FOLD_FRATT
ID FOLD_FRATT Reviewed; 282 AA.
AC Q5NGF3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=FTT_0892;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH PHOSPHATE, AND
RP SUBUNIT.
RG Center for structural genomics of infectious diseases (CSGID);
RT "X-ray crystal structure of methylenetetrahydrofolate
RT dehydrogenase/methenyltetrahydrofolate cyclohydrolase, putative
RT bifunctional protein FolD from Francisella tularensis.";
RL Submitted (JUL-2011) 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; AJ749949; CAG45525.1; -; Genomic_DNA.
DR RefSeq; WP_003020886.1; NZ_CP010290.1.
DR RefSeq; YP_169889.1; NC_006570.2.
DR PDB; 3L07; X-ray; 1.88 A; A/B=1-282.
DR PDBsum; 3L07; -.
DR AlphaFoldDB; Q5NGF3; -.
DR SMR; Q5NGF3; -.
DR IntAct; Q5NGF3; 1.
DR STRING; 177416.FTT_0892; -.
DR DNASU; 3191934; -.
DR EnsemblBacteria; CAG45525; CAG45525; FTT_0892.
DR KEGG; ftu:FTT_0892; -.
DR eggNOG; COG0190; Bacteria.
DR OMA; HIVGRPM; -.
DR UniPathway; UPA00193; -.
DR EvolutionaryTrace; Q5NGF3; -.
DR Proteomes; UP000001174; 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_0000268352"
FT BINDING 165..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT BINDING 231
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT HELIX 6..28
FT /evidence="ECO:0007829|PDB:3L07"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:3L07"
FT HELIX 43..58
FT /evidence="ECO:0007829|PDB:3L07"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:3L07"
FT HELIX 74..85
FT /evidence="ECO:0007829|PDB:3L07"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:3L07"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:3L07"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3L07"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:3L07"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:3L07"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:3L07"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:3L07"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:3L07"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:3L07"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:3L07"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:3L07"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3L07"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:3L07"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:3L07"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:3L07"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:3L07"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3L07"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:3L07"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:3L07"
FT HELIX 264..279
FT /evidence="ECO:0007829|PDB:3L07"
SQ SEQUENCE 282 AA; 30454 MW; 0DD0F5FEF81CEF09 CRC64;
MILIDGKSLS KDLKERLATQ VQEYKHHTAI TPKLVAIIVG NDPASKTYVA SKEKACAQVG
IDSQVITLPE HTTESELLEL IDQLNNDSSV HAILVQLPLP AHINKNNVIY SIKPEKDVDG
FHPTNVGRLQ LRDKKCLESC TPKGIMTMLR EYGIKTEGAY AVVVGASNVV GKPVSQLLLN
AKATVTTCHR FTTDLKSHTT KADILIVAVG KPNFITADMV KEGAVVIDVG INHVDGKIVG
DVDFAAVKDK VAAITPVPGG VGPMTITELL YNTFQCAQEL NR
