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5-formyltetrahydrofolate cyclo-ligase (EC 6.3.3.2) (5,10-methenyl-tetrahydrofolate synthetase) (MTHFS) (Methenyl-THF synthetase)

 MTHFS_MYCPN             Reviewed;         164 AA.
P75430;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-OCT-2017, entry version 100.
RecName: Full=5-formyltetrahydrofolate cyclo-ligase;
EC=6.3.3.2;
AltName: Full=5,10-methenyl-tetrahydrofolate synthetase;
Short=MTHFS;
Short=Methenyl-THF synthetase;
OrderedLocusNames=MPN_348; ORFNames=H91_orf164, MP488;
Mycoplasma pneumoniae (strain ATCC 29342 / M129).
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
NCBI_TaxID=272634;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29342 / M129;
PubMed=8948633; DOI=10.1093/nar/24.22.4420;
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C.,
Herrmann R.;
"Complete sequence analysis of the genome of the bacterium Mycoplasma
pneumoniae.";
Nucleic Acids Res. 24:4420-4449(1996).
[2]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT.
PubMed=15281135; DOI=10.1002/prot.20214;
Chen S., Shin D.-H., Pufan R., Kim R., Kim S.H.;
"Crystal structure of methenyltetrahydrofolate synthetase from
Mycoplasma pneumoniae (GI: 13508087) at 2.2 A resolution.";
Proteins 56:839-843(2004).
[3]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; ADP
AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, COFACTOR, AND SUBUNIT.
PubMed=16104022; DOI=10.1002/prot.20591;
Chen S., Yakunin A.F., Proudfoot M., Kim R., Kim S.H.;
"Structural and functional characterization of a 5,10-
methenyltetrahydrofolate synthetase from Mycoplasma pneumoniae (GI:
13508087).";
Proteins 61:433-443(2005).
-!- FUNCTION: Involved in folate metabolism. Catalyzes the
irreversible conversion of 5-formyltetrahydrofolate (5-FTHF) to
yield 5,10-methenyltetrahydrofolate.
{ECO:0000269|PubMed:16104022}.
-!- CATALYTIC ACTIVITY: ATP + 5-formyltetrahydrofolate = ADP +
phosphate + 5,10-methenyltetrahydrofolate.
{ECO:0000269|PubMed:16104022}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:16104022};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:16104022};
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:16104022};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:16104022};
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:16104022};
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:16104022};
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Evidence={ECO:0000269|PubMed:16104022};
Note=Magnesium. It can also use divalent cations such as
manganese, calcium, zinc, iron, cobalt and copper.
{ECO:0000269|PubMed:16104022};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=165 uM for 5-FTHF (at pH 6 and 37 degrees Celsius)
{ECO:0000269|PubMed:16104022};
KM=166 uM for ATP (at pH 6 and 37 degrees Celsius)
{ECO:0000269|PubMed:16104022};
Vmax=2.70 umol/min/mg enzyme toward 5-FTHF (at pH 6 and 37
degrees Celsius) {ECO:0000269|PubMed:16104022};
Vmax=2.84 umol/min/mg enzyme toward ATP (at pH 6 and 37 degrees
Celsius) {ECO:0000269|PubMed:16104022};
Note=Kcat is 0.94 sec(-1) for cyclo-ligase activity with 5-FTHF
(at pH 6 and 37 degrees Celsius). Kcat is 0.99 sec(-1) for
cyclo-ligase activity with ATP (at pH 6 and 37 degrees
Celsius).;
-!- SUBUNIT: Monomer or homodimer. {ECO:0000269|PubMed:15281135,
ECO:0000269|PubMed:16104022}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
family. {ECO:0000305}.
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EMBL; U00089; AAB96136.1; -; Genomic_DNA.
PIR; S73814; S73814.
RefSeq; NP_110036.1; NC_000912.1.
RefSeq; WP_010874704.1; NC_000912.1.
PDB; 1SBQ; X-ray; 2.20 A; A/B=1-164.
PDB; 1U3F; X-ray; 2.50 A; A/B=1-164.
PDB; 1U3G; X-ray; 2.50 A; A=1-164.
PDBsum; 1SBQ; -.
PDBsum; 1U3F; -.
PDBsum; 1U3G; -.
ProteinModelPortal; P75430; -.
SMR; P75430; -.
DrugBank; DB02800; 5-Hydroxymethylene-6-Hydrofolic Acid.
EnsemblBacteria; AAB96136; AAB96136; MPN_348.
GeneID; 876747; -.
KEGG; mpn:MPN348; -.
PATRIC; fig|272634.6.peg.375; -.
KO; K01934; -.
OMA; MQEANRI; -.
BRENDA; 6.3.3.2; 3534.
EvolutionaryTrace; P75430; -.
Proteomes; UP000000808; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
InterPro; IPR002698; FTHF_cligase.
PANTHER; PTHR23407:SF1; PTHR23407:SF1; 2.
Pfam; PF01812; 5-FTHF_cyc-lig; 1.
PIRSF; PIRSF006806; FTHF_cligase; 1.
TIGRFAMs; TIGR02727; MTHFS_bact; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasm; Ligase;
Magnesium; Metal-binding; Nucleotide-binding; Reference proteome.
CHAIN 1 164 5-formyltetrahydrofolate cyclo-ligase.
/FTId=PRO_0000200288.
NP_BIND 3 7 ATP.
NP_BIND 115 123 ATP. {ECO:0000305}.
METAL 124 124 Magnesium. {ECO:0000269|PubMed:16104022}.
METAL 154 154 Magnesium. {ECO:0000269|PubMed:16104022}.
BINDING 50 50 Substrate. {ECO:0000269|PubMed:16104022}.
BINDING 55 55 Substrate. {ECO:0000269|PubMed:16104022}.
BINDING 125 125 ATP.
BINDING 153 153 ATP.
HELIX 3 16 {ECO:0000244|PDB:1SBQ}.
HELIX 19 37 {ECO:0000244|PDB:1SBQ}.
STRAND 45 47 {ECO:0000244|PDB:1SBQ}.
HELIX 60 68 {ECO:0000244|PDB:1SBQ}.
STRAND 72 78 {ECO:0000244|PDB:1SBQ}.
STRAND 80 82 {ECO:0000244|PDB:1SBQ}.
STRAND 84 87 {ECO:0000244|PDB:1SBQ}.
HELIX 96 98 {ECO:0000244|PDB:1SBQ}.
STRAND 101 105 {ECO:0000244|PDB:1SBQ}.
STRAND 107 109 {ECO:0000244|PDB:1SBQ}.
STRAND 114 116 {ECO:0000244|PDB:1U3G}.
STRAND 118 120 {ECO:0000244|PDB:1U3F}.
HELIX 122 126 {ECO:0000244|PDB:1SBQ}.
HELIX 127 129 {ECO:0000244|PDB:1SBQ}.
STRAND 136 140 {ECO:0000244|PDB:1SBQ}.
HELIX 142 144 {ECO:0000244|PDB:1SBQ}.
STRAND 158 162 {ECO:0000244|PDB:1SBQ}.
SEQUENCE 164 AA; 19265 MW; D44365FDE62A9DDF CRC64;
MDKNALRKQI LQKRMALSTI EKSHLDQKIN QKLVAFLTPK PCIKTIALYE PIKNEVTFVD
FFFEFLKINQ IRAVYPKVIS DTEIIFIDQE TNTFEPNQID CFLIPLVGFN KDNYRLGFGK
GYYDRYLMQL TRQQPKIGIA YSFQKGDFLA DPWDVQLDLI INDE


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