Q48943 (FMDC_METBF) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Methanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP]

Taxonomic identifier

269797 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Methanogenesis
Domain	Repeat
Ligand	Molybdenum
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	methanogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	formylmethanofuran dehydrogenase activity Inferred from electronic annotation. Source: EC transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 301	301	Molybdenum-containing formylmethanofuran dehydrogenase 1 subunit C		PRO_0000144190
Regions
	Repeat	112 – 124	13	1
	Repeat	131 – 143	13	2
	Repeat	150 – 162	13	3
	Repeat	176 – 188	13	4
	Repeat	195 – 207	13	5
	Repeat	214 – 226	13	6
	Repeat	233 – 245	13	7
	Region	112 – 245	134	7 X 13 AA repeats of [GW]-X-X-[MQ]-X-X-G-X-[IL]-X-[IV]-X-G
Experimental info
	Sequence conflict	2	1	Missing AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q48943 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: D871C80B50AC000D	FASTA	301	31,551
	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

References

	« Hide 'large scale' referencesShow '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]. Strain: Fusaro / DSM 804.
[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
EMBL GenBank DDBJ	X93084 Genomic DNA. Translation: CAA63631.1. CP000099 Genomic DNA. Translation: AAZ70253.1.
PIR	S62199.
RefSeq	YP_304833.1. NC_007355.1.
3D structure databases
ProteinModelPortal	Q48943.
ModBase	Search...
Protein-protein interaction databases
STRING	Q48943.
Protein family/group databases
TCDB	3.D.8.1.2. Na+- or H+-pumping formyl methanofuran dehydrogenase (FMF-DH) family.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3627699.
GenomeReviews	Gene locus Mbar_A1290 in contig CP000099_GR.
KEGG	mba:Mbar_A1290.
NMPDR	fig|269797.3.peg.1295.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG05644.
HOGENOM	HBG541237.
OMA	GNADMYV.
ProtClustDB	CLSK449964.
Enzyme and pathway databases
BioCyc	MBAR269797:MBAR_A1290-MONOMER.
Family and domain databases
InterPro	IPR017550. Formylmethanofuran_DH_suC. IPR002489. Glu_synth_asu_C. [Graphical view]
Gene3D	G3DSA:2.160.20.60. Glu_synthase_C. 1 hit.
KO	K00202.
Pfam	PF01493. GXGXG. 1 hit. [Graphical view]
SUPFAM	SSF69336. Glu_synthase_C. 1 hit.
TIGRFAMs	TIGR03122. One_C_dehyd_C. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FMDC_METBF

Accession

Primary (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 16, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program