ID C0QCD8_DESAH Unreviewed; 1029 AA.
AC C0QCD8;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=FdhA7 {ECO:0000313|EMBL:ACN17155.1};
DE EC=1.2.1.2 {ECO:0000313|EMBL:ACN17155.1};
GN Name=fdhA7 {ECO:0000313|EMBL:ACN17155.1};
GN OrderedLocusNames=HRM2_40980 {ECO:0000313|EMBL:ACN17155.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN17155.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN17155.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
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; CP001087; ACN17155.1; -; Genomic_DNA.
DR STRING; 177437.HRM2_40980; -.
DR KEGG; dat:HRM2_40980; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_1_0_7; -.
DR OrthoDB; 9757870at2; -.
DR Proteomes; UP000000442; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
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:0045333; P:cellular respiration; IEA:InterPro.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR CDD; cd02752; MopB_Formate-Dh-Na-like; 1.
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; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006443; Formate-DH-alph_fdnG.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR01553; formate-DH-alph; 1.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 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; 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:ACN17155.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000442};
KW Selenium {ECO:0000313|EMBL:ACN17155.1};
KW Selenocysteine {ECO:0000313|EMBL:ACN17155.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 43..102
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT NON_STD 192
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:ACN17155.1"
SQ SEQUENCE 1029 AA; 114866 MW; 05DA41102DC928F3 CRC64;
MSFSRREFLK VSGVTAAGIA ASGLGFDLTP VKVHAQTLKT IYAKETTTVC CYCAVGCGAI
VHTSQRGDGR VINIEGDPDH VINRGALCSK GASLKQLIEN ENRLTEPMYR APYSKEWKTV
SWDWALDRIA ARVKETRDGG FDQTNAKGQQ VNRTMAMASV GSAAMDNEEC WIYQALMRSL
GLVYVEHQAR IUHSATVAAL AESFGRGAMT NHWIDIRNAD CVLIMGSNAA ENHPISFKYV
NQAMEKGAKL INVDPRFTRT SSKADIYAPL RSGTDIAFLG GMIKYILDND LYNNEYTAAY
TNAPFIVGKK FGFKDGLFSG YTKGESGPSR GGYDKGTWAF EMDEKGVPMT DPSMKHERSV
FQLLKKHYQR YNLDTVSKIT GTPKKDLMTV YETYAATGKR GKAGTIMYAM GWTQHTVGTQ
MIRTMAMIQL LLGNMGVAGG GVNALRGESN VQGSTDQCLL WHIWPGYLKT PVASDTTFDA
YNKHWTPHSN DPLSANWWQN YPKYSTSLLK SFFGANATES NQFGFPWLPK VDSGASYSWF
DIFDAMYKDK IKGFFAWGQN PACSGANAGK IRKAMEKLDW MVNVNLFDNE TGSFWNGPGT
DPSKIKTEVF MLPASASVEK EGSITNSGRW MQWRYRGPMP LGNSRPDGDI ILDLGRRIKK
LYRTGGVFPE PIVNLKWNYE SHGEYDAHKV AKEINGYFLK DVTIKGTTYK KGTLVPSFAF
LQSDGSTSSA NWLYCNSYTE KGNMSARRGQ KDAPNNIGLY PEFAWCWPVN RRILYNRASV
DTKGRPWNKD LPVISFAGEE KGGKWTTSKW VGDVPDGGWY PLENPDGTRR EDSKNPFIML
KDGMGQIFGP GRADGPFPEH YEPLECPVSE NYLNPQLTNP TAVVYSTKDD QHATCDPRFP
FVGTTYRVSE HWQTGLMTRP QAWLMELQPQ VFVEMSEELA KLRDITNGER VKVSTARASL
ECTAVVTKRF KPFWVGDAVV HQVGVPWHYG WRWPATGTEE SANLLTPPAG DPNTRIPETK
AFMVNVTKL
//
