ID   5FCL_ECO57              Reviewed;         182 AA.
AC   P0AC29; P09160;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase;
DE            Short=5-FCL;
DE            EC=6.3.3.2;
DE   AltName: Full=5,10-methenyltetrahydrofolate synthetase;
DE            Short=MTHFS;
GN   Name=ygfA; OrderedLocusNames=Z4249, ECs3782;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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). The reverse reaction is
CC       catalyzed by the serine hydroxymethyltransferase GlyA (SHMT) (By
CC       similarity). {ECO:0000250}.
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   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC   -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC       family. {ECO:0000305}.
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; AE005174; AAG58038.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37205.1; -; Genomic_DNA.
DR   PIR; F91101; F91101.
DR   RefSeq; NP_311809.3; NC_002695.1.
DR   AlphaFoldDB; P0AC29; -.
DR   SMR; P0AC29; -.
DR   STRING; 155864.EDL933_4114; -.
DR   EnsemblBacteria; AAG58038; AAG58038; Z4249.
DR   EnsemblBacteria; BAB37205; BAB37205; ECs_3782.
DR   GeneID; 916397; -.
DR   KEGG; ece:Z4249; -.
DR   KEGG; ecs:ECs_3782; -.
DR   PATRIC; fig|386585.9.peg.3947; -.
DR   eggNOG; COG0212; Bacteria.
DR   HOGENOM; CLU_066245_0_0_6; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..182
FT                   /note="5-formyltetrahydrofolate cyclo-ligase"
FT                   /id="PRO_0000200285"
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