ID A0A268U036_9HELI Unreviewed; 578 AA.
AC A0A268U036;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Hydrogenase 2 large subunit {ECO:0000313|EMBL:PAF50375.1};
GN ORFNames=BKH43_04595 {ECO:0000313|EMBL:PAF50375.1};
OS Helicobacter sp. 13S00401-1.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1905758 {ECO:0000313|EMBL:PAF50375.1, ECO:0000313|Proteomes:UP000216091};
RN [1] {ECO:0000313|EMBL:PAF50375.1, ECO:0000313|Proteomes:UP000216091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13S00401-1 {ECO:0000313|EMBL:PAF50375.1,
RC ECO:0000313|Proteomes:UP000216091};
RX PubMed=28827684; DOI=10.1038/s41598-017-09091-7;
RA Gilbert M.J., Duim B., Timmerman A.J., Zomer A.L., Wagenaar J.A.;
RT "Whole genome-based phylogeny of reptile-associated Helicobacter indicates
RT independent niche adaptation followed by diversification in a
RT poikilothermic host.";
RL Sci. Rep. 7:8387-8387(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAF50375.1}.
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DR EMBL; MLAR01000006; PAF50375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268U036; -.
DR OrthoDB; 9761717at2; -.
DR Proteomes; UP000216091; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000216091}.
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 62
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 65
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 65
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 551
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 554
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 557
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 578 AA; 64018 MW; 13EF48A841C19AC4 CRC64;
MTKKIVVDPI TRIEGHLRIE VTVDENNVIT DAHSSSTLWR GIETILKGRD PRDAGFLAGR
ICGVCTYSHY RAGIMAVEDA LGIVPPYNAQ LVRALMDQAL FLHDHTVHFY TLHGLDWCDV
VSALSASPAK AAKLAFAYTD NPISAGEDEL TAVQKRVKDF VSKGALGPFN NGYWGHPTYR
FSPEQNLIVL SHYLKLLEIQ REAAKMMAIF GGKQPHPQSL TVGGITSVMD VLDPSRLAEY
KFKFDKVADF VNRAYYPDLI MAGEVYVNEP SATAGCNLLN FMSSKEIRVG RDDFLLESGI
VLNGDISKLH PINEDLIKEE VTHSWYKYEN TNEIALQPYD GQTNPNYTGF VDGQSIGLSG
KNEPSKLLRT DDKYSWIKSP RYDSMPMEVG PLASLVVGLA AKNERVEKTA TDFLKKTGLP
LKAVFSTLGR TAARGIEAKI IADYGILTFN ALIENLKSDK STCVPYSIDK DKEYKGRYIG
DVPRGMLSHW ARIKNGVIEN YQCVVPSTWN AGPRDKAGKK GPYETSLIGT KIADVTKPLE
IIRTIHSFDP CIACAVHLVD TKGNEISNYK VDPSMARI
//
