NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 242-253; 275-290 AND 372-398.
PubMed=8954165 [NCBI, ExPASy, EBI, Israel, Japan]
Hochheimer A., Linder D., Thauer R.K., Hedderich R.;
"The molybdenum formylmethanofuran dehydrogenase operon and the tungsten formylmethanofuran dehydrogenase operon from Methanobacterium thermoautotrophicum. Structures and transcriptional regulation.";
Eur. J. Biochem. 242:156-162(1996).

[2]

PROTEIN SEQUENCE OF 2-18.
PubMed=8575452 [NCBI, ExPASy, EBI, Israel, Japan]
Hochheimer A., Schmitz R.A., Thauer R.K., Hedderich R.;
"The tungsten formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic for enzymes containing molybdopterin dinucleotide.";
Eur. J. Biochem. 234:910-920(1995).

Comments

FUNCTION: Catalyzes the reversible oxidation of CO(2) 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.
ENZYME REGULATION: Inactivated by cyanide.
PATHWAY: One-carbon metabolism; methanogenesis from carbone dioxide; 5,10-methenyl-H(4)MPT from CO(2): step 1/3 .
SUBUNIT: Consists of five subunits; fmdA, fmdB, fmdC, fmdD, and fmdE.
INDUCTION: By growth on molybdenum, under anaerobic conditions.
SIMILARITY: In the N-terminal section; belongs to the fwdC/fmdC family.
SIMILARITY: In the C-terminal section; belongs to the molybdenum dinucleotide binding protein family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X97820; CAA66401.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

P61937.

Ontologies

GO:0018493;	Molecular function: formylmethanofuran dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0030151;	Molecular function: molybdenum ion binding (inferred from electronic annotation from InterPro).
GO:0015948;	Biological process: methanogenesis (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR017550; Formylmethanofuran_DH_C.
IPR012048; Formylmethanofuran_DH_csu/dsu.
IPR002489; Glu_synthase_C.
IPR006657; MPT_dinuc_bd.
Graphical view of domain structure.

Gene3D

G3DSA:2.160.20.60; Glu_synthase_C; 1.

Pfam

PF01493; GXGXG; 1.
PF01568; Molydop_binding; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036633; FmdC_D; 1.

ProtoNet

P61937.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Methanogenesis; Molybdenum; Oxidoreductase; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 400`	`400`	`Molybdenum-containing formylmethanofuran dehydrogenase 1 subunit C.`	`PRO_0000144191`
`REPEAT`	`76 88`	`13`	`1.`
`REPEAT`	`95 107`	`13`	`2.`
`REPEAT`	`114 126`	`13`	`3.`
`REPEAT`	`140 152`	`13`	`4.`
`REPEAT`	`159 171`	`13`	`5.`
`REPEAT`	`178 190`	`13`	`6.`
`REPEAT`	`197 209`	`13`	`7.`
`REGION`	`76 209`	`134`	`7 X 13 AA repeats of [GW]-X-X-M-X-X-G-X-I-X-[IV]-X-G.`
`CONFLICT`	`14 14`		`P -> G (in Ref. 2; AA sequence).`

Sequence information

Length: 400 AA [This is the length of the unprocessed precursor]

Molecular weight: 43321 Da [This is the MW of the unprocessed precursor]

CRC64: 41F1C21A25CFBBC3 [This is a checksum on the sequence]

        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

P61937 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools