MTHFS_MYCPN
ID MTHFS_MYCPN Reviewed; 164 AA.
AC P75430;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase;
DE EC=6.3.3.2;
DE AltName: Full=5,10-methenyl-tetrahydrofolate synthetase;
DE Short=MTHFS;
DE Short=Methenyl-THF synthetase;
GN OrderedLocusNames=MPN_348; ORFNames=H91_orf164, MP488;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT.
RX PubMed=15281135; DOI=10.1002/prot.20214;
RA Chen S., Shin D.-H., Pufan R., Kim R., Kim S.H.;
RT "Crystal structure of methenyltetrahydrofolate synthetase from Mycoplasma
RT pneumoniae (GI: 13508087) at 2.2 A resolution.";
RL Proteins 56:839-843(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; ADP AND
RP MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, AND SUBUNIT.
RX PubMed=16104022; DOI=10.1002/prot.20591;
RA Chen S., Yakunin A.F., Proudfoot M., Kim R., Kim S.H.;
RT "Structural and functional characterization of a 5,10-
RT methenyltetrahydrofolate synthetase from Mycoplasma pneumoniae (GI:
RT 13508087).";
RL Proteins 61:433-443(2005).
CC -!- FUNCTION: Involved in folate metabolism. Catalyzes the irreversible
CC conversion of 5-formyltetrahydrofolate (5-FTHF) to yield 5,10-
CC methenyltetrahydrofolate. {ECO:0000269|PubMed:16104022}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5-formyl-5,6,7,8-tetrahydrofolate + ATP = 5,10-
CC methenyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:10488,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57455,
CC ChEBI:CHEBI:57457, ChEBI:CHEBI:456216; EC=6.3.3.2;
CC Evidence={ECO:0000269|PubMed:16104022};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16104022};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16104022};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:16104022};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16104022};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:16104022};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:16104022};
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:16104022};
CC Note=Magnesium. It can also use divalent cations such as manganese,
CC calcium, zinc, iron, cobalt and copper. {ECO:0000269|PubMed:16104022};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=165 uM for 5-FTHF (at pH 6 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:16104022};
CC KM=166 uM for ATP (at pH 6 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:16104022};
CC Vmax=2.70 umol/min/mg enzyme toward 5-FTHF (at pH 6 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:16104022};
CC Vmax=2.84 umol/min/mg enzyme toward ATP (at pH 6 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:16104022};
CC Note=kcat is 0.94 sec(-1) for cyclo-ligase activity with 5-FTHF (at
CC pH 6 and 37 degrees Celsius). kcat is 0.99 sec(-1) for cyclo-ligase
CC activity with ATP (at pH 6 and 37 degrees Celsius).;
CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000269|PubMed:15281135,
CC ECO:0000269|PubMed:16104022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC family. {ECO:0000305}.
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DR EMBL; U00089; AAB96136.1; -; Genomic_DNA.
DR PIR; S73814; S73814.
DR RefSeq; NP_110036.1; NC_000912.1.
DR RefSeq; WP_010874704.1; NC_000912.1.
DR PDB; 1SBQ; X-ray; 2.20 A; A/B=1-164.
DR PDB; 1U3F; X-ray; 2.50 A; A/B=1-164.
DR PDB; 1U3G; X-ray; 2.50 A; A=1-164.
DR PDBsum; 1SBQ; -.
DR PDBsum; 1U3F; -.
DR PDBsum; 1U3G; -.
DR AlphaFoldDB; P75430; -.
DR SMR; P75430; -.
DR STRING; 272634.MPN_348; -.
DR DrugBank; DB02800; 5-hydroxymethyl-5,6-dihydrofolic acid.
DR EnsemblBacteria; AAB96136; AAB96136; MPN_348.
DR GeneID; 66608995; -.
DR KEGG; mpn:MPN_348; -.
DR PATRIC; fig|272634.6.peg.375; -.
DR HOGENOM; CLU_066245_3_0_14; -.
DR OMA; ASDYWRE; -.
DR BioCyc; MPNE272634:G1GJ3-550-MON; -.
DR BRENDA; 6.3.3.2; 3534.
DR SABIO-RK; P75430; -.
DR EvolutionaryTrace; P75430; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10420; -; 1.
DR InterPro; IPR002698; FTHF_cligase.
DR InterPro; IPR024185; FTHF_cligase-like_sf.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR23407:SF1; PTHR23407:SF1; 1.
DR Pfam; PF01812; 5-FTHF_cyc-lig; 1.
DR PIRSF; PIRSF006806; FTHF_cligase; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR02727; MTHFS_bact; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..164
FT /note="5-formyltetrahydrofolate cyclo-ligase"
FT /id="PRO_0000200288"
FT BINDING 3..7
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16104022"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16104022"
FT BINDING 115..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16104022"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16104022"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:1SBQ"
FT HELIX 19..37
FT /evidence="ECO:0007829|PDB:1SBQ"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1SBQ"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:1SBQ"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:1SBQ"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1SBQ"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:1SBQ"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1SBQ"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1SBQ"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1SBQ"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1U3G"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1U3F"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:1SBQ"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1SBQ"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1SBQ"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1SBQ"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1SBQ"
SQ SEQUENCE 164 AA; 19265 MW; D44365FDE62A9DDF CRC64;
MDKNALRKQI LQKRMALSTI EKSHLDQKIN QKLVAFLTPK PCIKTIALYE PIKNEVTFVD
FFFEFLKINQ IRAVYPKVIS DTEIIFIDQE TNTFEPNQID CFLIPLVGFN KDNYRLGFGK
GYYDRYLMQL TRQQPKIGIA YSFQKGDFLA DPWDVQLDLI INDE
