MVHD_METTH
ID MVHD_METTH Reviewed; 141 AA.
AC Q50781; O27208;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=F420-non-reducing hydrogenase iron-sulfur subunit D;
DE EC=1.12.99.-;
DE AltName: Full=Methyl viologen-reducing hydrogenase subunit delta;
DE Short=MVH subunit D;
GN Name=mvhD; OrderedLocusNames=MTH_1136;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=2654933; DOI=10.1073/pnas.86.9.3031;
RA Reeve J.N., Beckler G.S., Cram D.S., Hamilton P.T., Brown J.W.,
RA Krzycki J.A., Kolodziej A.F., Alex L., Orme-Johnson W.H., Walsh C.T.;
RT "A hydrogenase-linked gene in Methanobacterium thermoautotrophicum strain
RT delta H encodes a polyferredoxin.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3031-3035(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: Part of a complex that provides reducing equivalents for
CC heterodisulfide reductase. MvhD may form the contact site to
CC heterodisulfide reductase (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC -!- SUBUNIT: The F420-non-reducing hydrogenase is composed of three
CC subunits; MvhA, MvhD and MvhG. It forms a complex with the
CC heterodisulfide reductase (hdr) (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MvhD/VhuD family. {ECO:0000305}.
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DR EMBL; J04540; AAB02349.1; -; Genomic_DNA.
DR EMBL; AE000666; AAB85625.1; -; Genomic_DNA.
DR PIR; A30315; A30315.
DR PIR; C69018; C69018.
DR RefSeq; WP_010876760.1; NC_000916.1.
DR AlphaFoldDB; Q50781; -.
DR SMR; Q50781; -.
DR IntAct; Q50781; 1.
DR STRING; 187420.MTH_1136; -.
DR EnsemblBacteria; AAB85625; AAB85625; MTH_1136.
DR GeneID; 24854260; -.
DR KEGG; mth:MTH_1136; -.
DR PATRIC; fig|187420.15.peg.1113; -.
DR HOGENOM; CLU_095272_2_0_2; -.
DR OMA; KIVMFCC; -.
DR BioCyc; MetaCyc:MVHDMAUTO-MON; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR003813; MvhD/FlpD.
DR Pfam; PF02662; FlpD; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..141
FT /note="F420-non-reducing hydrogenase iron-sulfur subunit D"
FT /id="PRO_0000218274"
FT CONFLICT 128
FT /note="D -> G (in Ref. 1; AAB02349)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 141 AA; 15910 MW; 6E2A69D0AFEC9070 CRC64;
MAEDDIKIVM FCCNWCSYGG ADTAGTARMQ YPTNIRVIRV MCSGRIEPQF VLKAFREGAD
GVLVTGCHHG DCHYDAGNYK LDRRMRLIYK LADELGIGRE RIHHDWISAS EGEKFAETVK
MMVNRIKDLG PSPIKKQLAE A