ID A0A1T0AS71_9PAST Unreviewed; 269 AA.
AC A0A1T0AS71;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-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=B0187_05050 {ECO:0000313|EMBL:OOR99131.1};
OS Haemophilus paracuniculus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Pasteurellales; Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=734 {ECO:0000313|EMBL:OOR99131.1, ECO:0000313|Proteomes:UP000190867};
RN [1] {ECO:0000313|EMBL:OOR99131.1, ECO:0000313|Proteomes:UP000190867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 43573 {ECO:0000313|EMBL:OOR99131.1,
RC ECO:0000313|Proteomes:UP000190867};
RA Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome sequence of Haemophilus paracuniculus CCUG 43573 type
RT strain.";
RL Submitted (FEB-2017) 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}.
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:OOR99131.1}.
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DR EMBL; MUYA01000007; OOR99131.1; -; Genomic_DNA.
DR RefSeq; WP_078236779.1; NZ_MUYA01000007.1.
DR AlphaFoldDB; A0A1T0AS71; -.
DR STRING; 734.B0187_05050; -.
DR OrthoDB; 3197277at2; -.
DR Proteomes; UP000190867; 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:UP000190867};
KW Transferase {ECO:0000313|EMBL:OOR99131.1}.
FT ACT_SITE 109
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00187"
FT BINDING 248..253
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00187"
SQ SEQUENCE 269 AA; 28916 MW; 473225A44971F564 CRC64;
MNATTTTQAV RLHQNFTAEI AEERLICEVP VALVYNGISH TVMMCTPTDL ADFALGFSLA
EGILDSPSQL YGLDIVKQAN GIEIQLEIAS RAFVALKEKR RSMAGRTGCG ICGVEQLEQV
SQCKILPKSH RLQGVDPTIL DGCLAQLEQA QQLAHQTGAS HAAAFFSPEG KLLAIREDVG
RHVALDKLLG WHANAGQPLG FVFVTSRASF EMVQKCLACG IEMLCAISAT TEMAVKLAQQ
LEFSLLAFTR KGRTTVYSGG HRVNGVASG
//
