ID   MVHA_METTM              Reviewed;         472 AA.
AC   P60227; D9PXZ8;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=F420-non-reducing hydrogenase subunit A;
DE            EC=1.12.99.-;
DE   AltName: Full=Methyl viologen-reducing hydrogenase subunit alpha;
DE            Short=MVH subunit A;
GN   Name=mvhA; OrderedLocusNames=MTBMA_c15170;
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 2-18, 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, 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. {ECO:0000269|PubMed:12856108}.
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000305};
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 [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
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DR   EMBL; CP001710; ADL59096.1; -; Genomic_DNA.
DR   RefSeq; WP_013296307.1; NC_014408.1.
DR   AlphaFoldDB; P60227; -.
DR   SMR; P60227; -.
DR   DIP; DIP-59603N; -.
DR   IntAct; P60227; 1.
DR   STRING; 79929.MTBMA_c15170; -.
DR   TCDB; 3.D.7.2.4; the h2:heterodisulfide oxidoreductase (hho) family.
DR   EnsemblBacteria; ADL59096; ADL59096; MTBMA_c15170.
DR   GeneID; 9705226; -.
DR   KEGG; mmg:MTBMA_c15170; -.
DR   PATRIC; fig|79929.8.peg.1470; -.
DR   HOGENOM; CLU_044556_0_0_2; -.
DR   OMA; VQNNPAM; -.
DR   OrthoDB; 32760at2157; -.
DR   Proteomes; UP000000345; Chromosome.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   Gene3D; 1.10.645.10; -; 1.
DR   InterPro; IPR001501; Ni-dep_hyd_lsu.
DR   InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   Pfam; PF00374; NiFeSe_Hases; 2.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR   PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Metal-binding; Nickel; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8119281"
FT   CHAIN           2..472
FT                   /note="F420-non-reducing hydrogenase subunit A"
FT                   /id="PRO_0000199727"
FT   BINDING         61
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         64
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         442
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         445
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        11
FT                   /note="R -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   472 AA;  52839 MW;  5993E7AC4BC0579F CRC64;
     MVKLTMEPVT RIEGHAKITV HLDDAGNVED TRLHVMEFRG FEKFLQGRPI EEAPRIVPRI
     CGICDVQHHL AAAKAVDACF GFEPDDVLPA AYKMREIMNW GSYMHSHGLH FYFLAAPDFI
     AGKDRKTRNV FQIIKDAPDV ALQAIELRKN ALEIVRATGG RPIHPTSSTP GGISTELDDE
     TQKDLLQKAQ RNVELAEATL ELAVPIFEEN IDLVNSLGNI ETYHTGLVKN GVWDVYDGIV
     RIKDKEGNLF REFKPADYAD TIAEHVKPYS WLKFPYIKDL GYPDGVYRVS PLSRLNVADK
     MPDAAPKAQD YFKEFQDKFG YAQQTLLYHW ARLIEVLACA ECAADALEGD LSGEKFPDSL
     ERQAGDGVGI VEAPRGTLTH HYTCDENGLI TKANIVVATI QNNPAMEMGI QKVAQDYIKP
     GVEVDDKIFN LMEMVIRAYD PCLSCATHTI DSQMRLATLE VYDSEGDLVK RI