FOLD_CAMJE
ID FOLD_CAMJE Reviewed; 282 AA.
AC Q0PA35;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Bifunctional protein FolD {ECO:0000255|HAMAP-Rule:MF_01576};
DE Includes:
DE RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01576};
DE EC=1.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01576};
DE Includes:
DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01576};
DE EC=3.5.4.9 {ECO:0000255|HAMAP-Rule:MF_01576};
GN Name=folD {ECO:0000255|HAMAP-Rule:MF_01576}; OrderedLocusNames=Cj0855;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
RG Center for structural genomics of infectious diseases (CSGID);
RT "Crystal structure of FolD bifunctional protein.";
RL Submitted (OCT-2010) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to
CC 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-
CC methenyltetrahydrofolate to 10-formyltetrahydrofolate.
CC {ECO:0000255|HAMAP-Rule:MF_01576}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-
CC methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812,
CC ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01576};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,10-methenyltetrahydrofolate + H2O = (6S)-10-
CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:57455; EC=3.5.4.9; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01576};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000255|HAMAP-Rule:MF_01576}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.2}.
CC -!- SIMILARITY: Belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000255|HAMAP-Rule:MF_01576}.
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DR EMBL; AL111168; CAL34983.1; -; Genomic_DNA.
DR PIR; G81358; G81358.
DR RefSeq; WP_002864845.1; NC_002163.1.
DR RefSeq; YP_002344262.1; NC_002163.1.
DR PDB; 3P2O; X-ray; 2.23 A; A/B=1-282.
DR PDB; 6DE8; X-ray; 2.10 A; A/B=1-282.
DR PDB; 6DEB; X-ray; 1.70 A; A/B=1-282.
DR PDBsum; 3P2O; -.
DR PDBsum; 6DE8; -.
DR PDBsum; 6DEB; -.
DR AlphaFoldDB; Q0PA35; -.
DR SMR; Q0PA35; -.
DR IntAct; Q0PA35; 36.
DR STRING; 192222.Cj0855; -.
DR PaxDb; Q0PA35; -.
DR PRIDE; Q0PA35; -.
DR EnsemblBacteria; CAL34983; CAL34983; Cj0855.
DR GeneID; 905155; -.
DR KEGG; cje:Cj0855; -.
DR PATRIC; fig|192222.6.peg.843; -.
DR eggNOG; COG0190; Bacteria.
DR HOGENOM; CLU_034045_2_1_7; -.
DR OMA; HIVGRPM; -.
DR UniPathway; UPA00193; -.
DR EvolutionaryTrace; Q0PA35; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR HAMAP; MF_01576; THF_DHG_CYH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000672; THF_DH/CycHdrlase.
DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR InterPro; IPR020867; THF_DH/CycHdrlase_CS.
DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR Pfam; PF00763; THF_DHG_CYH; 1.
DR Pfam; PF02882; THF_DHG_CYH_C; 1.
DR PRINTS; PR00085; THFDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00766; THF_DHG_CYH_1; 1.
DR PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase;
KW Methionine biosynthesis; Multifunctional enzyme; NADP;
KW One-carbon metabolism; Oxidoreductase; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..282
FT /note="Bifunctional protein FolD"
FT /id="PRO_0000268304"
FT BINDING 164..166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576,
FT ECO:0000269|Ref.2"
FT BINDING 189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576,
FT ECO:0000269|Ref.2"
FT BINDING 230
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576,
FT ECO:0000269|Ref.2"
FT HELIX 6..26
FT /evidence="ECO:0007829|PDB:6DEB"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:6DEB"
FT HELIX 42..57
FT /evidence="ECO:0007829|PDB:6DEB"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:6DEB"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:6DEB"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:6DEB"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:6DEB"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6DEB"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:6DEB"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6DEB"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:6DEB"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:6DEB"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:6DEB"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:6DEB"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:6DEB"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:6DEB"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:6DEB"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:6DEB"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:6DEB"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:6DEB"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:6DEB"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:6DEB"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:6DEB"
FT HELIX 261..279
FT /evidence="ECO:0007829|PDB:6DEB"
SQ SEQUENCE 282 AA; 30349 MW; A692A4469F5B9AEB CRC64;
MTLLDGKALS AKIKEELKEK NQFLKSKGIE SCLAVILVGD NPASQTYVKS KAKACEECGI
KSLVYHLNEN ITQNELLALI NTLNHDDSVH GILVQLPLPD HICKDLILES IISSKDVDGF
HPINVGYLNL GLESGFLPCT PLGVMKLLKA YEIDLEGKDA VIIGASNIVG RPMATMLLNA
GATVSVCHIK TKDLSLYTRQ ADLIIVAAGC VNLLRSDMVK EGVIVVDVGI NRLESGKIVG
DVDFEEVSKK SSYITPVPGG VGPMTIAMLL ENTVKSAKNR LN
