FDHD_ECOLI
ID FDHD_ECOLI Reviewed; 277 AA.
AC P32177; Q2M8J2;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Sulfur carrier protein FdhD {ECO:0000255|HAMAP-Rule:MF_00187, ECO:0000305};
DE AltName: Full=Sulfurtransferase FdhD {ECO:0000303|PubMed:22194618};
GN Name=fdhD {ECO:0000255|HAMAP-Rule:MF_00187, ECO:0000303|PubMed:3077634};
GN OrderedLocusNames=b3895, JW3866;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=3077634; DOI=10.1099/00221287-134-12-3129;
RA Mandrand-Berthelot M.A., Couchoux-Luthaud G., Santini C.L., Giordano G.;
RT "Mutants of Escherichia coli specifically deficient in respiratory formate
RT dehydrogenase activity.";
RL J. Gen. Microbiol. 134:3129-3139(1988).
RN [5]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=2170340; DOI=10.1128/jb.172.10.6112-6121.1990;
RA Schlindwein C., Giordano G., Santini C.L., Mandrand M.A.;
RT "Identification and expression of the Escherichia coli fdhD and fdhE genes,
RT which are involved in the formation of respiratory formate dehydrogenase.";
RL J. Bacteriol. 172:6112-6121(1990).
RN [6]
RP FUNCTION.
RX PubMed=8522521; DOI=10.1128/jb.177.24.7141-7149.1995;
RA Abaibou H., Pommier J., Giordano G., Mandrand-Berthelot M.-A.;
RT "Expression and characterization of the Escherichia coli fdo locus and a
RT possible physiological role for aerobic formate dehydrogenase.";
RL J. Bacteriol. 177:7141-7149(1995).
RN [7]
RP FUNCTION, INTERACTION WITH ISCS, ACTIVE SITE, AND MUTAGENESIS OF CYS-121
RP AND CYS-124.
RX PubMed=22194618; DOI=10.1074/jbc.m111.327122;
RA Thome R., Gust A., Toci R., Mendel R., Bittner F., Magalon A.,
RA Walburger A.;
RT "A sulfurtransferase is essential for activity of formate dehydrogenases in
RT Escherichia coli.";
RL J. Biol. Chem. 287:4671-4678(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH GDP, FUNCTION,
RP SUBUNIT, MOLYBDENUM-BINDING, AND MUTAGENESIS OF HIS-171; SER-240 AND
RP PHE-260.
RX PubMed=25649206; DOI=10.1038/ncomms7148;
RA Arnoux P., Ruppelt C., Oudouhou F., Lavergne J., Siponen M.I., Toci R.,
RA Mendel R.R., Bittner F., Pignol D., Magalon A., Walburger A.;
RT "Sulphur shuttling across a chaperone during molybdenum cofactor
RT maturation.";
RL Nat. Commun. 6:6148-6148(2015).
CC -!- FUNCTION: Required for formate dehydrogenase (FDH) activity
CC (PubMed:3077634, PubMed:8522521, PubMed:22194618, PubMed:25649206).
CC Acts as a sulfur carrier protein that transfers sulfur from IscS to the
CC molybdenum cofactor prior to its insertion into FDH. Specifically
CC interacts with IscS and stimulates its cysteine desulfurase activity.
CC Also binds the molybdenum cofactor (PubMed:22194618, PubMed:25649206).
CC Required for activity of formate dehydrogenase N (FDH-N), formate
CC dehydrogenase O (FDH-O) and formate dehydrogenase H (FDH-H)
CC (PubMed:3077634, PubMed:8522521, PubMed:22194618).
CC {ECO:0000269|PubMed:22194618, ECO:0000269|PubMed:25649206,
CC ECO:0000269|PubMed:3077634, ECO:0000269|PubMed:8522521}.
CC -!- SUBUNIT: Homodimer (PubMed:25649206). Interacts with IscS
CC (PubMed:22194618). {ECO:0000269|PubMed:22194618,
CC ECO:0000269|PubMed:25649206}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00187,
CC ECO:0000269|PubMed:2170340}.
CC -!- INDUCTION: Repressed by aerobiosis. {ECO:0000269|PubMed:2170340}.
CC -!- DISRUPTION PHENOTYPE: Mutants lack FDH-N activity and exhibit defects
CC in FDH-H activity. {ECO:0000269|PubMed:3077634}.
CC -!- SIMILARITY: Belongs to the FdhD family. {ECO:0000255|HAMAP-
CC Rule:MF_00187, ECO:0000305}.
