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Database: UniProt
Entry: F0P279_WEEVC
LinkDB: F0P279_WEEVC
Original site: F0P279_WEEVC 
ID   F0P279_WEEVC            Unreviewed;       291 AA.
AC   F0P279;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=Bifunctional protein FolD {ECO:0000256|HAMAP-Rule:MF_01576};
DE   Includes:
DE     RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01576};
DE              EC=1.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01576};
DE   Includes:
DE     RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01576};
DE              EC=3.5.4.9 {ECO:0000256|HAMAP-Rule:MF_01576};
GN   Name=folD {ECO:0000256|HAMAP-Rule:MF_01576};
GN   OrderedLocusNames=Weevi_1060 {ECO:0000313|EMBL:ADX67769.1};
OS   Weeksella virosa (strain ATCC 43766 / DSM 16922 / JCM 21250 / CCUG 30538 /
OS   CDC 9751 / IAM 14551 / NBRC 16016 / NCTC 11634 / CL345/78).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Weeksella.
OX   NCBI_TaxID=865938 {ECO:0000313|EMBL:ADX67769.1, ECO:0000313|Proteomes:UP000008641};
RN   [1] {ECO:0000313|EMBL:ADX67769.1, ECO:0000313|Proteomes:UP000008641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 /
RC   CL345/78 {ECO:0000313|Proteomes:UP000008641};
RX   PubMed=21475590;
RA   Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA   Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA   Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brambilla E.M., Kopitz M., Rohde M., Goker M., Tindall B.J., Detter J.C.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Weeksella virosa type strain (9751).";
RL   Stand. Genomic Sci. 4:81-90(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43766 / DSM 16922 / JCM 21250 / NBRC 16016 / NCTC 11634 /
RC   CL345/78 {ECO:0000313|Proteomes:UP000008641};
RX   DOI=10.4056/sigs.1603927;
RA   Lang E., Teshima H., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA   Nolan M., Cheng J., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA   Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Brambilla E.,
RA   Kopitz M., Rohde M., Goker M., Tindall B., Detter J., Woyke T., Bristow J.,
RA   Eisen J., Markowitz V., Hugenholtz P., Klenk H., Kyrpides N.;
RT   "Complete genome sequence of Weeksella virosa type strain (9751T).";
RL   Stand. Genomic Sci. 4:81-90(2011).
CC   -!- FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to
CC       5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-
CC       methenyltetrahydrofolate to 10-formyltetrahydrofolate.
CC       {ECO:0000256|HAMAP-Rule:MF_01576}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01576};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-
CC         5,10-methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812,
CC         ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01576};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|HAMAP-Rule:MF_01576}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01576}.
CC   -!- SIMILARITY: Belongs to the tetrahydrofolate
CC       dehydrogenase/cyclohydrolase family. {ECO:0000256|HAMAP-Rule:MF_01576}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01576}.
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DR   EMBL; CP002455; ADX67769.1; -; Genomic_DNA.
DR   RefSeq; WP_013598159.1; NC_015144.1.
DR   AlphaFoldDB; F0P279; -.
DR   STRING; 865938.Weevi_1060; -.
DR   KEGG; wvi:Weevi_1060; -.
DR   eggNOG; COG0190; Bacteria.
DR   HOGENOM; CLU_034045_2_1_10; -.
DR   OMA; VCHILTK; -.
DR   OrthoDB; 9803580at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000008641; Chromosome.
DR   GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
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; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR   PANTHER; PTHR48099:SF5; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01576};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW   Rule:MF_01576};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01576};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01576};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_01576};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01576};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01576}; Reference proteome {ECO:0000313|Proteomes:UP000008641}.
FT   DOMAIN          4..119
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          122..290
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
FT   BINDING         164..166
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01576"
FT   BINDING         234
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01576"
SQ   SEQUENCE   291 AA;  31905 MW;  C7FBD3D9F4207525 CRC64;
     MQILDGLKLS KQIKQEIKES VDQLITAGKR VPHLAAVLVG ENGASQTYVN SKIKDCEQVG
     FRSSLLRLPE TTSQEELLAV IEKLNNQADL DGFIVQLPLP KHIDQEMIIN AIDPKKDVDG
     FHPENFGKMA LDMESFIPAT PFGIMKLLER NEIETKGKHA VIIGRSRIVG KPMSILLARK
     GNPGDCTVTL VHSSTINIEE FTKKADIVVT ALGVPHFLKG DMVKEGAVII DVGITRVEDT
     DSPKGYKIAG DVDFESVQEK ASWITPVPGG VGPMTRAMLL ENTLLAYQRN N
//
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