ID   FDHD_BORBR              Reviewed;         276 AA.
AC   Q7WMS0;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Sulfur carrier protein FdhD {ECO:0000255|HAMAP-Rule:MF_00187};
GN   Name=fdhD {ECO:0000255|HAMAP-Rule:MF_00187}; OrderedLocusNames=BB1320;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(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; BX640441; CAE31818.1; -; Genomic_DNA.
DR   RefSeq; WP_003809308.1; NC_002927.3.
DR   AlphaFoldDB; Q7WMS0; -.
DR   SMR; Q7WMS0; -.
DR   STRING; 257310.BB1320; -.
DR   EnsemblBacteria; CAE31818; CAE31818; BB1320.
DR   GeneID; 56480006; -.
DR   KEGG; bbr:BB1320; -.
DR   eggNOG; COG1526; Bacteria.
DR   HOGENOM; CLU_056887_2_0_4; -.
DR   OMA; RAFWNLK; -.
DR   OrthoDB; 948173at2; -.
DR   Proteomes; UP000001027; 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..276
FT                   /note="Sulfur carrier protein FdhD"
FT                   /id="PRO_0000152891"
FT   ACT_SITE        120
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00187"
SQ   SEQUENCE   276 AA;  29097 MW;  26FB63008F872B1F CRC64;
     MDRLHTSSAD WPDHLATQVV RVRGGVLQAA GQSDHVAEET PVALEFNGIS HATMLVTPTH
     LDDFALGFAL TEGIVGGMAD VRGVELETRC DGIVVQVEIA TSCEVRLKER RRAMAGRTGC
     GLCGVETLPE VVRDVAPVAD SDALPVHNVL RAMQSLRSRQ TLHDATGATH AAGWADASGE
     VVLAREDVGR HNALDKLIGA LARQGIAPLP GMAVVSSRAS FEMVQKTASA GIPILAAVSA
     PTALAIRLAR QTNVTLLGFV RNTDATIYSH PQRIAA