ID   FDHD_SHIFL              Reviewed;         277 AA.
AC   Q83PE5; Q7BZE6;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Sulfur carrier protein FdhD {ECO:0000255|HAMAP-Rule:MF_00187};
GN   Name=fdhD {ECO:0000255|HAMAP-Rule:MF_00187};
GN   OrderedLocusNames=SF3971, S3777;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45406.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18794.1; -; Genomic_DNA.
DR   RefSeq; NP_709699.1; NC_004337.2.
DR   RefSeq; WP_000753620.1; NZ_UIQL01000126.1.
DR   AlphaFoldDB; Q83PE5; -.
DR   SMR; Q83PE5; -.
DR   STRING; 198214.SF3971; -.
DR   EnsemblBacteria; AAN45406; AAN45406; SF3971.
DR   EnsemblBacteria; AAP18794; AAP18794; S3777.
DR   GeneID; 1026226; -.
DR   GeneID; 58391679; -.
DR   KEGG; sfl:SF3971; -.
DR   KEGG; sfx:S3777; -.
DR   PATRIC; fig|198214.7.peg.4679; -.
DR   HOGENOM; CLU_056887_2_0_6; -.
DR   OMA; RYCAGAT; -.
DR   OrthoDB; 948173at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Reference proteome.
FT   CHAIN           1..277
FT                   /note="Sulfur carrier protein FdhD"
FT                   /id="PRO_0000152921"
FT   ACT_SITE        121
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00187"
FT   BINDING         260..265
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00187"
SQ   SEQUENCE   277 AA;  30588 MW;  5F0B9D07D80509D0 CRC64;
     MKKTQRKEIE NVTNITGVRQ IELWRRDDLQ HPRLDEVAEE VPVALVYNGI SHVVMMASPK
     DLEYFALGFS LSEGIIESPR DIFGMDVVPS CNGLEVQIEL SSRRFMGLKE RRRALAGRTG
     CGVCGVEQLN DIGKPVQPLP FTQTFDLNKL DDALRHLNDF QPVGRLTGCT HAAAWMLPSG
     ELVGGHEDVG RHVALDKLLG RRSQEGESWQ QGAVLVSSRA SYEMVQKSAM CGVEILFAVS
     AATTLAVEVA ERCNLTLVGF CKPGRATVYT HPQRLSN