ID   FDHD_PECAS              Reviewed;         277 AA.
AC   Q6DB09;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Sulfur carrier protein FdhD {ECO:0000255|HAMAP-Rule:MF_00187};
GN   Name=fdhD {ECO:0000255|HAMAP-Rule:MF_00187}; OrderedLocusNames=ECA0093;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG73013.1; -; Genomic_DNA.
DR   RefSeq; WP_011091736.1; NC_004547.2.
DR   AlphaFoldDB; Q6DB09; -.
DR   SMR; Q6DB09; -.
DR   STRING; 218491.ECA0093; -.
DR   EnsemblBacteria; CAG73013; CAG73013; ECA0093.
DR   KEGG; eca:ECA0093; -.
DR   PATRIC; fig|218491.5.peg.95; -.
DR   eggNOG; COG1526; Bacteria.
DR   HOGENOM; CLU_056887_2_0_6; -.
DR   OMA; RYCAGAT; -.
DR   OrthoDB; 948173at2; -.
DR   Proteomes; UP000007966; 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_0000152902"
FT   ACT_SITE        123
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00187"
SQ   SEQUENCE   277 AA;  29803 MW;  A0587FED4637EAB4 CRC64;
     MQVFQVKEVH SQADAVLEGA TQHSVYHPDS LHQPQSDWLA EEVPVALVYN GISHVVMMAS
     PKELEQFALG FSLSEGIIQS PADIYGIDVQ NACNGIEVQI ELSSRRFAGL KERRRSMDGR
     TGCGVCGVEQ LAEIGKPVAP LPFTQTFSLS KLENALVRLR DVQKIGQVTG CTHAASWIAP
     DGTLSGGSED VGRHVALDKL LGARAKQGWQ QGAALVSSRA SYEMVQKSAM CGVEILFAVS
     AATSLAVDVA QRCNLTLVGF CRPGQATIYT HPQRLSE