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Database: UniProt
Entry: A0AAF1KUA0_9PROT
LinkDB: A0AAF1KUA0_9PROT
Original site: A0AAF1KUA0_9PROT 
ID   A0AAF1KUA0_9PROT        Unreviewed;       270 AA.
AC   A0AAF1KUA0;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   02-APR-2025, entry version 4.
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:MBR0655797.1};
GN   ORFNames=GXW79_12005 {ECO:0000313|EMBL:MBR0655797.1};
OS   Plastoroseomonas arctica.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Acetobacterales; Acetobacteraceae; Plastoroseomonas.
OX   NCBI_TaxID=1509237 {ECO:0000313|EMBL:MBR0655797.1, ECO:0000313|Proteomes:UP001196068};
RN   [1] {ECO:0000313|EMBL:MBR0655797.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMG 28251 {ECO:0000313|EMBL:MBR0655797.1};
RA   Rat A.;
RL   Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBR0655797.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMG 28251 {ECO:0000313|EMBL:MBR0655797.1};
RA   Rat A., Naranjo H.D., Lebbe L., Cnockaert M., Krigas N., Grigoriadou K.,
RA   Maloupa E., Willems A.;
RT   "Roseomonas hellenica sp. nov., isolated from roots of wild-growing Alkanna
RT   tinctoria.";
RL   Syst. Appl. Microbiol. 44:0-0(2021).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-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:MBR0655797.1}.
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DR   EMBL; JAAEDH010000012; MBR0655797.1; -; Genomic_DNA.
DR   Proteomes; UP001196068; 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:UP001196068}.
FT   ACT_SITE        113
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00187"
SQ   SEQUENCE   270 AA;  27852 MW;  3FBE102D0A0F4E58 CRC64;
     MNAIPPPLIS LPRTAYTGAA LMAGERMLAE ETGIALSYDG VTHAVMMASP ADLEDFAVGF
     SLSEGIVATP AEITDMEVLS RAGLGIEIRM RLAEIPGSRH VRRRRALAGP VGCGLCGIES
     LQEAACPADP VLSDFRAWPG AIAEAMQALC DAQAMNGQAA AVHAAAFWRP AEGLVAIRED
     VGRHNALDKL AGAMARAGIG ATSGVVALTS RVSVEMVQKA ARMGAPIIAA ISAPTALAVR
     TAEACGMTLL AVARGECFEV FTHPARVIGV
//
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