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Database: UniProt
Entry: K8DYU0_9FIRM
LinkDB: K8DYU0_9FIRM
Original site: K8DYU0_9FIRM 
ID   K8DYU0_9FIRM            Unreviewed;       262 AA.
AC   K8DYU0;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   02-APR-2025, entry version 48.
DE   RecName: Full=Sulfur carrier protein FdhD {ECO:0000256|HAMAP-Rule:MF_00187};
GN   Name=fdhD {ECO:0000256|HAMAP-Rule:MF_00187,
GN   ECO:0000313|EMBL:CCO08069.1};
GN   ORFNames=DESHY_160193 {ECO:0000313|EMBL:CCO08069.1};
OS   Desulforamulus hydrothermalis Lam5 = DSM 18033.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=1121428 {ECO:0000313|EMBL:CCO08069.1, ECO:0000313|Proteomes:UP000009315};
RN   [1] {ECO:0000313|EMBL:CCO08069.1, ECO:0000313|Proteomes:UP000009315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lam5 / DSM 18033 {ECO:0000313|Proteomes:UP000009315};
RX   PubMed=23405336; DOI=10.1128/genomeA.00114-12;
RA   Amin O., Fardeau M.L., Valette O., Hirschler-Rea A., Barbe V., Medigue C.,
RA   Vacherie B., Ollivier B., Bertin P.N., Dolla A.;
RT   "Genome Sequence of the Sulfate-Reducing Bacterium Desulfotomaculum
RT   hydrothermale Lam5(T).";
RL   Genome Announc. 1:e00114-e00112(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCO08069.1}.
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DR   EMBL; CAOS01000008; CCO08069.1; -; Genomic_DNA.
DR   RefSeq; WP_008411271.1; NZ_CAOS01000008.1.
DR   AlphaFoldDB; K8DYU0; -.
DR   STRING; 1121428.DESHY_160193; -.
DR   eggNOG; COG1526; Bacteria.
DR   OrthoDB; 9782042at2; -.
DR   Proteomes; UP000009315; 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:UP000009315}.
FT   ACT_SITE        106
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00187"
FT   BINDING         245..250
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00187"
SQ   SEQUENCE   262 AA;  28679 MW;  2679DFCF8F8ADE83 CRC64;
     MVWQINKATQ KIVRIKGDKA FVTEDVVARE VPVTLFLNGK EFVTMVCSPQ ALEELAVGFL
     CSEGLLQSPE ELESITVDEE KGLITVQAPG CDAESKFLKR NITSCCGRGR PVFYFVNDAK
     SMNKVTGVLL VTPGQVWDLS DRLEQMSVLF KETGGVHNAA LCAPTEVILF YEDVGRHNAV
     DKIFGRAFLN RIPLHDKILV FSGRVSAEIV IKAGKMGLPV IVSRSAPTDL GLAMAEKLGI
     TVVGFAKSER MNVYTYPARI LG
//
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