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Reviewed, UniProtKB/Swiss-Prot P61938 (FMDC_METWO)

Last modified June 16, 2009. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Molybdenum-containing formylmethanofuran dehydrogenase 1 subunit C
    EC=1.2.99.5
Alternative name(s):
    Molybdenum-containing formylmethanofuran dehydrogenase I subunit C
Gene names
Name: fmdC
OrganismMethanobacterium wolfei
Taxonomic identifier145261 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the reversible oxidation of CO2 and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). Can only oxidize formylmethanofuran. This enzyme is oxygen-labile.

Catalytic activity

Formylmethanofuran + H2O + acceptor = CO2 + methanofuran + reduced acceptor.

Cofactor

Molybdenum.

Pathway

One-carbon metabolism; methanogenesis from carbone dioxide; 5,10-methenyl-H(4)MPT from CO(2): step 1/3.

Subunit structure

Consists of five subunits; fmdA, fmdB, fmdC, fmdD, and fmdE.

Induction

By growth on molybdenum, under anaerobic conditions.

Sequence similarities

In the N-terminal section; belongs to the fwdC/fmdC family.

In the C-terminal section; belongs to the molybdenum dinucleotide binding protein family.

Ontologies

Keywords
   Biological processMethanogenesis
   DomainRepeat
   LigandMolybdenum
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processmethanogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionformylmethanofuran dehydrogenase activity

Inferred from electronic annotation. Source: EC

molybdenum ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 400400Molybdenum-containing formylmethanofuran dehydrogenase 1 subunit C
PRO_0000144193

Regions

Repeat76 – 88131
Repeat95 – 107132
Repeat114 – 126133
Repeat140 – 152134
Repeat159 – 171135
Repeat178 – 190136
Repeat197 – 209137
Region76 – 2091347 X 13 AA repeats of [GW]-X-X-M-X-X-G-X-I-X-[IV]-X-G

Sequences

Sequence LengthMass (Da)Tools
P61938-1 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: 41F1C21A25CFBBC3

FASTA40043,321
        10         20         30         40         50         60 
MGFVLVPKSD FQIPLEADTI DPICLKGWDL DEIRSLQVYE GNIKRPLGEF FEIAETSHED 

        70         80         90        100        110        120 
QLIRIDGDVS RVKYIGSGMK SGKIIINGDV GLQLGCEMKG GEIEVNGNVS SWIGMEMHGG 

       130        140        150        160        170        180 
TIKINGNAGD YVGCAYRGEW RGMKGGKIII QGNAGNNIGG GMMAGEIYIG GDAGNFCGIR 

       190        200        210        220        230        240 
MNGGEITVRG DAGRAPGAEM VSGIIKIHGR ISSLLPGFKE ISTFKEDGSL MILFKGDLSE 

       250        260        270        280        290        300 
KNPEGNLYIN YNKNLHILEN ETDEGRVITK KGIKVIYNSG STIREGQIIK GGNKLTDDYI 

       310        320        330        340        350        360 
DECARCCISP EDYKLLGEPE NVVVSSHGNE VVLRAVEDPG IQMGTIFIPR GIWANVLTPP 

       370        380        390        400 
YTESTGSPMY KGVPVYLRKA SQGERILSAE ELVEEYGVGK 

« Hide

References

[1]"The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme."
Hochheimer A., Hedderich R., Thauer R.K.
Arch. Microbiol. 170:389-393(1998) [PubMed: 9818358] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

AJ009689 Genomic DNA. Translation: CAA08787.1.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.99.5. 7575.

Family and domain databases

InterProIPR012048. Formylmethanofuran_DH_csu/dsu.
IPR017550. Formylmethanofuran_DH_suC.
IPR002489. Glu_synthase_C.
IPR006657. MPT_dinuc_bd.
[Graphical view]
Gene3DG3DSA:2.160.20.60. Glu_synthase_C. 1 hit.
PfamPF01493. GXGXG. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
PIRSFPIRSF036633. FmdC_D. 1 hit.
TIGRFAMsTIGR03122. one_C_dehyd_C. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFMDC_METWO
AccessionPrimary (citable) accession number: P61938
Secondary accession number(s): P95294
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: June 16, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents