FOLD_EXIS2
ID FOLD_EXIS2 Reviewed; 277 AA.
AC B1YLQ1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Bifunctional protein FolD {ECO:0000255|HAMAP-Rule:MF_01576};
DE Includes:
DE RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01576};
DE EC=1.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01576};
DE Includes:
DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01576};
DE EC=3.5.4.9 {ECO:0000255|HAMAP-Rule:MF_01576};
GN Name=folD {ECO:0000255|HAMAP-Rule:MF_01576}; OrderedLocusNames=Exig_0904;
OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS 255-15).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=262543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_01576}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-
CC 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:0000255|HAMAP-
CC Rule:MF_01576};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,10-methenyltetrahydrofolate + H2O = (6S)-10-
CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:57455; EC=3.5.4.9; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01576};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000255|HAMAP-Rule:MF_01576}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01576}.
CC -!- SIMILARITY: Belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000255|HAMAP-Rule:MF_01576}.
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DR EMBL; CP001022; ACB60384.1; -; Genomic_DNA.
DR AlphaFoldDB; B1YLQ1; -.
DR SMR; B1YLQ1; -.
DR STRING; 262543.Exig_0904; -.
DR EnsemblBacteria; ACB60384; ACB60384; Exig_0904.
DR KEGG; esi:Exig_0904; -.
DR eggNOG; COG0190; Bacteria.
DR HOGENOM; CLU_034045_2_1_9; -.
DR OMA; HIVGRPM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001681; 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 HAMAP; MF_01576; THF_DHG_CYH; 1.
DR InterPro; IPR046346; Aminiacid_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 Pfam; PF00763; THF_DHG_CYH; 1.
DR Pfam; PF02882; THF_DHG_CYH_C; 1.
DR PRINTS; PR00085; THFDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00766; THF_DHG_CYH_1; 1.
DR PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase;
KW Methionine biosynthesis; Multifunctional enzyme; NADP;
KW One-carbon metabolism; Oxidoreductase; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..277
FT /note="Bifunctional protein FolD"
FT /id="PRO_1000196780"
FT BINDING 164..166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT BINDING 189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT BINDING 230
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
SQ SEQUENCE 277 AA; 29936 MW; 448012B75854402D CRC64;
MAVVIDGKQV AQSYRLKLKE EVARLKEERI QPKLTVILIG EDPASQSYVR GKEKAAQEIG
MDSDLIRLPE ETKESELLHL IERLNADASV HGILVQLPLP KHIDESKVIF AIAPEKDVDG
FHPVSVGKMM IGEPTFLPCT PNGILHLVKE MNVPIAGRHV VVVGRSQIVG KPVGMLFLNE
SATVTYCHSK TADLGAMTRQ ADILIVAVGV PKLITADMVK PEAVVIDVGV NRVDGKLVGD
VEFEAVKEVA SMITPVPGGV GPMTITMLLH NTIEAAK
