ID   FDHD_ECO8A              Reviewed;         277 AA.
AC   B7M697;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Sulfur carrier protein FdhD {ECO:0000255|HAMAP-Rule:MF_00187};
GN   Name=fdhD {ECO:0000255|HAMAP-Rule:MF_00187}; OrderedLocusNames=ECIAI1_4100;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928160; CAR00871.1; -; Genomic_DNA.
DR   RefSeq; WP_000753617.1; NC_011741.1.
DR   AlphaFoldDB; B7M697; -.
DR   SMR; B7M697; -.
DR   KEGG; ecr:ECIAI1_4100; -.
DR   HOGENOM; CLU_056887_2_0_6; -.
DR   OMA; RYCAGAT; -.
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..277
FT                   /note="Sulfur carrier protein FdhD"
FT                   /id="PRO_1000118559"
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;  30560 MW;  9E42BBDCB5B3D0F4 CRC64;
     MKKTQRKEIE NVTNITGVRQ IELWRRDDLQ HPRLDEVAEE VPVALVYNGI SHVVMMASPK
     DLEYFALGFS LSEGIIESPR DIFGMDVVPS CNGLEVQIEL SSRRFMGLKE RRRALAGRTG
     CGVCGVEQLN DIGKPVQPLP FTQTFDLNKL DDALRHLNDF QPVGQLTGCT HAAAWMLPSG
     ELVGGHEDVG RHVALDKLLG RRSQEGESWQ QGAVLVSSRA SYEMVQKSAM CGVEILFAVS
     AATTLAVEVA ERCNLTLVGF CKPGRATVYT HPQRLSN