MTHFS_RABIT
ID MTHFS_RABIT Reviewed; 201 AA.
AC P80405;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase;
DE EC=6.3.3.2;
DE AltName: Full=5,10-methenyl-tetrahydrofolate synthetase;
DE Short=MTHFS;
DE Short=Methenyl-THF synthetase;
GN Name=MTHFS;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE, ACETYLATION AT ALA-1, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND SUBSTRATE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=8034591; DOI=10.1016/s0021-9258(17)32326-8;
RA Maras B., Stover P., Valiante S., Barra D., Schirch V.;
RT "Primary structure and tetrahydropteroylglutamate binding site of rabbit
RT liver cytosolic 5,10-methenyltetrahydrofolate synthetase.";
RL J. Biol. Chem. 269:18429-18433(1994).
CC -!- FUNCTION: Contributes to tetrahydrofolate metabolism. Helps regulate
CC carbon flow through the folate-dependent one-carbon metabolic network
CC that supplies carbon for the biosynthesis of purines, thymidine and
CC amino acids. Catalyzes the irreversible conversion of 5-
CC formyltetrahydrofolate (5-CHO-H(4)PteGlu) to yield 5,10-
CC methenyltetrahydrofolate. It can also use 5-formyltetrahydropteroic
CC acid (5-CHO-H(4)Pte) and 5-formyltetrahydropteroylhistidine (5-CHO-
CC H(4)PteHis) as substrate. {ECO:0000269|PubMed:8034591}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 uM for 5-CHO-H(4)PteGlu(5) {ECO:0000269|PubMed:8034591};
CC KM=8 uM for 5-CHO-H(4)PteGlu {ECO:0000269|PubMed:8034591};
CC KM=11 uM for 5-CHO-H(4)PteHis {ECO:0000269|PubMed:8034591};
CC KM=21 uM for 5-CHO-H(4)Pte {ECO:0000269|PubMed:8034591};
CC Note=kcat is 2 sec(-1) for cyclo-ligase activity with 5-CHO-H(4)Pte.
CC kcat is 3 sec(-1) for cyclo-ligase activity with 5-CHO-H(4)PteHis.
CC kcat is 5 sec(-1) for cyclo-ligase activity with 5-CHO-H(4)PteGlu and
CC 5-CHO-H(4)PteGlu(5).;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8034591}.
CC -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC family. {ECO:0000305}.
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DR PIR; A53688; A53688.
DR AlphaFoldDB; P80405; -.
DR SMR; P80405; -.
DR STRING; 9986.ENSOCUP00000003720; -.
DR iPTMnet; P80405; -.
DR PRIDE; P80405; -.
DR eggNOG; KOG3093; Eukaryota.
DR InParanoid; P80405; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; ISS:UniProtKB.
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 Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Folate-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..201
FT /note="5-formyltetrahydrofolate cyclo-ligase"
FT /id="PRO_0000200277"
FT BINDING 10..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 145..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 148..152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:8034591"
SQ SEQUENCE 201 AA; 22733 MW; 6FD20B8D9C31EC46 CRC64;
AAAAAVSGAK RSLRAELKQR LRAISAEERL RCQRLLTQKV IAHRQYQKSQ RISIFLSMPD
EIETEEIIKD IFQQGKVCFI PRYRLQSNHM DMVKLASADE ISSLPKTSWN IHQPSESDTR
EEALATGGLD LIFMPGLGFD RNGNRLGRGR GYYDTYLQRC LQQQGAKPYT IALAFREQIC
PQVPVDDTDV SVDEVLYVDA A
