FOLD_MYCTU
ID FOLD_MYCTU Reviewed; 281 AA.
AC P9WG81; L0TDW6; O50385; Q7D5N0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
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=Rv3356c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RG Mycobacterium tuberculosis structural genomics consortium (TB);
RT "Three dimensional structure of bifunctional methylenetetrahydrofolate
RT dehydrogenase-cyclohydrolase from Mycobacterium tuberculosis.";
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.3}.
CC -!- SIMILARITY: Belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000255|HAMAP-Rule:MF_01576}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP46177.1; -; Genomic_DNA.
DR PIR; C70970; C70970.
DR RefSeq; NP_217873.1; NC_000962.3.
DR RefSeq; WP_003417751.1; NZ_NVQJ01000052.1.
DR PDB; 2C2X; X-ray; 2.00 A; A/B=2-281.
DR PDB; 2C2Y; X-ray; 2.30 A; A=2-281.
DR PDBsum; 2C2X; -.
DR PDBsum; 2C2Y; -.
DR AlphaFoldDB; P9WG81; -.
DR SMR; P9WG81; -.
DR STRING; 83332.Rv3356c; -.
DR PaxDb; P9WG81; -.
DR DNASU; 888145; -.
DR GeneID; 45427355; -.
DR GeneID; 888145; -.
DR KEGG; mtu:Rv3356c; -.
DR TubercuList; Rv3356c; -.
DR eggNOG; COG0190; Bacteria.
DR OMA; HIVGRPM; -.
DR PhylomeDB; P9WG81; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IBA:GO_Central.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IBA:GO_Central.
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; IBA:GO_Central.
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; 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.
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..281
FT /note="Bifunctional protein FolD"
FT /id="PRO_0000268404"
FT BINDING 165..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT BINDING 192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT BINDING 233
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT HELIX 8..28
FT /evidence="ECO:0007829|PDB:2C2X"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:2C2X"
FT HELIX 44..60
FT /evidence="ECO:0007829|PDB:2C2X"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:2C2X"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:2C2X"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2C2X"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:2C2X"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2C2X"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:2C2X"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:2C2X"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2C2X"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:2C2X"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:2C2X"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:2C2X"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:2C2X"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:2C2X"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:2C2X"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:2C2X"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:2C2X"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:2C2X"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:2C2X"
FT HELIX 246..250
FT /evidence="ECO:0007829|PDB:2C2X"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:2C2X"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:2C2X"
FT HELIX 263..280
FT /evidence="ECO:0007829|PDB:2C2X"
SQ SEQUENCE 281 AA; 29484 MW; E06A276B71CC9A1D CRC64;
MGAIMLDGKA TRDEIFGDLK QRVAALDAAG RTPGLGTILV GDDPGSQAYV RGKHADCAKV
GITSIRRDLP ADISTATLNE TIDELNANPD CTGYIVQLPL PKHLDENAAL ERVDPAKDAD
GLHPTNLGRL VLGTPAPLPC TPRGIVHLLR RYDISIAGAH VVVIGRGVTV GRPLGLLLTR
RSENATVTLC HTGTRDLPAL TRQADIVVAA VGVAHLLTAD MVRPGAAVID VGVSRTDDGL
VGDVHPDVWE LAGHVSPNPG GVGPLTRAFL LTNVVELAER R
