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
//