ID C5CM41_VARPS Unreviewed; 430 AA. AC C5CM41; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 66. DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ACS21300.1}; GN OrderedLocusNames=Vapar_4695 {ECO:0000313|EMBL:ACS21300.1}; OS Variovorax paradoxus (strain S110). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Variovorax. OX NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS21300.1}; RN [1] {ECO:0000313|EMBL:ACS21300.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S110 {ECO:0000313|EMBL:ACS21300.1}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Orwin P., RA Leadbetter J.R., Spain J.C., Han J.I.; RT "Complete sequence of chromosome 1 of Variovorax paradoxus S110."; RL Submitted (JUN-2009) 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001635; ACS21300.1; -; Genomic_DNA. DR AlphaFoldDB; C5CM41; -. DR STRING; 543728.Vapar_4695; -. DR KEGG; vap:Vapar_4695; -. DR eggNOG; COG0160; Bacteria. DR HOGENOM; CLU_016922_10_0_4; -. DR OrthoDB; 3398487at2; -. 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:ACS21300.1}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ACS21300.1}. SQ SEQUENCE 430 AA; 45308 MW; 6CCB5DF036D5C2CD CRC64; MQREPHLSNA ALMARRNAAV ARGVGQAHEI FVSRAANAEV WDVEGRRYID FAGGIAVLNT GHCHPEISAA VKAQVDLYSH TCFQVLAYEP YVELAERLNA LAPGNFAKKS IFLSTGAEAV ENAVKIARAH TRRPGVIAFN GGYHGRTMMT LGLTGKVAPY KLGFGPFPGE VFHALYPNVL HGVSVDDALH SVELLFKNDI EPERVAAFIL EPVQGEGGFY VAPNDFVEGL RALADRHGIL IIADEVQTGA GRTGTWFASE QWPVAPDLIT TAKSMAGGFP ISGVVGRAEV MDAPAPGGLG GTYAGSPIGC AAALAVLKVF DDEQLLARSR ALGGRLTAGL RRIAAGVPAI GDVRGLGAMV AIELFEDGDT ARPDAGLTRR VVAEAARRGL ILLSCGTYGN VIRVLVPLTA SDLLVDEGLA LLADSFAALR //