313|EMBL:KUP91021.1}.
SQ   SEQUENCE   425 AA;  45251 MW;  18C06946EF20FD8B CRC64;
     MRNSEISTRR DAAISRGVGM QTQVYVERAS GAEVWDVEGK RYIDFAAGIA VVNTGHCHPK
     VMEAVRRQTE AFTHTCHQVL PYENYIRLAE RLNDKVPGDF DKKTVFVTTG AEAVENAIKV
     ARAATGRNAI IAFGGGFHGR TFMGMSLTGK VAPYKKGFGA MMPDVFHVPF PVDLHGISTK
     DALAGIEKLF KADLDPDRVA AIILEPVQGE GGFYPAPADL MRGLRKLCDA HGILLIADEV
     QTGFARTGTL FAMEGYDVPA DITTLAKGLA GGLPLAALTG RAEVMDAAAP GGLGGTYGGN
     PLGIAAAHAV LDVIEEEDLC NRANELGSRL KQRLNAIRSR VPEMVDVRGP GFMIAAEFNT
     ADGKAPNPEM TNAIRAEALS RGLVLLTCGV YGNVIRFLAP LTIPDDIFAE AMDILEASID
     AVKGA
//
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