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Database: UniProt/TrEMBL
Entry: A0A165SLW2_9RHOB
LinkDB: A0A165SLW2_9RHOB
Original site: A0A165SLW2_9RHOB 
ID   A0A165SLW2_9RHOB        Unreviewed;       429 AA.
AC   A0A165SLW2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AMY69283.1};
GN   ORFNames=AKL17_2036 {ECO:0000313|EMBL:AMY69283.1};
OS   Frigidibacter mobilis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Frigidibacter.
OX   NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY69283.1, ECO:0000313|Proteomes:UP000076128};
RN   [1] {ECO:0000313|EMBL:AMY69283.1, ECO:0000313|Proteomes:UP000076128}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RA   Geng S., Pan X., Wu X.;
RT   "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT   oilfield in Xinjiang.";
RL   Submitted (SEP-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}.
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DR   EMBL; CP012661; AMY69283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165SLW2; -.
DR   STRING; 1335048.AKL17_2036; -.
DR   KEGG; daa:AKL17_2036; -.
DR   PATRIC; fig|1335048.3.peg.2125; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000076128; 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:AMY69283.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AMY69283.1}.
SQ   SEQUENCE   429 AA;  45333 MW;  03FCDD0D25348E23 CRC64;
     MTHSTITDAA LSARRTAAIA RGVGVTTQVY ADRAENAEIW DKTGTRYIDF AAGIAVVNTG
     HRHPRVIAAV KAQLDRFTHT CHQVVPYENY VTLAERLNDK VPGDFAKKTL FATTGAEAVE
     NAVKIARHHT GRAAVIAFAG GFHGRTFMGM ALTGKVQPYK AGFGPMMADV WHLPFPVALQ
     GVTAEDSLAA LDRLFKADLE PTRVAAILVE PVQGEGGFYE VPAGFMASLR AICDTHGIVL
     IADEVQTGFA RTGKLFAMEH HGVAADITTM AKGLGGGLPI SAVTGRAEIM DSPNPGGLGG
     TYAGNPLAIA AANAVLDVIE EEQLCDRAMR LGQRLKQRLA GLQEAVPQIA DIRGPGFMNA
     VEFAVPGTGA PDAGFANRVR EEALSRGLIL LTCGVYGNVI RFLAPLTIPD AVFDEALEIL
     EASVLAARG
//
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