ID C6A3Z3_THESM Unreviewed; 412 AA.
AC C6A3Z3;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=Membrane-bound hydrogenase MBH 2, subunit Mbh2L (NiFe hydrogenase catalytic subunit) {ECO:0000313|EMBL:ACS90338.1};
GN OrderedLocusNames=TSIB_1284 {ECO:0000313|EMBL:ACS90338.1};
OS Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=604354 {ECO:0000313|EMBL:ACS90338.1, ECO:0000313|Proteomes:UP000009079};
RN [1] {ECO:0000313|EMBL:ACS90338.1, ECO:0000313|Proteomes:UP000009079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12597 / MM 739 {ECO:0000313|Proteomes:UP000009079};
RX PubMed=19447963; DOI=10.1128/AEM.00718-09;
RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT analysis.";
RL Appl. Environ. Microbiol. 75:4580-4588(2009).
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; CP001463; ACS90338.1; -; Genomic_DNA.
DR RefSeq; WP_015849557.1; NC_012883.1.
DR AlphaFoldDB; C6A3Z3; -.
DR STRING; 604354.TSIB_1284; -.
DR GeneID; 8096285; -.
DR KEGG; tsi:TSIB_1284; -.
DR eggNOG; arCOG01547; Archaea.
DR HOGENOM; CLU_015134_1_2_2; -.
DR OMA; GIEYMGM; -.
DR OrthoDB; 43567at2157; -.
DR Proteomes; UP000009079; Chromosome.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR001501; Ni-dep_hyd_lsu.
DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR InterPro; IPR029014; NiFe-Hase_large.
DR PANTHER; PTHR43485:SF1; FORMATE HYDROGENLYASE SUBUNIT 5-RELATED; 1.
DR PANTHER; PTHR43485; HYDROGENASE-4 COMPONENT G; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR Pfam; PF00374; NiFeSe_Hases; 1.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR PROSITE; PS00507; NI_HGENASE_L_1; 1.
PE 4: Predicted;
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:UP000009079}.
FT DOMAIN 120..376
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 69
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 69
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 370
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
FT BINDING 373
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|PIRSR:PIRSR601501-1"
SQ SEQUENCE 412 AA; 46502 MW; A65B99521BDEBA47 CRC64;
MAKTTYYVPI GPIHPALKEP IRVEAEVEGE KIVKVDVKRG FAHRGIEYMG MKRNAIQTLY
LSERICGICS ISHPYAFVIG SEKALGIEAP PRAQYIRTII AELERIHSHI LWLGVIAHEI
GFDSLLFWTW KGREKVLDIL EAITGNRINY SMYMIGGVRR DLKESHIRVL KDMITYYWEF
TEHMKEVFLS DPVYKARTRG VAQVSKDVAL KLNLVGPTAR AAGLRMDIRQ DIPYDAYADI
DVKAVVPQDI VGEARGDAYD VTMVRIYEIE QSLDIIEYCI DNLPEGKILA IPNYIALLNK
IKKTEGEGIG AHEAPRGEVV HYFRYDGTRD GPAVWKVIAP SYNNINSWGY CLLGAEVADI
PVVVAYIDPC MCCNDRVAVV KDSTGKILDY SILHRKAVEK TRALEKELGV MK
//