ID   MVHA_METFE              Reviewed;         472 AA.
AC   Q49179;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 70.
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;
OS   Methanothermus fervidus.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanothermaceae; Methanothermus.
OX   NCBI_TaxID=2180;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2115877; DOI=10.1128/jb.172.8.4715-4718.1990;
RA   Steigerwald V.J., Beckler G.S., Reeve J.N.;
RT   "Conservation of hydrogenase and polyferredoxin structures in the
RT   hyperthermophilic archaebacterium Methanothermus fervidus.";
RL   J. Bacteriol. 172:4715-4718(1990).
CC   -!- FUNCTION: Part of a complex that provides reducing equivalents for
CC       heterodisulfide reductase. {ECO:0000250}.
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) (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
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DR   EMBL; M34016; AAA72832.1; -; Genomic_DNA.
DR   PIR; B37777; B37777.
DR   RefSeq; WP_013413806.1; NC_014658.1.
DR   AlphaFoldDB; Q49179; -.
DR   SMR; Q49179; -.
DR   GeneID; 9962459; -.
DR   OMA; VQNNPAM; -.
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   3: Inferred from homology;
KW   Metal-binding; Nickel; Oxidoreductase.
FT   CHAIN           1..472
FT                   /note="F420-non-reducing hydrogenase subunit A"
FT                   /id="PRO_0000199725"
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"
SQ   SEQUENCE   472 AA;  53311 MW;  4E8886BEDEBE3947 CRC64;
     MEKLVLEPVT RIEGHAKITV QLDEEGNVKD TRFHVMEFRG FEKFLQGRRI EEAPRIVPRI
     CGICQVQHHL ASAKAVDACF GFEPEDIPET AYKMREIMNW ASYVHSHGLH FYFLAAPDFI
     GGKDRETRNI FKIIQDSPDV AKQAIELRKN AQDIVAATGG RAIHPVSFIP GGITTELDKE
     TQEKLLKKAK RNVEIAESTL ELAIPIFEDN MDLVESLGTI ETYHMGLVKN GTWDVYDGVV
     RVKDKNGENF AEFGPDEYTK YIAEHVKPYS WLKFPYLKEL GYPDGVYRVS PLSRLNVADK
     MPDAAPKAQE YFKEFRNKFG YAQQPLLYHW ARLIEMLAAA ECMASVLEED LSGKKIHGKL
     ERQEGEGVGI VEAPRGTLIH HYACDKNGII TKANLIVATV QNNPAMEMGI QKVAKERIKP
     GVDVDDKIYN LMEMVIRAYD PCLSCATHTV DGKVKLFTLE VLDSEGNVVK RL