ID   MVHD_METTM              Reviewed;         141 AA.
AC   P60238; D9PY00;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   03-AUG-2022, entry version 67.
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=MTBMA_c15190;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/jb.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA   Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-12, SUBUNIT, AND ASSOCIATION WITH HETERODISULFIDE
RP   REDUCTASE.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=8119281; DOI=10.1111/j.1432-1033.1994.tb18608.x;
RA   Setzke E., Hedderich R., Heiden S., Thauer R.K.;
RT   "H2: heterodisulfide oxidoreductase complex from Methanobacterium
RT   thermoautotrophicum. Composition and properties.";
RL   Eur. J. Biochem. 220:139-148(1994).
RN   [3]
RP   FUNCTION, COFACTOR, AND ASSOCIATION WITH HETERODISULFIDE REDUCTASE.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=12856108; DOI=10.1007/s00203-003-0577-9;
RA   Stojanowic A., Mander G.J., Duin E.C., Hedderich R.;
RT   "Physiological role of the F420-non-reducing hydrogenase (Mvh) from
RT   Methanothermobacter marburgensis.";
RL   Arch. Microbiol. 180:194-203(2003).
CC   -!- FUNCTION: Part of a complex that provides reducing equivalents for
CC       heterodisulfide reductase. MvhD may form the contact site to
CC       heterodisulfide reductase. {ECO:0000269|PubMed:12856108}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000269|PubMed:12856108};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:12856108};
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). {ECO:0000269|PubMed:8119281}.
CC   -!- SIMILARITY: Belongs to the MvhD/VhuD family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001710; ADL59098.1; -; Genomic_DNA.
DR   RefSeq; WP_013296309.1; NC_014408.1.
DR   AlphaFoldDB; P60238; -.
DR   SMR; P60238; -.
DR   DIP; DIP-59604N; -.
DR   IntAct; P60238; 1.
DR   STRING; 79929.MTBMA_c15190; -.
DR   TCDB; 3.D.7.2.4; the h2:heterodisulfide oxidoreductase (hho) family.
DR   EnsemblBacteria; ADL59098; ADL59098; MTBMA_c15190.
DR   GeneID; 9705228; -.
DR   KEGG; mmg:MTBMA_c15190; -.
DR   PATRIC; fig|79929.8.peg.1472; -.
DR   HOGENOM; CLU_095272_2_0_2; -.
DR   OMA; KIVMFCC; -.
DR   OrthoDB; 91498at2157; -.
DR   Proteomes; UP000000345; 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   1: Evidence at protein level;
KW   2Fe-2S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8119281"
FT   CHAIN           2..141
FT                   /note="F420-non-reducing hydrogenase iron-sulfur subunit D"
FT                   /id="PRO_0000218275"
FT   CONFLICT        7
FT                   /note="K -> G (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        10..12
FT                   /note="MFC -> GFN (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   141 AA;  15929 MW;  6E2DAEBA0F42D4E7 CRC64;
     MAEDDIKIVM FCCNWCSYGG ADTAGTARMQ YPTNIRVIRV MCSGRIEPQF VFKAFREGAD
     GVLVTGCHHG DCHYDAGNYK LDRRMRLIYK LADELGIGRE RIHHDWISAS EGEKFAETVK
     MMVDRIRALG PSPIKKQLAE A