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Database: UniProt
Entry: A0A1I0WDG6_9CLOT
LinkDB: A0A1I0WDG6_9CLOT
Original site: A0A1I0WDG6_9CLOT 
ID   A0A1I0WDG6_9CLOT        Unreviewed;       263 AA.
AC   A0A1I0WDG6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   02-APR-2025, entry version 20.
DE   RecName: Full=Sulfur carrier protein FdhD {ECO:0000256|HAMAP-Rule:MF_00187};
GN   Name=fdhD {ECO:0000256|HAMAP-Rule:MF_00187};
GN   ORFNames=SAMN04488528_100511 {ECO:0000313|EMBL:SFA86789.1};
OS   Clostridium frigidicarnis.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=84698 {ECO:0000313|EMBL:SFA86789.1, ECO:0000313|Proteomes:UP000198619};
RN   [1] {ECO:0000313|EMBL:SFA86789.1, ECO:0000313|Proteomes:UP000198619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12271 {ECO:0000313|EMBL:SFA86789.1,
RC   ECO:0000313|Proteomes:UP000198619};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00187}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00187}.
CC   -!- SIMILARITY: Belongs to the FdhD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00187}.
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DR   EMBL; FOKI01000005; SFA86789.1; -; Genomic_DNA.
DR   RefSeq; WP_090039054.1; NZ_FOKI01000005.1.
DR   AlphaFoldDB; A0A1I0WDG6; -.
DR   STRING; 84698.SAMN04488528_100511; -.
DR   OrthoDB; 9782042at2; -.
DR   Proteomes; UP000198619; Unassembled WGS sequence.
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   Gene3D; 3.10.20.10; -; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   HAMAP; MF_00187; FdhD; 1.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR003786; FdhD.
DR   NCBIfam; TIGR00129; fdhD_narQ; 1.
DR   PANTHER; PTHR30592; FORMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR30592:SF1; SULFUR CARRIER PROTEIN FDHD; 1.
DR   Pfam; PF02634; FdhD-NarQ; 1.
DR   PIRSF; PIRSF015626; FdhD; 1.
DR   SUPFAM; SSF53927; Cytidine deaminase-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00187};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW   ECO:0000256|HAMAP-Rule:MF_00187};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198619}.
FT   ACT_SITE        121
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00187"
FT   BINDING         244..249
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00187"
SQ   SEQUENCE   263 AA;  29805 MW;  477545DDEC5B0F54 CRC64;
     MDKILKCNVI KLEEDKEYIC EESIVCEYPL TIFLNKEKLA TLLCSPENLK ELVIGFFRTE
     ELIKDLNEIE KINIDESMGI AQVETKGHLK INKFQCKKLE IQDNNMSYED NVKEFLESMS
     CNAISTKVKI QKKKIYEFMN KNLNHSSTFK NTGGVHTIAL CDEDDVLVIC EDVARHNAMD
     KVIGSSIIKS INLKDKIMIL SGRVSLEMIL KAARLEIPII ISKSAPTSLS LGLAKKLNIT
     LVGFVRGNRM NIYANGDRII ENN
//
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