ID GCTB_ACIFE STANDARD; PRT; 266 AA. AC Q59112; DT 15-JUL-1998 (REL. 36, CREATED) DT 15-JUL-1998 (REL. 36, LAST SEQUENCE UPDATE) DT 15-JUL-1998 (REL. 36, LAST ANNOTATION UPDATE) DE GLUTACONATE COA-TRANSFERASE SUBUNIT B (EC 2.8.3.12). GN GCTB. OS ACIDAMINOCOCCUS FERMENTANS. OC BACTERIA; FIRMICUTES; BACILLUS/CLOSTRIDIUM GROUP; SPOROMUSA SUBBRANCH; OC ACIDAMINOCOCCUS. RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. 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 (2.5 ANGSTROMS). 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: ACTIVATES (R)-2- HYDROXYGLUTARATE TO (R)-2- CC HYDROXYGLUTARYL-COA. CC -!- CATALYTIC ACTIVITY: ACETYL-COA + (E)-GLUTACONATE = ACETATE + CC GLUTACONYL-1-COA. CC -!- PATHWAY: GLUTAMATE FERMENTATION. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SUBUNIT: HETEROOCTAMER OF FOUR A AND FOUR B SUBUNITS. 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; G559393; -. DR PDB; 1POI; 18-MAR-98. KW TRANSFERASE; 3D-STRUCTURE. FT ACT_SITE 54 54 SQ SEQUENCE 266 AA; 29166 MW; FB2B70BF CRC32; 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 //