5FCL_ECOLI
ID 5FCL_ECOLI Reviewed; 182 AA.
AC P0AC28; P09160; Q2M9T0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase;
DE Short=5-FCL;
DE EC=6.3.3.2 {ECO:0000269|PubMed:20952389};
DE AltName: Full=5,10-methenyltetrahydrofolate synthetase;
DE Short=MTHFS;
GN Name=ygfA; OrderedLocusNames=b2912, JW2879;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2579060; DOI=10.1128/jb.161.3.1162-1170.1985;
RA Hsu L.M., Zagorski J., Wang Z., Fournier M.J.;
RT "Escherichia coli 6S RNA gene is part of a dual-function transcription
RT unit.";
RL J. Bacteriol. 161:1162-1170(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION.
RX PubMed=18519731; DOI=10.1128/aac.00144-08;
RA Hansen S., Lewis K., Vulic M.;
RT "Role of global regulators and nucleotide metabolism in antibiotic
RT tolerance in Escherichia coli.";
RL Antimicrob. Agents Chemother. 52:2718-2726(2008).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20952389; DOI=10.1074/jbc.m110.190504;
RA Jeanguenin L., Lara-Nunez A., Pribat A., Mageroy M.H., Gregory J.F. III,
RA Rice K.C., de Crecy-Lagard V., Hanson A.D.;
RT "Moonlighting glutamate formiminotransferases can functionally replace 5-
RT formyltetrahydrofolate cycloligase.";
RL J. Biol. Chem. 285:41557-41566(2010).
RN [6]
RP INDUCTION.
RX PubMed=21036909; DOI=10.1074/jbc.m110.150201;
RA Chae H., Han K., Kim K.S., Park H., Lee J., Lee Y.;
RT "Rho-dependent termination of ssrS (6S RNA) transcription in Escherichia
RT coli: implication for 3' processing of 6S RNA and expression of downstream
RT ygfA (putative 5-formyl-tetrahydrofolate cyclo-ligase).";
RL J. Biol. Chem. 286:114-122(2011).
CC -!- FUNCTION: Involved in the removal of 5-formyltetrahydrofolate. In
CC vitro, it is a potent inhibitor of various folate-dependent enzymes in
CC the C1 metabolism network and in vivo it might function as a folate
CC storage. 5-formyltetrahydrofolate is also used as an antifolate rescue
CC agent in cancer chemotherapy. Catalyzes the irreversible ATP-dependent
CC transformation of 5-formyltetrahydrofolate (5-CHO-THF) to form 5,10-
CC methenyltetrahydrofolate (5,10-CH=THF) (PubMed:20952389). The reverse
CC reaction is catalyzed by the serine hydroxymethyltransferase GlyA
CC (SHMT) (PubMed:20952389). {ECO:0000269|PubMed:18519731,
CC ECO:0000269|PubMed:20952389, ECO:0000303|PubMed:20952389}.
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:20952389};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10489;
CC Evidence={ECO:0000269|PubMed:20952389};
CC -!- INTERACTION:
CC P0AC28; P0A763: ndk; NbExp=5; IntAct=EBI-555094, EBI-370139;
CC -!- INDUCTION: During biofilm formation. {ECO:0000269|PubMed:21036909}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene does not cause a growth
CC defect in rich or minimal medium. However, when grown in minimal medium
CC with added glycine, the mutant accumulates 5-CHO-THF. If the only
CC nitrogen source in minimal medium is glycine, the mutant shows a severe
CC growth defect, likely due to inhibition of serine
CC hydroxymethyltransferase (SHMT) and the glycine cleavage system by the
CC accumulated 5-CHO-THF. This phenotype can be complemented by the
CC glutamate formiminotransferase (FT). {ECO:0000269|PubMed:20952389}.
CC -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC family. {ECO:0000305}.
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DR EMBL; M12965; AAA24651.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69079.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75949.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76976.1; -; Genomic_DNA.
DR PIR; A21894; QQEC2K.
DR RefSeq; NP_417387.3; NC_000913.3.
DR AlphaFoldDB; P0AC28; -.
DR SMR; P0AC28; -.
DR BioGRID; 4261171; 227.
DR DIP; DIP-48194N; -.
DR IntAct; P0AC28; 9.
DR STRING; 511145.b2912; -.
DR PaxDb; P0AC28; -.
DR PRIDE; P0AC28; -.
DR EnsemblBacteria; AAC75949; AAC75949; b2912.
DR EnsemblBacteria; BAE76976; BAE76976; BAE76976.
DR GeneID; 945167; -.
DR KEGG; ecj:JW2879; -.
DR KEGG; eco:b2912; -.
DR PATRIC; fig|511145.12.peg.3006; -.
DR EchoBASE; EB1147; -.
DR eggNOG; COG0212; Bacteria.
DR HOGENOM; CLU_066245_0_0_6; -.
DR InParanoid; P0AC28; -.
DR OMA; GIVFDFA; -.
DR PhylomeDB; P0AC28; -.
DR BioCyc; EcoCyc:EG11158-MON; -.
DR BioCyc; MetaCyc:EG11158-MON; -.
DR PRO; PR:P0AC28; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; IMP:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0022611; P:dormancy process; IMP:EcoCyc.
DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
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 ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..182
FT /note="5-formyltetrahydrofolate cyclo-ligase"
FT /id="PRO_0000200284"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 182 AA; 21105 MW; 389B13098552BF81 CRC64;
MIRQRRRALT PEQQQEMGQQ AATRMMTYPP VVMAHTVAVF LSFDGELDTQ PLIEQLWRAG
KRVYLPVLHP FSAGNLLFLN YHPQSELVMN RLKIHEPKLD VRDVLPLSRL DVLITPLVAF
DEYGQRLGMG GGFYDRTLQN WQHYKTQPVG YAHDCQLVEK LPVEEWDIPL PAVVTPSKVW
EW
