ID C6A1Y7_THESM Unreviewed; 627 AA.
AC C6A1Y7;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Predicted formate dehydrogenase {ECO:0000313|EMBL:ACS89632.1};
GN OrderedLocusNames=TSIB_0567 {ECO:0000313|EMBL:ACS89632.1};
OS Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=604354 {ECO:0000313|EMBL:ACS89632.1, ECO:0000313|Proteomes:UP000009079};
RN [1] {ECO:0000313|EMBL:ACS89632.1, 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=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP001463; ACS89632.1; -; Genomic_DNA.
DR RefSeq; WP_015848852.1; NC_012883.1.
DR AlphaFoldDB; C6A1Y7; -.
DR STRING; 604354.TSIB_0567; -.
DR GeneID; 8095555; -.
DR KEGG; tsi:TSIB_0567; -.
DR eggNOG; arCOG01491; Archaea.
DR HOGENOM; CLU_000422_13_3_2; -.
DR OrthoDB; 23466at2157; -.
DR Proteomes; UP000009079; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02766; MopB_3; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009079}.
FT DOMAIN 1..49
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 627 AA; 72046 MW; 39E482F71ECE2CDA CRC64;
MRDCYDTCSI ISELKEGVLR VKGNPSHPIT RGFLCPKGAL LSKWFHSEER LKTPLVREDL
REDFKETGWK EAINFVAARL SETIQKHGSE SVLVYNYAGD RGVVNYAFPL RLFHYLNASM
LDYGICDRAG QEALRDVYGT AVGMDPEDLK NQKLIVYWGV NPFWTNLHGF MLAKRYGLEK
WVVDVVKTET AKKSEKFFQI RPNTDVLFAL GVARVIVESN IYDREFVEKN VYGFEKFVEY
LSTIDLDFVA KETGIQGEKI EEFAFEYAEK KGVIHIGYGL QRSFMGGEAV RAIAILPTLV
GHKFGFIYDM KTIDKSYAEG EFLRTRPVKR IPQMKLAEFI ENGDIKFLYI YNANPLASLP
NQNRLRKAIM KNDVFVVVHD IFLTDTALYA HVVLPASTFF ERLDIADSYY HRYVALNEPV
TQLCGKSNSE VTRLLAKALD IKNPCLYESD EDVIRKILEK NGLSFEELKE RGFVKVEEKE
RFYNTPSGKV EFYSQRAVGR GLPPFPQYNP LKRKGLQLLS PTWKLTITSQ YHNTYNIIDP
YLHISPQDAD ERGIKDNDEV EVFNEYGNIK TRAKVSEDVP SGIVVLYKAF WPKLLGWNVN
FLTTDETVEK YGNGSAYHST WVEVRKI
//
