FMDC_METTM
ID FMDC_METTM Reviewed; 400 AA.
AC P61937; D9PXE6; P95294;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Molybdenum-containing formylmethanofuran dehydrogenase 1 subunit C;
DE EC=1.2.7.12 {ECO:0000250|UniProtKB:Q48943};
DE AltName: Full=Molybdenum-containing formylmethanofuran dehydrogenase I subunit C;
GN Name=fmdC; OrderedLocusNames=MTBMA_c13060;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 242-253; 275-290
RP AND 372-398.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=8954165; DOI=10.1111/j.1432-1033.1996.0156r.x;
RA Hochheimer A., Linder D., Thauer R.K., Hedderich R.;
RT "The molybdenum formylmethanofuran dehydrogenase operon and the tungsten
RT formylmethanofuran dehydrogenase operon from Methanobacterium
RT thermoautotrophicum. Structures and transcriptional regulation.";
RL Eur. J. Biochem. 242:156-162(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
RN [3]
RP PROTEIN SEQUENCE OF 2-18.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=8575452; DOI=10.1111/j.1432-1033.1995.910_a.x;
RA Hochheimer A., Schmitz R.A., Thauer R.K., Hedderich R.;
RT "The tungsten formylmethanofuran dehydrogenase from Methanobacterium
RT thermoautotrophicum contains sequence motifs characteristic for enzymes
RT containing molybdopterin dinucleotide.";
RL Eur. J. Biochem. 234:910-920(1995).
CC -!- FUNCTION: Catalyzes the reversible oxidation of CO(2) and methanofuran
CC (MFR) to N-formylmethanofuran (CHO-MFR). Can only oxidize
CC formylmethanofuran. This enzyme is oxygen-labile.
CC {ECO:0000250|UniProtKB:Q48943}.
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:0000250|UniProtKB:Q48943};
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: Consists of five subunits; FmdA, FmdB, FmdC, FmdD, and FmdE.
CC -!- INDUCTION: By growth on molybdenum, under anaerobic conditions.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FwdC/FmdC family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the molybdenum
CC dinucleotide binding protein family. {ECO:0000305}.
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; X97820; CAA66401.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL58894.1; -; Genomic_DNA.
DR RefSeq; WP_013296115.1; NC_014408.1.
DR AlphaFoldDB; P61937; -.
DR SMR; P61937; -.
DR STRING; 79929.MTBMA_c13060; -.
DR EnsemblBacteria; ADL58894; ADL58894; MTBMA_c13060.
DR GeneID; 9705014; -.
DR KEGG; mmg:MTBMA_c13060; -.
DR PATRIC; fig|79929.8.peg.1270; -.
DR HOGENOM; CLU_661592_0_0_2; -.
DR OMA; SSWIGME; -.
DR OrthoDB; 29442at2157; -.
DR UniPathway; UPA00640; UER00692.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway.
DR CDD; cd00980; FwdC/FmdC; 1.
DR CDD; cd02789; MopB_CT_FmdC-FwdD; 1.
DR Gene3D; 2.160.20.60; -; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041717; FmdC/FwdD_MopB-bd.
DR InterPro; IPR012048; Formylmethanofuran_DH_csu/dsu.
DR InterPro; IPR017550; Formylmethanofuran_DH_suC.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF036633; FmdC_D; 1.
DR SUPFAM; SSF50692; SSF50692; 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..400
FT /note="Molybdenum-containing formylmethanofuran
FT dehydrogenase 1 subunit C"
FT /id="PRO_0000144191"
FT REPEAT 76..88
FT /note="1"
FT REPEAT 95..107
FT /note="2"
FT REPEAT 114..126
FT /note="3"
FT REPEAT 140..152
FT /note="4"
FT REPEAT 159..171
FT /note="5"
FT REPEAT 178..190
FT /note="6"
FT REPEAT 197..209
FT /note="7"
FT REGION 76..209
FT /note="7 X 13 AA repeats of [GW]-X-X-M-X-X-G-X-I-X-[IV]-X-
FT G"
FT CONFLICT 14
FT /note="P -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 21..28
FT /note="RPDLFEGL -> DPICLKGW (in Ref. 1; CAA66401)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 43336 MW; 57A1B8CC71602F9C CRC64;
MGFVLVPKSD FQIPLEADTI RPDLFEGLDL DEIRSLQVYE GNIKRPLGEF FEIAETSHED
QLIRIDGDVS RVKYIGSGMK SGKIIINGDV GLQLGCEMKG GEIEVNGNVS SWIGMEMHGG
TIKINGNAGD YVGCAYRGEW RGMKGGKIII QGNAGNNIGG GMMAGEIYIG GDAGNFCGIR
MNGGEITVRG DAGRAPGAEM VSGIIKIHGR ISSLLPGFKE ISTFKEDGSL MILFKGDLSE
KNPEGNLYIN YNKNLHILEN ETDEGRVITK KGIKVIYNSG STIREGQIIK GGNKLTDDYI
DECARCCISP EDYKLLGEPE NVVVSSHGNE VVLRAVEDPG IQMGTIFIPR GIWANVLTPP
YTESTGSPMY KGVPVYLRKA SQGERILSAE ELVEEYGVGK
