5FCL_MYCS2
ID 5FCL_MYCS2 Reviewed; 194 AA.
AC A0R3H2;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=MSMEG_5472, MSMEI_5322;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=16381882; DOI=10.1093/nar/gkj060;
RA Perrodou E., Deshayes C., Muller J., Schaeffer C., Van Dorsselaer A.,
RA Ripp R., Poch O., Reyrat J.M., Lecompte O.;
RT "ICDS database: interrupted CoDing sequences in prokaryotic genomes.";
RL Nucleic Acids Res. 34:D338-D343(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=21372133; DOI=10.1074/jbc.m111.231076;
RA Ogwang S., Nguyen H.T., Sherman M., Bajaksouzian S., Jacobs M.R.,
RA Boom W.H., Zhang G.F., Nguyen L.;
RT "Bacterial conversion of folinic acid is required for antifolate
RT resistance.";
RL J. Biol. Chem. 286:15377-15390(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). The reverse reaction is
CC catalyzed by the serine hydroxymethyltransferase GlyA (SHMT).
CC {ECO:0000269|PubMed:21372133}.
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:21372133};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene lead to an accumulation
CC of 5-CHO-THF. This mutant becomes more susceptible to antifolates that
CC inhibit folate biosynthesis (sulfonamides) or reduction (trimethoprim).
CC {ECO:0000269|PubMed:21372133}.
CC -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC family. {ECO:0000305}.
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DR EMBL; CP000480; ABK72547.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41763.1; -; Genomic_DNA.
DR RefSeq; WP_011730558.1; NZ_SIJM01000006.1.
DR RefSeq; YP_889710.1; NC_008596.1.
DR AlphaFoldDB; A0R3H2; -.
DR SMR; A0R3H2; -.
DR STRING; 246196.MSMEI_5322; -.
DR EnsemblBacteria; ABK72547; ABK72547; MSMEG_5472.
DR EnsemblBacteria; AFP41763; AFP41763; MSMEI_5322.
DR KEGG; msg:MSMEI_5322; -.
DR KEGG; msm:MSMEG_5472; -.
DR PATRIC; fig|246196.19.peg.5331; -.
DR eggNOG; COG0212; Bacteria.
DR OMA; GIVFDFA; -.
DR OrthoDB; 1816478at2; -.
DR BRENDA; 6.3.3.2; 3512.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..194
FT /note="5-formyltetrahydrofolate cyclo-ligase"
FT /id="PRO_0000430014"
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 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 194 AA; 20749 MW; D35EDED2EDD651A3 CRC64;
MSPRSKSQLR TALLQNRRSV PEAVREGEAE ALRGWLSGLK ISGRTVCAYV PVGSEPGSIA
LLDTLLELGA RVLLPVARND AAGIPLPLQW GKYRPGTLVA AEFGLREPPP PWLPAETIGE
ADVILVPALA VDRSGARLGR GAGFYDRTLH HAAATAQVIA VVRDDELLDE IPAEPHDVAM
THVLTPKRGI VALR
