ID A1S025_THEPD Unreviewed; 1170 AA.
AC A1S025;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Formate dehydrogenase alpha subunit {ECO:0000313|EMBL:ABL78805.1};
DE EC=1.2.1.2 {ECO:0000313|EMBL:ABL78805.1};
GN OrderedLocusNames=Tpen_1408 {ECO:0000313|EMBL:ABL78805.1};
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408 {ECO:0000313|EMBL:ABL78805.1, ECO:0000313|Proteomes:UP000000641};
RN [1] {ECO:0000313|Proteomes:UP000000641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5 {ECO:0000313|Proteomes:UP000000641};
RX PubMed=18263724; DOI=10.1128/JB.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
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; CP000505; ABL78805.1; -; Genomic_DNA.
DR RefSeq; WP_011753070.1; NC_008698.1.
DR AlphaFoldDB; A1S025; -.
DR STRING; 368408.Tpen_1408; -.
DR EnsemblBacteria; ABL78805; ABL78805; Tpen_1408.
DR GeneID; 4601822; -.
DR KEGG; tpe:Tpen_1408; -.
DR eggNOG; arCOG01491; Archaea.
DR HOGENOM; CLU_274368_0_0_2; -.
DR OrthoDB; 23466at2157; -.
DR Proteomes; UP000000641; 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 CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 2.20.25.90; ADC-like domains; 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 InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
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:ABL78805.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000641};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 53..109
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1170 AA; 131252 MW; 59DEDA75BBFDC3C2 CRC64;
MPGEIDRRSF LKLAAIAASA LALPVEAQPI PLKPWKTQWG FGEIGGKGDL AKARITPVIC
PYCSMGCSID FYTFGDQILW TEGSPDSYIN FGALCPKGKA AFELVENEMR VTQPMIRTGP
KPPPEEILSA KSWDELVALV KKYPPQWKPV SWDEAFRFIA SRVAKILNEW RSSSGAPKQP
DGYYYVGSKV PIQLIGSSIM VNEAGYLTTK LAEFLGTTNV DSQYRKCHSS TVSSLALTYG
WGAETATIED VALADVVLFF SSPAEAHPLS FQYFLKGKKE RGTIFITFDP RYSRTAMASD
LWVPFRSGTD TAIFLYILHY AFFERDPPID SLDAFKALRS RWNVTDDDLA DFKELIKEYD
AETVSRITGV PVDMLRTVAR IYVENSGVAT NHKKHGVVQW AMGMTQHTNA TINIIRAAAI
MQLLLGNVGF PGGGAHPFRG HSNVQGVTDV QGGGLGALPG YHASPSSTFY VRLYQDWKLQ
GMPDAWNWVV PEWARKTFTT TTPDKGSADL TKILQVYTFY GWRRFELLWG FFCGTVPEDD
PVNGTVVCDF PFGTGSTEIT FPRRVLNGEI RAAFIFGENP AVTNPNAKVI WAALSKLDLL
VVSDIFETET AWFADVLLPA SSFAEVEGTK TNGNRVIQWT YAALNPRGES RPDYWIITKL
FQYLRNYGAV KLPSEVFGLK SEKVKVRKGG RVVLLYERPL RPDASWDYSG GKGAASPIRS
IEAEVNPRII NKEINFAVLI YQGMYDPVRD EFTSMRRDKR LRQPGEIDGL FSSTFKVYKN
WGWSWPMNVR ILYSYTGLAD TLGTTDTVYA AGRQWQATGE TGEWIDEYTG EYRPAFIPGH
NFWLPRAFKR RLSGVADLYG GIDVMHLIRH NELRPLGLFA VEDGGEVKLL TFEEYVASTG
MKYLWANDTL YWDQDTAIAV KATVKRAFFP GGGWRQFKPT YEQMRATLKK YYEQTGNMRD
AVNKTIQELK GWYPGYSFTW PIHTEPVESP DLEMAIRYPT LAWLNSYNLQ VLNEQPDIVR
GKPVGVALTP QDLSSIPGEL VVITTNRLTE HWHSGSMTRR TPLLAELDPE PFVYVPRELA
RKLGVNSGDY VEIITARGSI KMRAYVTEGE AYLTVNGRQL PHVNVVWAFS FLGYVTGPQG
NFISPDVGDV VTTIQETKAW IGKIRKAEVV
//
