FOLD_THET8
ID FOLD_THET8 Reviewed; 282 AA.
AC Q5SJ94;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=TTHA1120;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_01576}.
CC -!- SIMILARITY: Belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000255|HAMAP-Rule:MF_01576}.
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DR EMBL; AP008226; BAD70943.1; -; Genomic_DNA.
DR RefSeq; WP_011228455.1; NC_006461.1.
DR RefSeq; YP_144386.1; NC_006461.1.
DR PDB; 6V6Y; X-ray; 2.15 A; A=1-277.
DR PDBsum; 6V6Y; -.
DR AlphaFoldDB; Q5SJ94; -.
DR SMR; Q5SJ94; -.
DR STRING; 300852.55772502; -.
DR EnsemblBacteria; BAD70943; BAD70943; BAD70943.
DR GeneID; 3169194; -.
DR KEGG; ttj:TTHA1120; -.
DR PATRIC; fig|300852.9.peg.1099; -.
DR eggNOG; COG0190; Bacteria.
DR HOGENOM; CLU_034045_2_1_0; -.
DR OMA; HIVGRPM; -.
DR PhylomeDB; Q5SJ94; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000532; 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; 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_0000268546"
FT BINDING 162..164
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT BINDING 187
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT BINDING 228
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT HELIX 8..24
FT /evidence="ECO:0007829|PDB:6V6Y"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:6V6Y"
FT HELIX 41..57
FT /evidence="ECO:0007829|PDB:6V6Y"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:6V6Y"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:6V6Y"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:6V6Y"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:6V6Y"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6V6Y"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:6V6Y"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:6V6Y"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:6V6Y"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:6V6Y"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:6V6Y"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:6V6Y"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:6V6Y"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:6V6Y"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6V6Y"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:6V6Y"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:6V6Y"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:6V6Y"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:6V6Y"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:6V6Y"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:6V6Y"
FT HELIX 257..276
FT /evidence="ECO:0007829|PDB:6V6Y"
SQ SEQUENCE 282 AA; 30608 MW; F1DB18E5DE7C5492 CRC64;
MAAQVLSGHE AAEAVYEEIR ARLRSLSFTP SLRVIRLGED PASVAYVRLK DKRARALGYR
SQVEVYPEDL PEEALLERIA ALNADEEVDG ILVQLPLPPH IRTQRVLEAI HPLKDVDGFH
PLNVGRLWSG GKGLFPCTPL GVVRLLKHYG VDLRGKEVVV VGRSNIVGKP LAGLLLREDA
TVTLAHSKTQ DLPEVTRRAQ VLVVAVGRPH LVRKEWVREG AIVVDVGVNR VEGRLLGDVH
PEVAEVAFAL TPVPGGVGPM TVAMLMGNTL EAALLRRHGA SG
