ID G4RJU8_THETK Unreviewed; 1175 AA.
AC G4RJU8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Formate dehydrogenase alpha subunit {ECO:0000313|EMBL:CCC81843.1};
DE EC=1.2.1.2 {ECO:0000313|EMBL:CCC81843.1};
GN Name=fdhA {ECO:0000313|EMBL:CCC81843.1};
GN OrderedLocusNames=TTX_1203 {ECO:0000313|EMBL:CCC81843.1};
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679 {ECO:0000313|EMBL:CCC81843.1, ECO:0000313|Proteomes:UP000002654};
RN [1] {ECO:0000313|EMBL:CCC81843.1, ECO:0000313|Proteomes:UP000002654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1
RC {ECO:0000313|Proteomes:UP000002654};
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(2011).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FN869859; CCC81843.1; -; Genomic_DNA.
DR RefSeq; WP_014127098.1; NC_016070.1.
DR AlphaFoldDB; G4RJU8; -.
DR STRING; 768679.TTX_1203; -.
DR PaxDb; 768679-TTX_1203; -.
DR GeneID; 11262088; -.
DR KEGG; ttn:TTX_1203; -.
DR PATRIC; fig|768679.9.peg.1211; -.
DR eggNOG; arCOG01491; Archaea.
DR HOGENOM; CLU_274368_0_0_2; -.
DR OrthoDB; 23466at2157; -.
DR Proteomes; UP000002654; 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:UniProtKB-KW.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43598:SF5; DMSO REDUCTASE CHAIN A; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 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; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CCC81843.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002654};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 52..108
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1175 AA; 130526 MW; A32FEBE3BD39E74E CRC64;
MTVSTTRRGF LKISALAALA LGLPSSAQSP LILQKTSWTL GEIGGKSALT RTRVTPVICP
FCSMGCSIDF YTAGNDVVWT SGSSDSYINW GALCPKGKVA YQLVTNPKRL DSPMIRTGPK
PPVEEILSAK TWDDLVAVVK RYPPQWEKVS WEEAFTFIAR RLASILNQWR NATGAPVQKD
GYYYVGTNNP VMVIGSSILT NEEAYLSRKL AAFLGTSNTD SQYRKCHSST VTALALTYGW
GAETASIEDV ALADVVLFFS SPAEAHPLSF YYFLKGKRER GTILITFDPR YSRTAEASDI
WVPFRPGTDT AILNYILHYA FFERNPPIDQ LPEFQRLMAQ RWNITQDDLE DLKALISEYD
LQTVANITGA PPDLLRTVAS IFVENSGVVT GHKKHGVIQW AMGFTQHTDA TLSIIRAAAI
VQLLLGNVGY PGGGTHPFRG HSNVQGATDV QGGGLGVLPG YHAQPATSFD VRLYQEWKLQ
GMPDAWNWEV PDWALKSFST STPSRGAADV AKALAVYNFY GWRRFELLWG IYCGTIPPDD
PVNGKVVCDI PFGTGYSEVT FIRNALAGKI NAALIFAENP AVTNPNVKLV MAALSSLQLL
VLTDIFETET AWFADVVLPG AAFAEKEGTR TDGNRVIQWT WRAVPPRGEA RPDYWIIAGL
YKYLRKEGAV LLPSEVAGVN KEEVKFRKRG NIIFVYERPL RPDHSWDYSG GVGSSAPISD
IEAEVNPRII TKEINYAVMI YQGIYDPVRD SFTPMRRSNE LRKPGEIDGT FSSTFKVYKN
WGWSWPMNVR FMYNFDSLEV ILGKPDVVNA AGQQWTVTGE TGEIIDEYTG EYRPAFVPGH
NFFAPKTFKR RLSGVADLFG GLDLMKFIRT GEKVFLGKFV VETDTGVQLV DFDSYAAMTG
MRYLWANDAL YWDQETLSDK AFLKRVFYPG SGWRQFKPTY EKMRSLLKQY YQQLGDLKAA
TLKVIQEMGG WYKGYTFQWP IHAEPVESPV TDMAISYPTL AWLNPYNLMV LNNQPDVVSR
GMTGVALDPK ELQAELQGLG ITGITVALTS NRLTEHWHSG SMTRNIPDLV ELVPRPFAIV
SKSLAQQLGI NSGDYVEIWT ARGGIKLRAF VTDGEAYVSV NGQTVPVVNV VWSWSFQGTD
TGASANFLVP DVGDVITTIQ ESKAWLGMIR KAPSV
//
