ID GCTA_ACIFV Reviewed; 320 AA. AC Q59111; D2RM71; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 135. DE RecName: Full=Glutaconate CoA-transferase subunit A; DE EC=2.8.3.12; DE AltName: Full=GCT large subunit; GN Name=gctA; OrderedLocusNames=Acfer_1819; OS Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP OS 106432 / VR4). OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae; OC Acidaminococcus. OX NCBI_TaxID=591001; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-13. RX PubMed=7957258; DOI=10.1111/j.1432-1033.1994.tb20024.x; RA Mack M., Bendrat K., Zelder O., Eckel E., Linder D., Buckel W.; RT "Location of the two genes encoding glutaconate coenzyme A-transferase at RT the beginning of the hydroxyglutarate operon in Acidaminococcus RT fermentans."; RL Eur. J. Biochem. 226:41-51(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4; RX PubMed=21304687; DOI=10.4056/sigs.1002553; RA Chang Y.J., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Han C., RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Liolios K., RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M., RA Hauser L., Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Acidaminococcus fermentans type strain RT (VR4)."; RL Stand. Genomic Sci. 3:1-14(2010). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS). RX PubMed=9083111; DOI=10.1016/s0969-2126(97)00198-6; RA Jacob U., Mack M., Clausen T., Huber R., Buckel W., Messerschmidt A.; RT "Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal RT structure reveals homology with other CoA-transferases."; RL Structure 5:415-426(1997). CC -!- FUNCTION: Catalyzes the transfer of the CoA moiety from acetyl-CoA to CC (R)-2-hydroxyglutarate and related compounds like glutaconate. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + trans-glutaconate = (2E)-glutaconyl-CoA + CC acetate; Xref=Rhea:RHEA:23208, ChEBI:CHEBI:30089, ChEBI:CHEBI:36460, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57353; EC=2.8.3.12; CC -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via CC hydroxyglutarate pathway; crotonoyl-CoA from L-glutamate: step 3/5. CC -!- SUBUNIT: Heterooctamer of four A and four B subunits. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase subunit A family. CC {ECO:0000305}. 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; X81440; CAA57199.1; -; Genomic_DNA. DR EMBL; CP001859; ADB48173.1; -; Genomic_DNA. DR PIR; S51051; S51051. DR RefSeq; WP_012939156.1; NZ_CP085936.1. DR PDB; 1POI; X-ray; 2.50 A; A/C=2-318. DR PDBsum; 1POI; -. DR AlphaFoldDB; Q59111; -. DR SMR; Q59111; -. DR DIP; DIP-6200N; -. DR IntAct; Q59111; 1. DR STRING; 591001.Acfer_1819; -. DR GeneID; 78335515; -. DR KEGG; afn:Acfer_1819; -. DR eggNOG; COG1788; Bacteria. DR HOGENOM; CLU_049557_0_0_9; -. DR OrthoDB; 9777193at2; -. DR BioCyc; MetaCyc:MONOMER-1028; -. DR BRENDA; 2.8.3.12; 85. DR SABIO-RK; Q59111; -. DR UniPathway; UPA00533; UER00686. DR EvolutionaryTrace; Q59111; -. DR Proteomes; UP000001902; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0018730; F:glutaconate CoA-transferase activity; IEA:UniProtKB-EC. DR GO; GO:0019552; P:glutamate catabolic process via 2-hydroxyglutarate; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.30.40; -; 1. DR Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 1. DR InterPro; IPR004165; CoA_trans_fam_I. DR InterPro; IPR037171; NagB/RpiA_transferase-like. DR Pfam; PF01144; CoA_trans; 1. DR SMART; SM00882; CoA_trans; 1. DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome; KW Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:7957258" FT CHAIN 2..320 FT /note="Glutaconate CoA-transferase subunit A" FT /id="PRO_0000157927" FT HELIX 7..14 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 20..23 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 33..41 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 47..50 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 56..63 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 67..75 FT /evidence="ECO:0007829|PDB:1POI" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 81..83 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 85..93 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 96..100 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 103..115 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 118..123 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 129..132 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 138..142 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 153..157 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 160..169 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 174..183 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 198..204 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 205..215 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 218..222 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 225..227 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 232..234 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 237..240 FT /evidence="ECO:0007829|PDB:1POI" FT TURN 242..247 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 248..250 FT /evidence="ECO:0007829|PDB:1POI" FT TURN 251..253 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 258..267 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 271..281 FT /evidence="ECO:0007829|PDB:1POI" FT TURN 282..284 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 288..295 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 297..301 FT /evidence="ECO:0007829|PDB:1POI" FT TURN 307..309 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 315..317 FT /evidence="ECO:0007829|PDB:1POI" SQ SEQUENCE 320 AA; 35722 MW; C51B214FE17FEB46 CRC64; MSKVMTLKDA IAKYVHSGDH IALGGFTTDR KPYAAVFEIL RQGITDLTGL GGAAGGDWDM LIGNGRVKAY INCYTANSGV TNVSRRFRKW FEAGKLTMED YSQDVIYMMW HAAALGLPFL PVTLMQGSGL TDEWGISKEV RKTLDKVPDD KFKYIDNPFK PGEKVVAVPV PQVDVAIIHA QQASPDGTVR IWGGKFQDVD IAEAAKYTIV TCEEIISDEE IRRDPTKNDI PGMCVDAVVL APYGAHPSQC YGLYDYDNPF LKVYDKVSKT QEDFDAFCKE WVFDLKDHDE YLNKLGATRL INLKVVPGLG YHIDMTKEDK //