FMDC_METBF
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 25-MAY-2022, entry version 133.
DE RecName: Full=Molybdenum-containing formylmethanofuran dehydrogenase 1 subunit C;
DE EC=1.2.7.12 {ECO:0000269|PubMed:8125106};
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; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-23.
RX PubMed=8617280; 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 molybdenum
RT formylmethanofuran dehydrogenase from Methanosarcina barkeri.";
RL Eur. J. Biochem. 236:309-317(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., 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 FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=8125106; 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. Substrate
RT specificity, EPR properties and reversible inactivation by cyanide of the
RT molybdenum or tungsten iron-sulfur proteins.";
RL Eur. J. Biochem. 220:477-484(1994).
CC -!- FUNCTION: Catalyzes the reversible oxidation of CO(2) and methanofuran
CC (MFR) to N-formylmethanofuran (CHO-MFR). Can use N-furfurylformamide,
CC formamide, N-methylformamide, and formate as substrates. This enzyme is
CC oxygen-labile. {ECO:0000269|PubMed:8125106}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-[ferredoxin]
CC = CO2 + H(+) + methanofuran + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:19841, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57727,
CC ChEBI:CHEBI:58151; EC=1.2.7.12;
CC Evidence={ECO:0000269|PubMed:8125106};
CC -!- ACTIVITY REGULATION: Inactivated by cyanide.
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10-
CC methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 1/3.
CC -!- SUBUNIT: This enzyme is composed of six subunits; FmdA (65 kDa), FmdB
CC (50 kDa), FmdC (34 kDa), FmdD (17 kDa), FmdE (23 kDa) and FmdF (37
CC kDa).
CC -!- INDUCTION: By growth on molybdenum, under anaerobic conditions.
CC -!- SIMILARITY: Belongs to the FwdC/FmdC family. {ECO:0000305}.
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DR EMBL; X93084; CAA63631.1; -; Genomic_DNA.
DR EMBL; CP000099; AAZ70253.1; -; Genomic_DNA.
DR PIR; S62199; S62199.
DR AlphaFoldDB; Q48943; -.
DR SMR; Q48943; -.
DR STRING; 269797.Mbar_A1290; -.
DR TCDB; 3.D.8.1.2; the na(+)- or h(+)-pumping formyl methanofuran dehydrogenase (fmf-dh) family.
DR EnsemblBacteria; AAZ70253; AAZ70253; Mbar_A1290.
DR KEGG; mba:Mbar_A1290; -.
DR eggNOG; arCOG00097; Archaea.
DR HOGENOM; CLU_072248_0_0_2; -.
DR OMA; NMHPEDY; -.
DR UniPathway; UPA00640; UER00692.
DR GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway.
DR CDD; cd00980; FwdC/FmdC; 1.
DR Gene3D; 2.160.20.60; -; 2.
DR InterPro; IPR017550; Formylmethanofuran_DH_suC.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR Pfam; PF01493; GXGXG; 1.
DR SUPFAM; SSF69336; SSF69336; 1.
DR TIGRFAMs; TIGR03122; one_C_dehyd_C; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Methanogenesis; Oxidoreductase; Repeat.
FT CHAIN 1..301
FT /note="Molybdenum-containing formylmethanofuran
FT dehydrogenase 1 subunit C"
FT /id="PRO_0000144190"
FT REPEAT 112..124
FT /note="1"
FT REPEAT 131..143
FT /note="2"
FT REPEAT 150..162
FT /note="3"
FT REPEAT 176..188
FT /note="4"
FT REPEAT 195..207
FT /note="5"
FT REPEAT 214..226
FT /note="6"
FT REPEAT 233..245
FT /note="7"
FT REGION 112..245
FT /note="7 X 13 AA repeats of [GW]-X-X-[MQ]-X-X-G-X-[IL]-X-
FT [IV]-X-G"
FT CONFLICT 2
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
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
