FDHD_YERPA
ID FDHD_YERPA Reviewed; 274 AA.
AC Q1C3I5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Sulfur carrier protein FdhD {ECO:0000255|HAMAP-Rule:MF_00187};
GN Name=fdhD {ECO:0000255|HAMAP-Rule:MF_00187}; OrderedLocusNames=YPA_3025;
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG14987.1; -; Genomic_DNA.
DR RefSeq; WP_002209612.1; NZ_CP009906.1.
DR AlphaFoldDB; Q1C3I5; -.
DR SMR; Q1C3I5; -.
DR EnsemblBacteria; ABG14987; ABG14987; YPA_3025.
DR GeneID; 57974655; -.
DR KEGG; ypa:YPA_3025; -.
DR OMA; RYCAGAT; -.
DR Proteomes; UP000001971; 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..274
FT /note="Sulfur carrier protein FdhD"
FT /id="PRO_1000020831"
FT ACT_SITE 121
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00187"
FT BINDING 258..263
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00187"
SQ SEQUENCE 274 AA; 29735 MW; 684ECCD9FAFD455C CRC64;
MSQIKPSRLS SSAEIRGARQ LDVLQRHKLA EPQQDWLAEE VPVALVYNGI SHVVMMATPK
DLAAFALGFS LSEGIISSPQ EIYSIEMTPG CNGIEVNIEL SSRRFAGLKE RRRAMAGRTG
CGVCGIEQLD DIFRPITPLP FTQAFNLEHL DTALAQLKQV QPVGQLTGCT HAAAWINPEG
ELLGGCEDVG RHVALDKLLG IRAKQPWQQG AVLVSSRASY EMVQKTAMCG AEILFAVSAA
TTLAVEVAER CNLTLVGFSK PGRATVYTHP QRIK