ID   A0A1W1WC74_SULTA        Unreviewed;       564 AA.
AC   A0A1W1WC74;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Quinone-reactive Ni/Fe-hydrogenase large subunit {ECO:0000313|EMBL:SMC03343.1};
GN   ORFNames=SAMN00768000_1037 {ECO:0000313|EMBL:SMC03343.1};
OS   Sulfobacillus thermosulfidooxidans (strain DSM 9293 / VKM B-1269 / AT-1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX   NCBI_TaxID=929705 {ECO:0000313|EMBL:SMC03343.1, ECO:0000313|Proteomes:UP000192660};
RN   [1] {ECO:0000313|Proteomes:UP000192660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9293 {ECO:0000313|Proteomes:UP000192660};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601501-1};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000256|ARBA:ARBA00001967,
CC         ECO:0000256|PIRSR:PIRSR601501-1};
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC       {ECO:0000256|ARBA:ARBA00011771}.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC       family. {ECO:0000256|ARBA:ARBA00009292, ECO:0000256|RuleBase:RU003896}.
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DR   EMBL; FWWY01000001; SMC03343.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1WC74; -.
DR   STRING; 28034.BFX07_00095; -.
DR   OrthoDB; 9761717at2; -.
DR   Proteomes; UP000192660; Unassembled WGS sequence.
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; Cytochrome-c3 Hydrogenase, chain B; 1.
DR   InterPro; IPR001501; Ni-dep_hyd_lsu.
DR   InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR42958; HYDROGENASE-2 LARGE CHAIN; 1.
DR   PANTHER; PTHR42958:SF2; UPTAKE HYDROGENASE LARGE SUBUNIT; 1.
DR   Pfam; PF00374; NiFeSe_Hases; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   PROSITE; PS00507; NI_HGENASE_L_1; 1.
DR   PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601501-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601501-1};
KW   Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRSR:PIRSR601501-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003896};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192660}.
FT   BINDING         45
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         64
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         67
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         67
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         542
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         545
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT   BINDING         548
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ   SEQUENCE   564 AA;  61824 MW;  6F4C0A328F80C483 CRC64;
     MAQLKRFTID PITRIEGHLR IEVDLDPNNV VKDAYSSSGM FRGIELIMQD RDFHDVGLFA
     QRICGVCTYT HYRVGTEAVE AALGVQIPTD ARIVRNLLHA SLFLHDHVVH FYQLHGMDWF
     DVVAALSADP EKAAAVALKY SPTPYNAGAG TFRAVQERVS ALVASGELGP FANGYWGNPS
     YKLTPEQDLI MLSHYLDALA VQRTLAQAMA VFGGKNPHPQ SLVVGGVTSI MDIVDPSRVA
     EFLGKMQSGA QFIQNAYLPD IRMIADAYIQ EAKSGEGYGV PDFMSYGAFP LDNIPWPKGA
     MLFPSGVFNR NTGMVNDLNA DQIKEDVTRA WYQGPNEGVY PGEESTIPDY TGYEADGALN
     RSGKYSWIKA PRYQGLPMET GPLARLLIGR ARKDPLIEKA MTDFERSVPR GFSPDEWYST
     VGRTAARAVE ADIIASQVGA WVDELAANVG QGQTQTYTAP SNTSGEGFRL LDAPRGALGH
     WIRIENGRVT HYQAVVPSTW NASPRDHKGQ MGPYEASLIN TRLAVANQPL EVLRTVHSFD
     PCIGCAVHIV DSKGAEVARF QVDV
//