ID A0A917VDH4_9ACTN Unreviewed; 332 AA.
AC A0A917VDH4;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 08-OCT-2025, entry version 8.
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:GGK65663.1};
GN ORFNames=GCM10007964_05850 {ECO:0000313|EMBL:GGK65663.1};
OS Sphaerisporangium melleum.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Sphaerisporangium.
OX NCBI_TaxID=321316 {ECO:0000313|EMBL:GGK65663.1, ECO:0000313|Proteomes:UP000645217};
RN [1] {ECO:0000313|EMBL:GGK65663.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 13064 {ECO:0000313|EMBL:GGK65663.1};
RX PubMed=25193709;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Walter F., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium casei LMG S-19264T (=DSM
RT 44701T), isolated from a smear-ripened cheese.";
RL Int. J. Syst. Evol. Microbiol. 189:76-77(2014).
RN [2] {ECO:0000313|EMBL:GGK65663.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 13064 {ECO:0000313|EMBL:GGK65663.1};
RA Sun Q., Ohkuma M.;
RL Submitted (SEP-2020) 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:GGK65663.1}.
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DR EMBL; BMNT01000002; GGK65663.1; -; Genomic_DNA.
DR RefSeq; WP_189161339.1; NZ_BMNT01000002.1.
DR Proteomes; UP000645217; 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 NCBIfam; NF001943; PRK00724.1-2; 1.
DR PANTHER; PTHR30592; FORMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR30592:SF1; SULFUR CARRIER PROTEIN FDHD; 1.
DR Pfam; PF02634; FdhD-NarQ; 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:UP000645217}.
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..31
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00187"
FT BINDING 315..320
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00187"
SQ SEQUENCE 332 AA; 34753 MW; 9F14DBB6881939BC CRC64;
MTTTGPGRRP PGAPPRTAAE PPGTRGARPA GGEAGPVVED RWLGPLESGA AVRPGPTRRA
RVREVSATGV RDRRDDLATE EPLEIRLSAG GHTRTLAITM RTPGADFELA AGFLSGEGIA
GPDEIASIAY CTDEDLPPEA RYNTVTVRLH GDTLPDSPAL HRHFVTSSAC GVCGTASLDA
LRTRRTTLGR VAPPALPPVP AEVLYTLPDR LRAAQGVFGK TGGLHAAGLF TADGSLLAVR
EDVGRHNAVD KLVGWALLSG RLPLAANLLL VSGRTSYEIM QKALAAGIPM VCGVSAPSSL
AVDLAREFGL TLVGFLRGER FNIYATPDRV IT
//
