ID   VHCA_METVO              Reviewed;         474 AA.
AC   Q00404;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=F420-non-reducing hydrogenase vhc subunit A;
DE            EC=1.12.99.-;
GN   Name=vhcA;
OS   Methanococcus voltae.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2188;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RX   PubMed=1603063; DOI=10.1007/bf00587582;
RA   Halboth S., Klein A.;
RT   "Methanococcus voltae harbors four gene clusters potentially encoding two
RT   [NiFe] and two [NiFeSe] hydrogenases, each of the cofactor F420-reducing or
RT   F420-non-reducing types.";
RL   Mol. Gen. Genet. 233:217-224(1992).
RN   [2]
RP   TRANSCRIPTIONAL REGULATION.
RC   STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RX   PubMed=8121392; DOI=10.1007/bf00281785;
RA   Berghoefer Y., Agha-Amiri K., Klein A.;
RT   "Selenium is involved in the negative regulation of the expression of
RT   selenium-free [NiFe] hydrogenases in Methanococcus voltae.";
RL   Mol. Gen. Genet. 242:369-373(1994).
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000305};
CC   -!- SUBUNIT: The F420-non-reducing hydrogenase vhc is composed of three
CC       subunits; VhcA, VhcD and VhcG. {ECO:0000250}.
CC   -!- INDUCTION: By selenium deprivation. {ECO:0000269|PubMed:8121392}.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
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DR   EMBL; X61203; CAA43506.1; -; Genomic_DNA.
DR   PIR; S16727; S16727.
DR   AlphaFoldDB; Q00404; -.
DR   SMR; Q00404; -.
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   2: Evidence at transcript level;
KW   Metal-binding; Nickel; Oxidoreductase.
FT   CHAIN           1..474
FT                   /note="F420-non-reducing hydrogenase vhc subunit A"
FT                   /id="PRO_0000199729"
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         445
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         448
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   474 AA;  52914 MW;  4BA3F16EC5F18B44 CRC64;
     MTKLSIEPVT RVEGHGKVTL SFDDSGKLDK VNFHVVEVRG FEKFLEGRYI EDAPIFTPRI
     CGICQVSHHL ASAKAVDNVF GVKIPETANM LRNLIHQASN VHSHALHFGM LASPDLMFPT
     TDDALKRNLL GVAGENMDMI KDSIAMRKVG QTIVQKVGGR AIHPVTAIVG GQSKPLTEEE
     RDELLTLSDN LVETAERTLN VGKEMVENLK EKDLMNLGYF ESYHMGLVNN GAQDIYEGNI
     RVVNSEGKIE YEFDPAEYAN YITEGVRPYS YLKFLALLKR RGEGKGAYRV NTLSRLNVCD
     KMPTPIAQKY YEEFVKTYGK PAHQPMLFHY ARLIELLSSS ELIRKFLEDD KIVDTDVRAE
     VDPKNITGEG VGCVEAPRGT LIHHFKTDDR GIINDTNLVV ATVQNNPAMD IGVQKVAEKY
     IKTPEVAKPH ILNHMEMVIR AYDPCLSCAT HTIGEEPKIL SIHVCQGGKL IKTL