ID D6Z224_DESAT Unreviewed; 566 AA.
AC D6Z224;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Nickel-dependent hydrogenase large subunit {ECO:0000313|EMBL:ADH85599.1};
GN OrderedLocusNames=DaAHT2_0895 {ECO:0000313|EMBL:ADH85599.1};
OS Desulfurivibrio alkaliphilus (strain DSM 19089 / UNIQEM U267 / AHT2).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfobulbaceae; Desulfurivibrio.
OX NCBI_TaxID=589865 {ECO:0000313|EMBL:ADH85599.1, ECO:0000313|Proteomes:UP000001508};
RN [1] {ECO:0000313|Proteomes:UP000001508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19089 / UNIQEM U267 / AHT2
RC {ECO:0000313|Proteomes:UP000001508};
RG US DOE Joint Genome Institute;
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Sorokin D.Y., Muyzer G.,
RA Woyke T.;
RT "Complete sequence of Desulfurivibrio alkaliphilus AHT2.";
RL Submitted (FEB-2010) 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; CP001940; ADH85599.1; -; Genomic_DNA.
DR RefSeq; WP_013163129.1; NC_014216.1.
DR AlphaFoldDB; D6Z224; -.
DR STRING; 589865.DaAHT2_0895; -.
DR KEGG; dak:DaAHT2_0895; -.
DR eggNOG; COG0374; Bacteria.
DR HOGENOM; CLU_030087_0_0_7; -.
DR InParanoid; D6Z224; -.
DR OrthoDB; 9761717at2; -.
DR Proteomes; UP000001508; 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; 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:UP000001508}.
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 63
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 66
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 66
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 543
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 546
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 549
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 566 AA; 63296 MW; F8814358E7127592 CRC64;
MAAKRIVVDP ITRIEGHLRM EVVVDDNNVI QDAYASSTLW RGIELILKGR DPRDAGLITQ
RICGVCTYSH YRVGIEAVEN ALGITPPYNA ILTRTLMSQA LFLHDHIVHF YHLHGLDWCD
ITRALEADPR KASDLAFKYA DIPIATGADE LTAVQARLKG FVAEGHLGPF ANAYWGHKTY
HFTPEQNLIV LSHYLKALEV QRNAAQMLAI FGGKQPHPQS LVVGGVTCVM DLLNPNRLGE
YLTKFEEVSD FMNRAYYADV KMAAEAYIGE DSVLKGSGVQ NFIAARDFQI SRNEWLFDRG
MVLDGDLGRA HDVDEEKITE EATHAWYHDD QSRHPYNGVT DPNYTGFRDG DTLQGRAKII
DEKGKYTWVK APRYDDRVME VGPLAQMLVG YARGNEKVRA VVDNFLAETG VPVPALFSTL
GRTAGRMLQT KLIADHGKTT LLNLVENLKV DQETCAPYVI DKNREYQGRA LNDVPRGMLG
HWVKIKNGVI ENYQCVVPTT WNASPMDSAS QHGPYEAALI GTRLADPSQP LEIIRTIHSF
DPCLACAVHV MDYRGNELAN YRVEAK
//
