ID Q129G6_POLSJ Unreviewed; 430 AA. AC Q129G6; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 27-MAR-2024, entry version 91. DE SubName: Full=4-aminobutyrate aminotransferase apoenzyme {ECO:0000313|EMBL:ABE44826.1}; DE EC=2.6.1.19 {ECO:0000313|EMBL:ABE44826.1}; GN OrderedLocusNames=Bpro_2912 {ECO:0000313|EMBL:ABE44826.1}; OS Polaromonas sp. (strain JS666 / ATCC BAA-500). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Polaromonas. OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE44826.1, ECO:0000313|Proteomes:UP000001983}; RN [1] {ECO:0000313|Proteomes:UP000001983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983}; RX PubMed=18723656; DOI=10.1128/AEM.00197-08; RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S., RA Stothard P., Coleman N.V.; RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of RT relevance to biotechnology."; RL Appl. Environ. Microbiol. 74:6405-6416(2008). 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; CP000316; ABE44826.1; -; Genomic_DNA. DR RefSeq; WP_011483824.1; NC_007948.1. DR AlphaFoldDB; Q129G6; -. DR STRING; 296591.Bpro_2912; -. DR KEGG; pol:Bpro_2912; -. DR eggNOG; COG0160; Bacteria. DR HOGENOM; CLU_016922_10_0_4; -. DR OrthoDB; 3398487at2; -. DR Proteomes; UP000001983; 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:ABE44826.1}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, KW ECO:0000256|RuleBase:RU003560}; KW Reference proteome {ECO:0000313|Proteomes:UP000001983}; KW Transferase {ECO:0000313|EMBL:ABE44826.1}. SQ SEQUENCE 430 AA; 45663 MW; ACB4D8A0D6836497 CRC64; MPSNQPTTNA ALMARRKAAV ARGVGQTHEI FVSRARNAEF WDVEDRRYID FAGGIAVLNT GHLHPQVIAA VKTQLDLYTH TCFQVVAYEP YVELSEKLNA LAPGNFAKKT LLLSTGAEAV ENAVKVARAY TKRPGIIAFT GGYHGRTNMT LGMTGKVAPY KLGFGPFPGE VFHALYPNVL HGVSVDQALH SVELILKNDI EAERVAAFIL EPVQGEGGFY IAPPEFITGL KALADRHGIL LIADEVQTGA GRTGTWFASE QWPVAPDLIT TAKSMAGGFP ISGLVGRADV MDAPAPGGLG GTYAGSPIGC AAALAVLKVF EDEKLLERSK ALGAHLLKGL RAIAEKEVTI GDVRGLGAMV AMELFENGDV ARPNAALTQR VVAEAARRGL ILLSCGTYGN VIRILVPLTA NDALLDEGLK ILADSFSALR //