ID   FDHD_BORPD              Reviewed;         278 AA.
AC   A9I097;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Sulfur carrier protein FdhD {ECO:0000255|HAMAP-Rule:MF_00187};
GN   Name=fdhD {ECO:0000255|HAMAP-Rule:MF_00187}; OrderedLocusNames=Bpet3686;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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; AM902716; CAP44029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9I097; -.
DR   SMR; A9I097; -.
DR   STRING; 94624.Bpet3686; -.
DR   EnsemblBacteria; CAP44029; CAP44029; Bpet3686.
DR   KEGG; bpt:Bpet3686; -.
DR   eggNOG; COG1526; Bacteria.
DR   OMA; RAFWNLK; -.
DR   Proteomes; UP000001225; 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..278
FT                   /note="Sulfur carrier protein FdhD"
FT                   /id="PRO_1000098779"
FT   ACT_SITE        120
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00187"
SQ   SEQUENCE   278 AA;  29279 MW;  E428F950C6F12CF3 CRC64;
     MDRLYHPAPS RTDCADAAVL RVRGGIVGAA TQSDRVAEET PVALEYNGIS HATMLASPAD
     LEDYALGFSL TEGIVERPAD VRGIEIVPQF NGIVVQVEIS SACAARLKTR RRAMAGRTGC
     GLCGVETLPE VLRQVPTVAD AAPVPLTAVL HGMRAMRGSQ ALHDITGATH AAAWADAEGR
     VQLVREDVGR HNALDKLVGA LARQAIDPRS GMVLVSSRAS FEMVQKCAAA GIGILAAVSA
     PTALAIRVAQ NTNVALLGFV RNADAAIYSH PERLRLRP