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DR EMBL; L19201; AAB03028.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76877.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77414.1; -; Genomic_DNA.
DR PIR; S40839; S40839.
DR RefSeq; NP_418331.1; NC_000913.3.
DR RefSeq; WP_000753617.1; NZ_STEB01000017.1.
DR PDB; 4PDE; X-ray; 2.80 A; A=1-277.
DR PDBsum; 4PDE; -.
DR AlphaFoldDB; P32177; -.
DR SMR; P32177; -.
DR BioGRID; 4263324; 13.
DR BioGRID; 852690; 1.
DR DIP; DIP-9570N; -.
DR IntAct; P32177; 20.
DR STRING; 511145.b3895; -.
DR jPOST; P32177; -.
DR PaxDb; P32177; -.
DR PRIDE; P32177; -.
DR EnsemblBacteria; AAC76877; AAC76877; b3895.
DR EnsemblBacteria; BAE77414; BAE77414; BAE77414.
DR GeneID; 948393; -.
DR KEGG; ecj:JW3866; -.
DR KEGG; eco:b3895; -.
DR PATRIC; fig|1411691.4.peg.2812; -.
DR EchoBASE; EB1805; -.
DR eggNOG; COG1526; Bacteria.
DR HOGENOM; CLU_056887_2_0_6; -.
DR InParanoid; P32177; -.
DR OMA; RYCAGAT; -.
DR PhylomeDB; P32177; -.
DR BioCyc; EcoCyc:EG11859-MON; -.
DR PRO; PR:P32177; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IDA:EcoCyc.
DR GO; GO:0097163; F:sulfur carrier activity; IMP:EcoCyc.
DR GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:EcoCyc.
DR HAMAP; MF_00187; FdhD; 1.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR003786; FdhD.
DR PANTHER; PTHR30592; PTHR30592; 1.
DR Pfam; PF02634; FdhD-NarQ; 1.
DR PIRSF; PIRSF015626; FdhD; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR TIGRFAMs; TIGR00129; fdhD_narQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Molybdenum cofactor biosynthesis;
KW Reference proteome.
FT CHAIN 1..277
FT /note="Sulfur carrier protein FdhD"
FT /id="PRO_0000152899"
FT ACT_SITE 121
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00187,
FT ECO:0000269|PubMed:22194618"
FT BINDING 260..265
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00187,
FT ECO:0000305|PubMed:25649206"
FT MUTAGEN 121
FT /note="C->A: Prevents sulfur transfer from IscS and impairs
FT FDH-H activity."
FT /evidence="ECO:0000269|PubMed:22194618"
FT MUTAGEN 124
FT /note="C->A: Does not affect sulfur transfer from IscS, but
FT abolishes FDH-H activity."
FT /evidence="ECO:0000269|PubMed:22194618"
FT MUTAGEN 171
FT /note="H->A: Does not affect overall structural integrity,
FT but cannot promote FDH activity."
FT /evidence="ECO:0000269|PubMed:25649206"
FT MUTAGEN 240
FT /note="S->D: Strongly impairs FDH activity."
FT /evidence="ECO:0000269|PubMed:25649206"
FT MUTAGEN 260
FT /note="F->D: Strongly impairs FDH activity."
FT /evidence="ECO:0000269|PubMed:25649206"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:4PDE"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:4PDE"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:4PDE"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:4PDE"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:4PDE"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:4PDE"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4PDE"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:4PDE"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:4PDE"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:4PDE"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4PDE"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:4PDE"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:4PDE"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:4PDE"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:4PDE"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:4PDE"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:4PDE"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:4PDE"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:4PDE"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:4PDE"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:4PDE"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:4PDE"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:4PDE"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:4PDE"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:4PDE"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4PDE"
SQ SEQUENCE 277 AA; 30560 MW; 9E42BBDCB5B3D0F4 CRC64;
MKKTQRKEIE NVTNITGVRQ IELWRRDDLQ HPRLDEVAEE VPVALVYNGI SHVVMMASPK
DLEYFALGFS LSEGIIESPR DIFGMDVVPS CNGLEVQIEL SSRRFMGLKE RRRALAGRTG
CGVCGVEQLN DIGKPVQPLP FTQTFDLNKL DDALRHLNDF QPVGQLTGCT HAAAWMLPSG
ELVGGHEDVG RHVALDKLLG RRSQEGESWQ QGAVLVSSRA SYEMVQKSAM CGVEILFAVS
AATTLAVEVA ERCNLTLVGF CKPGRATVYT HPQRLSN
