ID PORB_METTM Reviewed; 10 AA. AC P80901; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 04-NOV-2008, entry version 28. DE RecName: Full=Pyruvate synthase subunit porB; DE EC=1.2.7.1; DE AltName: Full=Pyruvate oxidoreductase beta chain; DE Short=POR; DE AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit beta; DE Flags: Fragment; GN Name=porB; OS Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133). OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; OC Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=79929; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=97261844; PubMed=9108258; RA Tersteegen A., Linder D., Thauer R.K., Hedderich R.; RT "Structures and functions of four anabolic 2-oxoacid oxidoreductases RT in Methanobacterium thermoautotrophicum."; RL Eur. J. Biochem. 244:862-868(1997). CC -!- CATALYTIC ACTIVITY: Pyruvate + CoA + 2 oxidized ferredoxin = CC acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 10.0; CC Temperature dependence: CC Optimum temperature is 80 degrees Celsius; CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one CC gamma chain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR GO; GO:0019164; F:pyruvate synthase activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Direct protein sequencing; Oxidoreductase. FT CHAIN 1 >10 Pyruvate synthase subunit porB. FT /FTId=PRO_0000099905. FT NON_TER 10 10 SQ SEQUENCE 10 AA; 1236 MW; 167011DAF6DB0760 CRC64; XXIPEQXFLR //