ID GCTB_ACIFV Reviewed; 266 AA. AC Q59112; D2RM70; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-NOV-2024, entry version 135. DE RecName: Full=Glutaconate CoA-transferase subunit B; DE EC=2.8.3.12; DE AltName: Full=GCT small subunit; GN Name=gctB; OrderedLocusNames=Acfer_1818; 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 2-19 AND 44-66. 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=trans-glutaconate + acetyl-CoA = (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 B 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; CAA57200.1; -; Genomic_DNA. DR EMBL; CP001859; ADB48172.1; -; Genomic_DNA. DR PIR; S51052; S51052. DR RefSeq; WP_012939155.1; NZ_CP085936.1. DR PDB; 1POI; X-ray; 2.50 A; B/D=3-262. DR PDBsum; 1POI; -. DR AlphaFoldDB; Q59112; -. DR SMR; Q59112; -. DR DIP; DIP-6201N; -. DR IntAct; Q59112; 1. DR STRING; 591001.Acfer_1818; -. DR GeneID; 78335514; -. DR KEGG; afn:Acfer_1818; -. DR eggNOG; COG2057; Bacteria. DR HOGENOM; CLU_069088_0_0_9; -. DR OrthoDB; 9805230at2; -. DR BioCyc; MetaCyc:MONOMER-1029; -. DR BRENDA; 2.8.3.12; 85. DR SABIO-RK; Q59112; -. DR UniPathway; UPA00533; UER00686. DR EvolutionaryTrace; Q59112; -. 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; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 1. DR InterPro; IPR004165; CoA_trans_fam_I. DR InterPro; IPR037171; NagB/RpiA_transferase-like. DR PANTHER; PTHR43293; ACETATE COA-TRANSFERASE YDIF; 1. DR PANTHER; PTHR43293:SF3; CHOLESTEROL RING-CLEAVING HYDROLASE IPDB SUBUNIT; 1. 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..266 FT /note="Glutaconate CoA-transferase subunit B" FT /id="PRO_0000157930" FT ACT_SITE 54 FT HELIX 9..18 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 33..43 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 50..53 FT /evidence="ECO:0007829|PDB:1POI" FT TURN 54..56 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 72..75 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 84..97 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 102..106 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 120..123 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 125..131 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 138..144 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 147..150 FT /evidence="ECO:0007829|PDB:1POI" FT TURN 155..157 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 176..179 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 188..193 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 196..200 FT /evidence="ECO:0007829|PDB:1POI" FT TURN 202..204 FT /evidence="ECO:0007829|PDB:1POI" FT STRAND 207..212 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 218..223 FT /evidence="ECO:0007829|PDB:1POI" FT HELIX 242..250 FT /evidence="ECO:0007829|PDB:1POI" SQ SEQUENCE 266 AA; 29166 MW; 1E691B864237A784 CRC64; MADYTNYTNK EMQAVTIAKQ IKNGQVVTVG TGLPLIGASV AKRVYAPDCH IIVESGLMDC SPVEVPRSVG DLRFMAHCGC IWPNVRFVGF EINEYLHKAN RLIAFIGGAQ IDPYGNVNST SIGDYHHPKT RFTGSGGANG IATYSNTIIM MQHEKRRFMN KIDYVTSPGW IDGPGGRERL GLPGDVGPQL VVTDKGILKF DEKTKRMYLA AYYPTSSPED VLENTGFDLD VSKAVELEAP DPAVIKLIRE EIDPGQAFIQ VPTEAK //