ID   Q6DDQ6_XENLA            Unreviewed;       335 AA.
AC   Q6DDQ6;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=methenyltetrahydrofolate cyclohydrolase {ECO:0000256|ARBA:ARBA00012776};
DE            EC=3.5.4.9 {ECO:0000256|ARBA:ARBA00012776};
GN   Name=mthfd2l.S {ECO:0000313|RefSeq:XP_018109776.1,
GN   ECO:0000313|Xenbase:XB-GENE-6256673};
GN   Synonyms=mthfd2-prov {ECO:0000313|EMBL:AAH77480.1}, mthfd2l
GN   {ECO:0000313|Xenbase:XB-GENE-6256673};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH77480.1};
RN   [1] {ECO:0000313|EMBL:AAH77480.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen {ECO:0000313|EMBL:AAH77480.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|RefSeq:XP_018109776.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018109776.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018109776.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-
CC         formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455,
CC         ChEBI:CHEBI:195366; EC=3.5.4.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00036357};
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DR   EMBL; BC077480; AAH77480.1; -; mRNA.
DR   RefSeq; NP_001086806.1; NM_001093337.1.
DR   RefSeq; XP_018109776.1; XM_018254287.2.
DR   STRING; 8355.Q6DDQ6; -.
DR   PaxDb; 8355-Q6DDQ6; -.
DR   DNASU; 446641; -.
DR   GeneID; 446641; -.
DR   KEGG; xla:446641; -.
DR   AGR; Xenbase:XB-GENE-6256673; -.
DR   CTD; 446641; -.
DR   Xenbase; XB-GENE-6256673; mthfd2l.S.
DR   OMA; VCHILTK; -.
DR   OrthoDB; 5386942at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 446641; Expressed in blastula and 19 other cell types or tissues.
DR   GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_01576; THF_DHG_CYH; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000672; THF_DH/CycHdrlase.
DR   InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR   InterPro; IPR020867; THF_DH/CycHdrlase_CS.
DR   InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR   PANTHER; PTHR48099:SF15; BIFUNCTIONAL METHYLENETETRAHYDROFOLATE DEHYDROGENASE_CYCLOHYDROLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 1.
DR   Pfam; PF00763; THF_DHG_CYH; 1.
DR   Pfam; PF02882; THF_DHG_CYH_C; 1.
DR   PRINTS; PR00085; THFDHDRGNASE.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00766; THF_DHG_CYH_1; 1.
DR   PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE   2: Evidence at transcript level;
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT   DOMAIN          33..148
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          151..323
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
SQ   SEQUENCE   335 AA;  36241 MW;  AFD32EDBEA2C14A8 CRC64;
     MATITSLRSL CCAVRAQVRA IHCTPCRNEA VIISGRKLAR QIRQEARHEV EQWVAAGNKR
     PHLSVVLVGD NPASHSYVLN KTKAAADVGI SSETIIKPTS ITEEELLDLI NKLNNDDHVD
     GLLVQLPLPE HLDERAICNA VTPDKDVDGF HVVNVGKMCL DQYSMLPATP WGVWEIIKRT
     GIPTLGKNVV VAGRSKNVGM PIAMLLHTDG RHERPGGDAT VTISHRYTPK EQLKMHTKLA
     DIVVAAAGIP NLITADMIKE GAAVIDVGIN RVQDPVTGKP KLVGDVDFEG VRKKASYITP
     VPGGVGPMTV AMLMKNTIIA AKKMLKPTEL QALAM
//