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Reviewed, UniProtKB/Swiss-Prot Q48943 (FMDC_METBF)

Last modified November 3, 2009. Version 66. 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
Ordered Locus Names: Mbar_A1290
OrganismMethanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP]
Taxonomic identifier269797 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length301 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the reversible oxidation of CO2 and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). Can use N-furfurylformamide, formamide, N-methylformamide, and formate as substrates. This enzyme is oxygen-labile.

Catalytic activity

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

Cofactor

Molybdenum.

Enzyme regulation

Inactivated by cyanide.

Pathway

One-carbon metabolism; methanogenesis from CO(2); 5,10-methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 1/3.

Subunit structure

This enzyme is composed of six subunits; fmdA (65 kDa), fmdB (50 kDa), fmdC (34 kDa), fmdD (17 kDa), fmdE (23 kDa) and fmdF (37 kDa).

Induction

By growth on molybdenum, under anaerobic conditions.

Sequence similarities

Belongs to the fwdC/fmdC family.

Ontologies

Keywords
   Biological processMethanogenesis
   DomainRepeat
   LigandMolybdenum
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
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 – 301301Molybdenum-containing formylmethanofuran dehydrogenase 1 subunit C
PRO_0000144190

Regions

Repeat112 – 124131
Repeat131 – 143132
Repeat150 – 162133
Repeat176 – 188134
Repeat195 – 207135
Repeat214 – 226136
Repeat233 – 245137
Region112 – 2451347 X 13 AA repeats of [GW]-X-X-[MQ]-X-X-G-X-[IL]-X-[IV]-X-G

Experimental info

Sequence conflict21Missing AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q48943-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D871C80B50AC000D

FASTA30131,551
        10         20         30         40         50         60 
MTEGVLINEN EVESKLEAVI KPGSFTGENA GEMAEVILIP KKAIDIKLEA DVITPDSFAG 

        70         80         90        100        110        120 
KSAEEIGKLS VWQGPKTYPL SEFFEVTGNG GSSAAETLIR IKGDAMRIKR IGESMSAGKI 

       130        140        150        160        170        180 
EIEGSAGMHV GTGMKGGELV VYGDADSWAG MEMTGGLLHI KGNAGDHVGC AYRGKWHGMK 

       190        200        210        220        230        240 
GGRIVIEGSA RHQLGGGMDG GEILVEGDVK SFCGIRQNGG LIFVKGSALR GVGAEMAGGT 

       250        260        270        280        290        300 
IVIGGKIERF SPGFEFVSME NSITSGEVEL IGEFKKFTGD YAISKRAKGA LYVVADTNPE 


L 

« Hide

References

« Hide 'large scale' references
[1]"A polyferredoxin with eight [4Fe-4S] clusters as a subunit of molybdenum formylmethanofuran dehydrogenase from Methanosarcina barkeri."
Vorholt J.A., Vaupel M., Thauer R.K.
Eur. J. Biochem. 236:309-317(1996) [PubMed: 8617280] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-23.
[2]"The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes."
Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.
J. Bacteriol. 188:7922-7931(2006) [PubMed: 16980466] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Formylmethanofuran dehydrogenases from methanogenic Archaea. Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulfur proteins."
Bertram P.A., Karrach M., Schmitz R.A., Boecher R., Albracht S.P.J., Thauer R.K.
Eur. J. Biochem. 220:477-484(1994) [PubMed: 8125106] [Abstract]
Cited for: SUBSTRATE SPECIFICITY.

Cross-references

Sequence databases

X93084 Genomic DNA. Translation: CAA63631.1.
CP000099 Genomic DNA. Translation: AAZ70253.1.
PIRS62199.
RefSeqYP_304833.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ48943.

Protein family/group databases

TCDB3.D.8.1.2. Na+- or H+-pumping formyl methanofuran dehydrogenase (FMF-DH) family.

Genome annotation databases

GeneID3627699.
GenomeReviewsGene locus Mbar_A1290 in contig CP000099_GR.
KEGGmba:Mbar_A1290.
NMPDRfig|269797.3.peg.1295.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ48943.
OMAVWANVIV.

Enzyme and pathway databases

BioCycMBAR269797:MBAR_A1290-MON.

Family and domain databases

InterProIPR017550. Formylmethanofuran_DH_suC.
IPR002489. Glu_synthase_C.
[Graphical view]
Gene3DG3DSA:2.160.20.60. Glu_synthase_C. 1 hit.
PfamPF01493. GXGXG. 1 hit.
[Graphical view]
TIGRFAMsTIGR03122. one_C_dehyd_C. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFMDC_METBF
AccessionPrimary (citable) accession number: Q48943
Secondary accession number(s): Q46CY9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: November 3, 2009
This is version 66 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