ID A1R958_PAEAT Unreviewed; 456 AA. AC A1R958; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 115. DE SubName: Full=4-aminobutyrate transaminase {ECO:0000313|EMBL:ABM08874.1}; DE EC=2.6.1.19 {ECO:0000313|EMBL:ABM08874.1}; GN Name=gabT {ECO:0000313|EMBL:ABM08874.1}; GN OrderedLocusNames=AAur_3069 {ECO:0000313|EMBL:ABM08874.1}; OS Paenarthrobacter aurescens (strain TC1). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Paenarthrobacter. OX NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM08874.1, ECO:0000313|Proteomes:UP000000637}; RN [1] {ECO:0000313|EMBL:ABM08874.1, ECO:0000313|Proteomes:UP000000637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TC1 {ECO:0000313|EMBL:ABM08874.1, RC ECO:0000313|Proteomes:UP000000637}; RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214; RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B., RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H., RA Wackett L.P., Nelson K.E., Sadowsky M.J.; RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter RT aurescens TC1."; RL PLoS Genet. 2:2094-2106(2006). RN [2] {ECO:0007829|PDB:4ATP, ECO:0007829|PDB:4ATQ} RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS), AND PYRIDOXAL PHOSPHATE AT LYS-295. RX PubMed=23027742; DOI=10.1107/S1744309112030023; RA Bruce H., Nguyen Tuan A., Mangas Sanchez J., Leese C., Hopwood J., Hyde R., RA Hart S., Turkenburg J.P., Grogan G.; RT "Structures of a gamma-aminobutyrate (GABA) transaminase from the s- RT triazine-degrading organism Arthrobacter aurescens TC1 in complex with PLP RT and with its external aldimine PLP-GABA adduct."; RL Acta Crystallogr. F Struct. Biol. Commun. 68:1175-1180(2012). 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; CP000474; ABM08874.1; -; Genomic_DNA. DR RefSeq; WP_011775705.1; NC_008711.1. DR PDB; 4ATP; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-456. DR PDB; 4ATQ; X-ray; 2.75 A; A/B/C/D/E/F/G/H/I/J/K/L=1-456. DR PDBsum; 4ATP; -. DR PDBsum; 4ATQ; -. DR AlphaFoldDB; A1R958; -. DR SMR; A1R958; -. DR STRING; 290340.AAur_3069; -. DR KEGG; aau:AAur_3069; -. DR eggNOG; COG0160; Bacteria. DR HOGENOM; CLU_016922_10_0_11; -. DR OrthoDB; 9801052at2; -. DR Proteomes; UP000000637; 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 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4ATP, ECO:0007829|PDB:4ATQ}; KW Aminotransferase {ECO:0000313|EMBL:ABM08874.1}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ABM08874.1}. FT BINDING 134 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4ATQ" FT BINDING 134 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ATP" FT BINDING 135 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ATP" FT BINDING 135 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4ATQ" FT BINDING 269 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ATP" FT BINDING 295 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_label="1" FT /ligand_note="covalent" FT /evidence="ECO:0007829|PDB:4ATP" FT BINDING 324 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4ATQ" FT BINDING 324 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4ATP" SQ SEQUENCE 456 AA; 47557 MW; 7318C673C41B1ECB CRC64; MTTTANELSY RIEQKRNING AFPGPKSQAL AERRSAVVAA GVASGVPVYV EDADGGIIRD VDGNSFIDLG SGIAVTSVGA SDPAVVAAVQ EAAAHFTHTC FMVTPYEGYV AVAEQLNRLT PGDHAKRTVL FNSGAEAVEN AVKVARLATG RDAVVAFDHA YHGRTNLTMA LTAKAMPYKT NFGPFAPEVY RMPMSYPFRE ENPEITGAEA AKRAITMIEK QIGGDQVAAI IIEPIQGEGG FIVPAEGFLP ALSEWAKEKG IVFIADEVQS GFCRTGEWFA VDHEGVVPDI ITMAKGIAGG LPLSAITGRA DLLDAVHPGG LGGTYGGNPV ACAAALAAID TMEQHDLNGR ARHIEELALG KLRELAAELS AGGGSVVGDI RGRGAMLAIE LVQPGSKEPN AELTKAVAAA CLKEGVIILT CGTYGNVIRL LPPLVISDEL LIDGLEVLAA AIKAHA //