FOLD_THEAC
ID FOLD_THEAC Reviewed; 276 AA.
AC Q05213;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 127.
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=Ta0898;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=8436115; DOI=10.1111/j.1432-1033.1993.tb17581.x;
RA Bright J.R., Byrom D., Danson M.J., Hough D.W., Towner P.;
RT "Cloning, sequencing and expression of the gene encoding glucose
RT dehydrogenase from the thermophilic archaeon Thermoplasma acidophilum.";
RL Eur. J. Biochem. 211:549-554(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT.
RX PubMed=21333632; DOI=10.1016/j.bbrc.2011.02.074;
RA Lee W.H., Sung M.W., Kim J.H., Kim Y.K., Han A., Hwang K.Y.;
RT "Crystal structure of bifunctional 5,10-methylenetetrahydrofolate
RT dehydrogenase/cyclohydrolase from Thermoplasma acidophilum.";
RL Biochem. Biophys. Res. Commun. 406:459-463(2011).
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 ECO:0000269|PubMed:21333632}.
CC -!- SIMILARITY: Belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000255|HAMAP-Rule:MF_01576}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA42451.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL445065; CAC12027.1; -; Genomic_DNA.
DR EMBL; X59788; CAA42451.1; ALT_FRAME; Genomic_DNA.
DR PIR; S29789; S29789.
DR RefSeq; WP_010901308.1; NC_002578.1.
DR PDB; 3NGL; X-ray; 2.40 A; A/C=1-276.
DR PDB; 3NGX; X-ray; 2.30 A; A/B=1-276.
DR PDBsum; 3NGL; -.
DR PDBsum; 3NGX; -.
DR AlphaFoldDB; Q05213; -.
DR SMR; Q05213; -.
DR STRING; 273075.Ta0898; -.
DR EnsemblBacteria; CAC12027; CAC12027; CAC12027.
DR GeneID; 1456434; -.
DR KEGG; tac:Ta0898; -.
DR eggNOG; arCOG04538; Archaea.
DR HOGENOM; CLU_034045_0_0_2; -.
DR OMA; HIVGRPM; -.
DR OrthoDB; 48572at2157; -.
DR BRENDA; 1.5.1.5; 6324.
DR BRENDA; 3.5.4.9; 6324.
DR UniPathway; UPA00193; -.
DR EvolutionaryTrace; Q05213; -.
DR Proteomes; UP000001024; 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..276
FT /note="Bifunctional protein FolD"
FT /id="PRO_0000199318"
FT BINDING 157..159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576,
FT ECO:0000269|PubMed:21333632"
FT BINDING 182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576,
FT ECO:0000269|PubMed:21333632"
FT BINDING 223
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576,
FT ECO:0000269|PubMed:21333632"
FT HELIX 7..23
FT /evidence="ECO:0007829|PDB:3NGX"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:3NGX"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:3NGX"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:3NGX"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:3NGX"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:3NGX"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:3NGX"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3NGX"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:3NGX"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:3NGX"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:3NGX"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:3NGX"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:3NGX"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3NGX"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:3NGX"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:3NGX"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:3NGX"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3NGX"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:3NGX"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3NGX"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:3NGX"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:3NGX"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:3NGX"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:3NGX"
FT HELIX 257..275
FT /evidence="ECO:0007829|PDB:3NGX"
SQ SEQUENCE 276 AA; 30622 MW; 55DFA04ADBCBF907 CRC64;
MKILRGEEIA EKKAENLHGI IERSGLEPSL KLIQIGDNEA ASIYARAKIR RGKKIGIAVD
LEKYDDISMK DLLKRIDDLA KDPQINGIMI ENPLPKGFDY YEIVRNIPYY KDVDALSPYN
QGLIALNREF LVPATPRAVI DIMDYYGYHE NTVTIVNRSP VVGRPLSMML LNRNYTVSVC
HSKTKDIGSM TRSSKIVVVA VGRPGFLNRE MVTPGSVVID VGINYVNDKV VGDANFEDLS
EYVEAITPVP GGVGPITATN ILENVVKAAE FQKNNL
