ID   FDHD_METJA              Reviewed;         227 AA.
AC   Q57743;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Protein FdhD {ECO:0000255|HAMAP-Rule:MF_00187};
GN   Name=fdhD {ECO:0000255|HAMAP-Rule:MF_00187}; OrderedLocusNames=MJ0295;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Required for formate dehydrogenase (FDH) activity.
CC       {ECO:0000255|HAMAP-Rule:MF_00187}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00187}.
CC   -!- SIMILARITY: Belongs to the FdhD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00187}.
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DR   EMBL; L77117; AAB98280.1; -; Genomic_DNA.
DR   PIR; H64336; H64336.
DR   RefSeq; WP_010869793.1; NC_000909.1.
DR   AlphaFoldDB; Q57743; -.
DR   SMR; Q57743; -.
DR   STRING; 243232.MJ_0295; -.
DR   EnsemblBacteria; AAB98280; AAB98280; MJ_0295.
DR   GeneID; 1451150; -.
DR   KEGG; mja:MJ_0295; -.
DR   eggNOG; arCOG04358; Archaea.
DR   HOGENOM; CLU_056887_4_2_2; -.
DR   InParanoid; Q57743; -.
DR   OMA; WAALFDF; -.
DR   OrthoDB; 68783at2157; -.
DR   PhylomeDB; Q57743; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00187; FdhD; 1.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR003786; FdhD.
DR   PANTHER; PTHR30592; PTHR30592; 2.
DR   Pfam; PF02634; FdhD-NarQ; 1.
DR   PIRSF; PIRSF015626; FdhD; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   TIGRFAMs; TIGR00129; fdhD_narQ; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Molybdenum cofactor biosynthesis; Reference proteome.
FT   CHAIN           1..227
FT                   /note="Protein FdhD"
FT                   /id="PRO_0000152936"
FT   BINDING         210..215
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00187"
SQ   SEQUENCE   227 AA;  26119 MW;  80CCC2FCF90D43CC CRC64;
     MIKKVKIKKF NGRDFYDMED YVAVEESYNI FINGEFVKSL SMSPNFLNEF AVGFAISEGF
     LNKIDKVEVD KNNINIFGEK NDREIKNNKN NKEIKIDIEI IKKIISYEIK AKYWEITGSF
     HWASMFDLKG NSIIFVEDIG RHNAVDKVIG YAILNNYNLN KLILRYSGRI PSDIVKKAIN
     SGLNIIISKS PPTDKAIELA EENNILLIGF ARNGKFNIYT SGRLWEE