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Database: UniProt
Entry: M0LZP8_HALMO
LinkDB: M0LZP8_HALMO
Original site: M0LZP8_HALMO 
ID   M0LZP8_HALMO            Unreviewed;       314 AA.
AC   M0LZP8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 60.
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   ORFNames=C448_15426 {ECO:0000313|EMBL:EMA38911.1};
OS   Halococcus morrhuae DSM 1307.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=931277 {ECO:0000313|EMBL:EMA38911.1, ECO:0000313|Proteomes:UP000011568};
RN   [1] {ECO:0000313|EMBL:EMA38911.1, ECO:0000313|Proteomes:UP000011568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1307 {ECO:0000313|EMBL:EMA38911.1,
RC   ECO:0000313|Proteomes:UP000011568};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMA38911.1}.
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DR   EMBL; AOMC01000166; EMA38911.1; -; Genomic_DNA.
DR   RefSeq; WP_004056071.1; NZ_AOMC01000166.1.
DR   AlphaFoldDB; M0LZP8; -.
DR   STRING; 931277.C448_15426; -.
DR   PATRIC; fig|931277.6.peg.3032; -.
DR   eggNOG; arCOG04538; Archaea.
DR   OrthoDB; 9455at2157; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000011568; Unassembled WGS sequence.
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|HAMAP-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}; Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011568}.
FT   DOMAIN          5..119
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          122..306
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
FT   REGION          238..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   314 AA;  33309 MW;  6A0C7DD53106AE23 CRC64;
     MTNVIDGNAV ADGIRADLED CVDTLDNAGV TPGLATVLVG DDPASETYVS MKQRDCEEVG
     MNGIHVELDG DAAPDELYDT IDDLNDDSSV HGYLVQDPVP DQIDYREVIR RIDPAKDVDG
     FHPENVGRLV AGDARFKPCT PHGVQKLLDA ADVDPEGKDV TIVGRSRIVG KPLANLLMQK
     TDGGNATVTV CHSRTQDLAE KTRRADIVVA AVGAPELVDG SMLSEGTTVI DVGVNRVDAD
     TDEQRSSSSQ NSSSSDDTEK GYELVGDVEF DSAKEKASAI TPVPGGVGPM TRAMLLYNTV
     KAASQQEDVD VSLP
//
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