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 07-NOV-2018, entry version 110. 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 / VR4). OC Bacteria; Firmicutes; Negativicutes; Acidaminococcales; OC Acidaminococcaceae; Acidaminococcus. OX NCBI_TaxID=591001; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-19 AND RP 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 RT at 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 / 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., RA Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Brettin T., RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., RA 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 RT crystal 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 CC to (R)-2-hydroxyglutarate and related compounds like glutaconate. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + (E)-glutaconate = acetate + CC glutaconyl-1-CoA. CC -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via CC hydroxyglutarate pathway; crotonoyl-CoA from L-glutamate: step CC 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 CC family. {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; NC_013740.1. DR PDB; 1POI; X-ray; 2.50 A; B/D=3-262. DR PDBsum; 1POI; -. DR ProteinModelPortal; Q59112; -. DR SMR; Q59112; -. DR DIP; DIP-6201N; -. DR IntAct; Q59112; 1. DR STRING; 591001.Acfer_1818; -. DR EnsemblBacteria; ADB48172; ADB48172; Acfer_1818. DR KEGG; afn:Acfer_1818; -. DR eggNOG; ENOG4107UHT; Bacteria. DR eggNOG; COG2057; LUCA. DR HOGENOM; HOG000221246; -. DR KO; K01040; -. DR OMA; KTHAPNL; -. DR OrthoDB; POG091H036G; -. DR BioCyc; AFER591001:G1GH7-1881-MONOMER; -. 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 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; SSF100950; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; KW Reference proteome; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7957258}. FT CHAIN 2 266 Glutaconate CoA-transferase subunit B. FT /FTId=PRO_0000157930. FT ACT_SITE 54 54 FT HELIX 9 18 {ECO:0000244|PDB:1POI}. FT STRAND 26 28 {ECO:0000244|PDB:1POI}. FT HELIX 33 43 {ECO:0000244|PDB:1POI}. FT STRAND 50 53 {ECO:0000244|PDB:1POI}. FT TURN 54 56 {ECO:0000244|PDB:1POI}. FT STRAND 57 60 {ECO:0000244|PDB:1POI}. FT HELIX 72 75 {ECO:0000244|PDB:1POI}. FT STRAND 77 81 {ECO:0000244|PDB:1POI}. FT HELIX 84 97 {ECO:0000244|PDB:1POI}. FT STRAND 102 106 {ECO:0000244|PDB:1POI}. FT STRAND 109 111 {ECO:0000244|PDB:1POI}. FT STRAND 120 123 {ECO:0000244|PDB:1POI}. FT STRAND 125 131 {ECO:0000244|PDB:1POI}. FT HELIX 138 144 {ECO:0000244|PDB:1POI}. FT STRAND 147 150 {ECO:0000244|PDB:1POI}. FT TURN 155 157 {ECO:0000244|PDB:1POI}. FT HELIX 176 179 {ECO:0000244|PDB:1POI}. FT STRAND 188 193 {ECO:0000244|PDB:1POI}. FT STRAND 196 200 {ECO:0000244|PDB:1POI}. FT TURN 202 204 {ECO:0000244|PDB:1POI}. FT STRAND 207 212 {ECO:0000244|PDB:1POI}. FT HELIX 218 223 {ECO:0000244|PDB:1POI}. FT HELIX 242 250 {ECO:0000244|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 //