FDHD_ESCF3
ID FDHD_ESCF3 Reviewed; 278 AA.
AC B7LVF3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Sulfur carrier protein FdhD {ECO:0000255|HAMAP-Rule:MF_00187};
GN Name=fdhD {ECO:0000255|HAMAP-Rule:MF_00187}; OrderedLocusNames=EFER_3881;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
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; CU928158; CAQ91316.1; -; Genomic_DNA.
DR RefSeq; WP_000753607.1; NC_011740.1.
DR AlphaFoldDB; B7LVF3; -.
DR SMR; B7LVF3; -.
DR EnsemblBacteria; CAQ91316; CAQ91316; EFER_3881.
DR KEGG; efe:EFER_3881; -.
DR HOGENOM; CLU_056887_2_0_6; -.
DR OMA; RYCAGAT; -.
DR OrthoDB; 948173at2; -.
DR BioCyc; EFER585054:EFER_RS19385-MON; -.
DR Proteomes; UP000000745; 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..278
FT /note="Sulfur carrier protein FdhD"
FT /id="PRO_1000118561"
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 278 AA; 30664 MW; 4D7A068BCF149F17 CRC64;
MKKTQQKEIK NVTNITGVRQ IELWRRDDLQ HPRIDEVAEE VPVALVYNGI SHVVMMASPK
DLEYFALGFS LSEGIIESPR DIFGMDVVPS CNGLEVQIEL SSRRFMGLKE RRRALAGRTG
CGVCGVEQLN DIGKPVQPLP FTQAFDLNKL DDALRHLNDF QPVGQLTGCT HAAAWMLPSG
ELVGGHEDVG RHVALDKLLG RRSQEGESWQ QGAVLVSSRA SYEMVQKSAM CGVEILFAVS
AATTLAVEVA ERCNLTLVGF CKPGRATVYT HPQRLIHN