ID GCTB_ACIFE STANDARD; PRT; 265 AA. AC Q59112; DT 15-JUL-1998 (Rel. 36, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE GLUTACONATE COA-TRANSFERASE SUBUNIT B (EC 2.8.3.12) (GCT SMALL DE SUBUNIT). GN GCTB. OS Acidaminococcus fermentans. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Sporomusa subbranch; OC Acidaminococcus. RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 1-18 AND 43-65. RC STRAIN=ATCC 25085; RX MEDLINE; 95045599. RA Mack M., Bendrat K., Zelder O., Eckel E., Linder D., Buckel W.; RT "Location of the two genes encoding glutaconate coenzyme RT A-transferase at the beginning of the hydroxyglutarate operon in RT Acidaminococcus fermentans."; RL Eur. J. Biochem. 226:41-51(1994). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS). RC STRAIN=ATCC 25085; RX MEDLINE; 97238937. 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: GLUTAMATE FERMENTATION. CC -!- SUBUNIT: HETEROOCTAMER OF FOUR A AND FOUR B SUBUNITS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE GLUTACONATE COA-TRANSFERASE SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; -. DR PDB; 1POI; 18-MAR-98. KW Transferase; 3D-structure. FT INIT_MET 0 0 FT ACT_SITE 53 53 SQ SEQUENCE 265 AA; 29035 MW; 1E7FF61B42162FB4 CRC64; ADYTNYTNKE MQAVTIAKQI KNGQVVTVGT GLPLIGASVA KRVYAPDCHI IVESGLMDCS PVEVPRSVGD LRFMAHCGCI WPNVRFVGFE INEYLHKANR LIAFIGGAQI DPYGNVNSTS IGDYHHPKTR FTGSGGANGI ATYSNTIIMM QHEKRRFMNK IDYVTSPGWI DGPGGRERLG LPGDVGPQLV VTDKGILKFD EKTKRMYLAA YYPTSSPEDV LENTGFDLDV SKAVELEAPD PAVIKLIREE IDPGQAFIQV PTEAK //