ID   5FCL_HAEIN              Reviewed;         187 AA.
AC   P44905;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 119.
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   OrderedLocusNames=HI_0858;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=10675023;
RX   DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA   Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA   Fountoulakis M.;
RT   "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL   Electrophoresis 21:411-429(2000).
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}.
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DR   EMBL; L42023; AAC22517.1; -; Genomic_DNA.
DR   PIR; D64160; D64160.
DR   RefSeq; NP_439018.1; NC_000907.1.
DR   RefSeq; WP_005693206.1; NC_000907.1.
DR   AlphaFoldDB; P44905; -.
DR   SMR; P44905; -.
DR   STRING; 71421.HI_0858; -.
DR   EnsemblBacteria; AAC22517; AAC22517; HI_0858.
DR   KEGG; hin:HI_0858; -.
DR   PATRIC; fig|71421.8.peg.899; -.
DR   eggNOG; COG0212; Bacteria.
DR   HOGENOM; CLU_066245_0_0_6; -.
DR   OMA; MPLVGFD; -.
DR   PhylomeDB; P44905; -.
DR   BioCyc; HINF71421:G1GJ1-899-MON; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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..187
FT                   /note="5-formyltetrahydrofolate cyclo-ligase"
FT                   /id="PRO_0000200286"
FT   BINDING         6..10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         139..146
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   187 AA;  21821 MW;  01164CB8302A8C8A CRC64;
     MNTQKRQQIR TEIRKIRANL TALQQHQAEQ SVTQHALNLI EQRQAKNIAL YFSFDGEIST
     KALIQSLWMQ NKNVYLPVLH PFTKHYLLFL RYLPDTPMKQ NQFGIWEPKL NVQNVLPLNE
     LDILFTPLVA FDKKGNRLGM GGGFYDRTLQ NWQNKSFIPV GLAYQCQQVE NLPTEHWDVP
     LFDILVG