ID A0A385NRN3_9BACI Unreviewed; 468 AA.
AC A0A385NRN3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Ni/Fe hydrogenase {ECO:0000313|EMBL:AYA76930.1};
GN ORFNames=DOE78_16610 {ECO:0000313|EMBL:AYA76930.1};
OS Bacillus sp. Y1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=352858 {ECO:0000313|EMBL:AYA76930.1, ECO:0000313|Proteomes:UP000265711};
RN [1] {ECO:0000313|EMBL:AYA76930.1, ECO:0000313|Proteomes:UP000265711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y1 {ECO:0000313|EMBL:AYA76930.1};
RA Rathod J., Jean J.-S.;
RT "Arsenic resistant and redox active subsurface bacterial isolate Bacillus
RT sp. Y1 from Yichu borehole sediment.";
RL Submitted (JUN-2018) 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; CP030028; AYA76930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A385NRN3; -.
DR KEGG; bacq:DOE78_16610; -.
DR OrthoDB; 9761717at2; -.
DR Proteomes; UP000265711; 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; 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; 3.
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:UP000265711}.
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 61
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
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 400
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 448
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 451
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 454
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 468 AA; 53034 MW; D2720FD7224D17A0 CRC64;
MSKRIVINPL TRISGFMEID VIIEQNQVVD VKTKGNLFRG FEQMLVGRSP FDAVYFTQRI
CGICSAAHSM ASSLALEDAL NIEPMEQGKY LRDIIHCCEF LQNHIRHFYQ YTVPDYVKIE
QNSLFQSDHD DFRLPKNIND RISQHYFDSL KFSRLAHEML AVLGGKAPHN HGVFIGGITT
QATAEKVVHI DSILGKITRF IDEKMIPDVY DIAHFYADYF RIGGGYGNLL TYGAFNHYKE
LGTLYVDPLV STMESVEAFD ERKIQEKIDY SYFKSITNSN QANEEVTEPD MDKEKAYSWV
KAPRYNGLPI EVGPLARLIL SGAYNNGISA MDRTIARALE AKKITEIMKI LLQQIIPGVD
VQKKYELPEL ASGRGLVDTT RGALGHWLKI RDKKISFYQI ITPSTWDFST RDDNGFRGTA
EEALVGTPIQ NPDKPAEIGR ILRSFDPCMS CATHVYSPGK QVKTIKVF
//
