GenomeNet

Database: UniProt
Entry: C6A3Z3_THESM
LinkDB: C6A3Z3_THESM
Original site: C6A3Z3_THESM 
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system