ID   FDHD_YERE8              Reviewed;         275 AA.
AC   A1JT32;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Sulfur carrier protein FdhD {ECO:0000255|HAMAP-Rule:MF_00187};
GN   Name=fdhD {ECO:0000255|HAMAP-Rule:MF_00187}; OrderedLocusNames=YE4137;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Required for formate dehydrogenase (FDH) activity. Acts as a
CC       sulfur carrier protein that transfers sulfur from IscS to the
CC       molybdenum cofactor prior to its insertion into FDH.
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; AM286415; CAL14153.1; -; Genomic_DNA.
DR   RefSeq; YP_001008273.1; NC_008800.1.
DR   AlphaFoldDB; A1JT32; -.
DR   SMR; A1JT32; -.
DR   STRING; 393305.YE4137; -.
DR   EnsemblBacteria; CAL14153; CAL14153; YE4137.
DR   KEGG; yen:YE4137; -.
DR   PATRIC; fig|393305.7.peg.4403; -.
DR   eggNOG; COG1526; Bacteria.
DR   HOGENOM; CLU_056887_2_0_6; -.
DR   OMA; RYCAGAT; -.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097163; F:sulfur carrier activity; IEA:UniProtKB-UniRule.
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; 1.
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.
FT   CHAIN           1..275
FT                   /note="Sulfur carrier protein FdhD"
FT                   /id="PRO_1000020830"
FT   ACT_SITE        121
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00187"
FT   BINDING         258..263
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00187"
SQ   SEQUENCE   275 AA;  29913 MW;  9EC2F5CDC74FAC71 CRC64;
     MSQIKPSDID LSTEICGARQ LNVLQRHHMA EPQLDWLAEE VPVALVYNGI SHVVMMATPK
     DLEAFALGFS LSEGIITAPQ EIYAIDVTPS CNGIEVNIEL SSRRFAGLKE RRRAMAGRTG
     CGVCGIEQLD DIFRPIAPLP FTQTFNLNQL DNALAQLKQV QTVGQLTGCT HAAAWINPQG
     ELLGGCEDVG RHVALDKLLG VRAKQPWQQG AVLVSSRASY EMVQKTAMCG AEILFAVSAA
     TTLAVEVAER YNLTLVGFSK PGRATVYTHP NRIQE