ID Q8NKS2_THEKO Unreviewed; 428 AA.
AC Q8NKS2; Q5JHW6;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE SubName: Full=Cytosolic NiFe-hydrogenase, alpha subunit {ECO:0000313|EMBL:BAD86258.1};
DE SubName: Full=Sulfhydrogenase alpha subunit {ECO:0000313|EMBL:BAC00531.1};
GN Name=hydA {ECO:0000313|EMBL:BAC00531.1};
GN OrderedLocusNames=TK2069 {ECO:0000313|EMBL:BAD86258.1};
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014 {ECO:0000313|EMBL:BAC00531.1};
RN [1] {ECO:0000313|EMBL:BAC00531.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KOD1 {ECO:0000313|EMBL:BAC00531.1};
RX PubMed=12591889; DOI=10.1128/JB.185.5.1705-1711.2003;
RA Kanai T., Ito S., Imanaka T.;
RT "Characterization of a cytosolic NiFe-hydrogenase from the
RT hyperthermophilic archaeon Thermococcus kodakaraensis KOD1.";
RL J. Bacteriol. 185:1705-1711(2003).
RN [2] {ECO:0000313|EMBL:BAD86258.1, ECO:0000313|Proteomes:UP000000536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1
RC {ECO:0000313|Proteomes:UP000000536}, and KOD1
RC {ECO:0000313|EMBL:BAD86258.1};
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [3] {ECO:0007829|PDB:5YXY, ECO:0007829|PDB:5YY0}
RP X-RAY CRYSTALLOGRAPHY (3.24 ANGSTROMS).
RX PubMed=29915046; DOI=10.1073/pnas.1801955115;
RA Kwon S., Watanabe S., Nishitani Y., Kawashima T., Kanai T., Atomi H.,
RA Miki K.;
RT "Crystal structures of a [NiFe] hydrogenase large subunit HyhL in an
RT immature state in complex with a Ni chaperone HypA.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:7045-7050(2018).
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|PIRSR:PIRSR601501-1};
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DR EMBL; AB075598; BAC00531.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD86258.1; -; Genomic_DNA.
DR RefSeq; WP_011251019.1; NC_006624.1.
DR PDB; 5YXY; X-ray; 3.30 A; A/B/C=1-428.
DR PDB; 5YY0; X-ray; 3.24 A; A=1-428.
DR PDBsum; 5YXY; -.
DR PDBsum; 5YY0; -.
DR AlphaFoldDB; Q8NKS2; -.
DR SMR; Q8NKS2; -.
DR STRING; 69014.TK2069; -.
DR EnsemblBacteria; BAD86258; BAD86258; TK2069.
DR GeneID; 78448604; -.
DR KEGG; tko:TK2069; -.
DR PATRIC; fig|69014.16.peg.2024; -.
DR eggNOG; arCOG01549; Archaea.
DR HOGENOM; CLU_044556_0_0_2; -.
DR OrthoDB; 42371at2157; -.
DR BRENDA; 1.12.1.3; 5246.
DR BRENDA; 1.12.99.6; 5246.
DR Proteomes; UP000000536; 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 NCBIfam; NF040832; sulfhyd_HydA; 1.
DR PANTHER; PTHR43600; COENZYME F420 HYDROGENASE, SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43600:SF2; CYTOSOLIC NIFE-HYDROGENASE, ALPHA SUBUNIT; 1.
DR Pfam; PF00374; NiFeSe_Hases; 2.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5YXY, ECO:0007829|PDB:5YY0};
KW Iron {ECO:0000256|PIRSR:PIRSR601501-1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR601501-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601501-1};
KW Nickel {ECO:0000256|PIRSR:PIRSR601501-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000536}.
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 68
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 68
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 374
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 418
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 421
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 424
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 428 AA; 48287 MW; 13347324451C194C CRC64;
MKNVYLPITV DHIARVEGKG GVEIVVGDDG VKEVKLNIIE GPRFFEAITL GKKLDEALAI
YPRICSFCSA AHKLTAVEAA EKAIGFTPRE EIQALREVLY IGDMIESHAL HLYLLVLPDY
LGYSGPLHMI DEYKKEMSIA LDLKNLGSWM MDELGSRAIH QENAVLGGFG KLPDKSVLEN
MKRRLKEALP KAEYTFELFT KLEQYEEVEG PITHIAVKPR NGVYGIYGDY LKASDGNEFP
SEEYREHIKE FVVEHSFAKH SHYHGKPFMV GAISRLVNNA DTLYGRAKEL YESYKDLLRS
TNPFANNLAQ ALELVYFTER AIDLIDEALA KWPIRPRDEV ALKDGFGVST TEAPRGVLVY
ALKVENGRVS YADIITPTAF NLAMMEQHVR MMAEKHYNDD PEKLKLLAEM VVRAYDPCIS
CSVHVARL
//
