ID   FMDC_METBF              Reviewed;         301 AA.
AC   Q48943; Q46CY9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Molybdenum-containing formylmethanofuran dehydrogenase 1 subunit C;
DE            EC=1.2.99.5;
DE   AltName: Full=Molybdenum-containing formylmethanofuran dehydrogenase I subunit C;
GN   Name=fmdC; OrderedLocusNames=Mbar_A1290;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-23.
RX   MEDLINE=96184912; PubMed=8617280;
RX   DOI=10.1111/j.1432-1033.1996.t01-1-00309.x;
RA   Vorholt J.A., Vaupel M., Thauer R.K.;
RT   "A polyferredoxin with eight [4Fe-4S] clusters as a subunit of
RT   molybdenum formylmethanofuran dehydrogenase from Methanosarcina
RT   barkeri.";
RL   Eur. J. Biochem. 236:309-317(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
RN   [3]
RP   SUBSTRATE SPECIFICITY.
RX   MEDLINE=94170797; PubMed=8125106;
RX   DOI=10.1111/j.1432-1033.1994.tb18646.x;
RA   Bertram P.A., Karrach M., Schmitz R.A., Boecher R., Albracht S.P.J.,
RA   Thauer R.K.;
RT   "Formylmethanofuran dehydrogenases from methanogenic Archaea.
RT   Substrate specificity, EPR properties and reversible inactivation by
RT   cyanide of the molybdenum or tungsten iron-sulfur proteins.";
RL   Eur. J. Biochem. 220:477-484(1994).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of CO(2) and
CC       methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). Can use N-
CC       furfurylformamide, formamide, N-methylformamide, and formate as
CC       substrates. This enzyme is oxygen-labile.
CC   -!- CATALYTIC ACTIVITY: Formylmethanofuran + H(2)O + acceptor = CO(2)
CC       + methanofuran + reduced acceptor.
CC   -!- COFACTOR: Molybdenum.
CC   -!- ENZYME REGULATION: Inactivated by cyanide.
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from carbone
CC       dioxide; 5,10-methenyl-H(4)MPT from CO(2): step 1/3.
CC   -!- SUBUNIT: This enzyme is composed of six subunits; fmdA (65 kDa),
CC       fmdB (50 kDa), fmdC (34 kDa), fmdD (17 kDa), fmdE (23 kDa) and
CC       fmdF (37 kDa).
CC   -!- INDUCTION: By growth on molybdenum, under anaerobic conditions.
CC   -!- SIMILARITY: Belongs to the fwdC/fmdC family.
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DR   EMBL; X93084; CAA63631.1; -; Genomic_DNA.
DR   EMBL; CP000099; AAZ70253.1; -; Genomic_DNA.
DR   PIR; S62199; S62199.
DR   RefSeq; YP_304833.1; -.
DR   TCDB; 3.D.8.1.2; Na+- or H+-pumping formyl methanofuran dehydrogenase (FMF-DH) family.
DR   GeneID; 3627699; -.
DR   GenomeReviews; CP000099_GR; Mbar_A1290.
DR   KEGG; mba:Mbar_A1290; -.
DR   NMPDR; fig|269797.3.peg.1295; -.
DR   HOGENOM; Q48943; -.
DR   OMA; Q48943; VWANVIV.
DR   BioCyc; MBAR269797:MBAR_A1290-MON; -.
DR   GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:EC.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR017550; Formylmethanofuran_DH_suC.
DR   InterPro; IPR002489; Glu_synthase_C.
DR   Gene3D; G3DSA:2.160.20.60; Glu_synthase_C; 1.
DR   Pfam; PF01493; GXGXG; 1.
DR   TIGRFAMs; TIGR03122; one_C_dehyd_C; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Methanogenesis;
KW   Molybdenum; Oxidoreductase; Repeat.
FT   CHAIN         1    301       Molybdenum-containing formylmethanofuran
FT                                dehydrogenase 1 subunit C.
FT                                /FTId=PRO_0000144190.
FT   REPEAT      112    124       1.
FT   REPEAT      131    143       2.
FT   REPEAT      150    162       3.
FT   REPEAT      176    188       4.
FT   REPEAT      195    207       5.
FT   REPEAT      214    226       6.
FT   REPEAT      233    245       7.
FT   REGION      112    245       7 X 13 AA repeats of [GW]-X-X-[MQ]-X-X-G-
FT                                X-[IL]-X-[IV]-X-G.
FT   CONFLICT      2      2       Missing (in Ref. 1; AA sequence).
SQ   SEQUENCE   301 AA;  31551 MW;  D871C80B50AC000D CRC64;
     MTEGVLINEN EVESKLEAVI KPGSFTGENA GEMAEVILIP KKAIDIKLEA DVITPDSFAG
     KSAEEIGKLS VWQGPKTYPL SEFFEVTGNG GSSAAETLIR IKGDAMRIKR IGESMSAGKI
     EIEGSAGMHV GTGMKGGELV VYGDADSWAG MEMTGGLLHI KGNAGDHVGC AYRGKWHGMK
     GGRIVIEGSA RHQLGGGMDG GEILVEGDVK SFCGIRQNGG LIFVKGSALR GVGAEMAGGT
     IVIGGKIERF SPGFEFVSME NSITSGEVEL IGEFKKFTGD YAISKRAKGA LYVVADTNPE
     L
//