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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//