ID   VHCA_ARCPA              Reviewed;         486 AA.
AC   P84625; D2REQ2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=F420-non-reducing hydrogenase iron-sulfur subunit A;
DE            EC=1.12.99.-;
GN   Name=mvhA; OrderedLocusNames=Arcpr_1550;
OS   Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=572546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5631 / JCM 9629 / NBRC 100127 / Av18;
RX   PubMed=21304717; DOI=10.4056/sigs.942153;
RA   von Jan M., Lapidus A., Del Rio T.G., Copeland A., Tice H., Cheng J.F.,
RA   Lucas S., Chen F., Nolan M., Goodwin L., Han C., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Chertkov O., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Saunders E.,
RA   Brettin T., Detter J.C., Chain P., Eichinger K., Huber H., Spring S.,
RA   Rohde M., Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Archaeoglobus profundus type strain (AV18).";
RL   Stand. Genomic Sci. 2:327-346(2010).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-20, COFACTOR, INTERACTION WITH HETERODISULFIDE
RP   REDUCTASE, AND SUBCELLULAR LOCATION.
RX   PubMed=15009189; DOI=10.1111/j.1432-1033.2004.04013.x;
RA   Mander G.J., Pierik A.J., Huber H., Hedderich R.;
RT   "Two distinct heterodisulfide reductase-like enzymes in the sulfate-
RT   reducing archaeon Archaeoglobus profundus.";
RL   Eur. J. Biochem. 271:1106-1116(2004).
CC   -!- FUNCTION: Part of a complex that provides reducing equivalents for
CC       heterodisulfide reductase. {ECO:0000269|PubMed:15009189}.
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000269|PubMed:15009189};
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:15009189}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15009189}.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ADB58596.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001857; ADB58596.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048084930.1; NC_013741.1.
DR   AlphaFoldDB; P84625; -.
DR   SMR; P84625; -.
DR   STRING; 572546.Arcpr_1550; -.
DR   EnsemblBacteria; ADB58596; ADB58596; Arcpr_1550.
DR   GeneID; 8740240; -.
DR   KEGG; apo:Arcpr_1550; -.
DR   eggNOG; arCOG01549; Archaea.
DR   HOGENOM; CLU_044556_0_0_2; -.
DR   OMA; QNNLAMN; -.
DR   OrthoDB; 32760at2157; -.
DR   Proteomes; UP000001901; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.645.10; -; 1.
DR   InterPro; IPR001501; Ni-dep_hyd_lsu.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   Pfam; PF00374; NiFeSe_Hases; 2.
DR   SUPFAM; SSF56762; SSF56762; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Metal-binding; Nickel;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..486
FT                   /note="F420-non-reducing hydrogenase iron-sulfur subunit A"
FT                   /id="PRO_0000199728"
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"
SQ   SEQUENCE   486 AA;  54452 MW;  3516D6C12C67F066 CRC64;
     MKKIEIEPMT RLEGHGKIAI FLDDKGNVAD AFYQIVEFRG YETFLRGLPI EEVPRTVSTI
     CGVCRAVHHT ASTKASDGVY GVEPTETAKK IRELYLNAHY VEDHCAILYA LGLPDFVVGI
     EADPAERNLV GLIKKVGVDV GKTVLKKRFA AVKVLEMLGG KPIHPVAGLP GGWSKRITED
     ERKEIEALAK EMVELGELTL QVFEDVILKN EKLLELITAD YYRVVVNYLG TVDDAGKVNY
     YDGWQVGIDT KGNEVFRFKG KDYLNYIAER VVPWSYVKMP YFKQLGWKGF VDGEGTSLYS
     VGPLARCNIG DMNTPKAKEA QEKMFDVLKE RPIHYIMAYH WARAVELLNA AERVLELAQD
     PEITSPDVRA ELGEVTGEGV GIIEAPRGTL IHHYKTDENG IVTDANLIVA TTHNHAPINI
     AIKKAAQHFI QENKEINDKL LNYVEIAYRP YDICQACASH ALPGRYPLEV LVYDSEGELI
     KTIRNF