ID A0A0J8G3F8_CLOCY Unreviewed; 477 AA.
AC A0A0J8G3F8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Ni,Fe-hydrogenase I large subunit {ECO:0000313|EMBL:KMT22241.1};
DE EC=1.12.99.6 {ECO:0000313|EMBL:KMT22241.1};
GN ORFNames=CLCY_4c02140 {ECO:0000313|EMBL:KMT22241.1};
OS Clostridium cylindrosporum DSM 605.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121307 {ECO:0000313|EMBL:KMT22241.1, ECO:0000313|Proteomes:UP000036756};
RN [1] {ECO:0000313|EMBL:KMT22241.1, ECO:0000313|Proteomes:UP000036756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 605 {ECO:0000313|EMBL:KMT22241.1,
RC ECO:0000313|Proteomes:UP000036756};
RA Poehlein A., Schiel-Bengelsdorf B., Bengelsdorf F., Daniel R., Duerre P.;
RT "Draft genome sequence of the purine-degrading Clostridium cylindrosporum
RT HC-1 (DSM 605).";
RL Submitted (JUN-2015) 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}.
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:KMT22241.1}.
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DR EMBL; LFVU01000024; KMT22241.1; -; Genomic_DNA.
DR RefSeq; WP_048570331.1; NZ_LFVU01000024.1.
DR AlphaFoldDB; A0A0J8G3F8; -.
DR STRING; 1121307.CLCY_4c02140; -.
DR PATRIC; fig|1121307.3.peg.1870; -.
DR OrthoDB; 9761717at2; -.
DR Proteomes; UP000036756; Unassembled WGS sequence.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0033748; F:hydrogenase (acceptor) activity; IEA:UniProtKB-EC.
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.
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:0000313|EMBL:KMT22241.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036756}.
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 59
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 62
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
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 409
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 457
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 460
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 477 AA; 52621 MW; 35EC5149AE8F08EB CRC64;
MKIVIDPVTR VSGLLKIEVE VEGNKVVSAK SSGGQFRGFE KMFQGRDPLD AIWLSPRVCG
ICSTHHTLAA TLALENALNV APDFNGVVVR EIANGFEFLQ NHLRQIYFFT LPDFVQIDNV
SPLYKTISPN DADYRLPINI TAKLNGDYVK AVKYSRDAHR AAATIIGKVP HGHGIFVGGT
TIDMNVQQMQ ACLYTVREIK EFIEGNLLED INIIASYYKD YYTMGAGPQN FMSYGLYDNP
KFPVKYVSPG VILKSSTNQY IREEFDRNNI TESIKNSWLI PETGNQTSKP GTAPPPSPNA
YKEGAYSWVA AARYKGHAME GGPLARMILS GIYTRGVSVM DRIIARALEA RKICECIESL
LAVVKLGPPY QEKWKVPEKA FGVGLTDASR GTLGHWVNIS GGKIANYTLI PPSTWNLGPT
DEKGVLGTVE QALIGTTINN VQHPVEIGRI VRSFDPCLNC AAHITSDRYS PFEINLV
//
