FOLD_FRATN
ID FOLD_FRATN Reviewed; 282 AA.
AC A0Q505;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=FTN_0417;
OS Francisella tularensis subsp. novicida (strain U112).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=401614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U112;
RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT "Comparison of Francisella tularensis genomes reveals evolutionary events
RT associated with the emergence of human pathogenic strains.";
RL Genome Biol. 8:R102.1-R102.16(2007).
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; CP000439; ABK89320.1; -; Genomic_DNA.
DR RefSeq; WP_003038445.1; NZ_CP009633.1.
DR AlphaFoldDB; A0Q505; -.
DR SMR; A0Q505; -.
DR EnsemblBacteria; ABK89320; ABK89320; FTN_0417.
DR KEGG; ftn:FTN_0417; -.
DR OMA; HIVGRPM; -.
DR OrthoDB; 1449514at2; -.
DR BioCyc; FTUL401614:G1G75-436-MON; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000762; 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.
FT CHAIN 1..282
FT /note="Bifunctional protein FolD"
FT /id="PRO_0000305816"
FT BINDING 165..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT BINDING 231
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
SQ SEQUENCE 282 AA; 30431 MW; C6F0F5FCC61CEF08 CRC64;
MILIDGKSLS KDLKERLATQ VQEYKHNTAI TPKLVAIIVG NDPASKTYVA SKEKACAQVG
IDSQVITLPE HTTESELLEL IDQLNNDSSV HAILVQLPLP AHINKNNVIY SIKPEKDVDG
FHPTNVGRLQ LRDKKCLESC TPKGIMTMLR EYGIKTEGAY AVVVGASNVV GKPVSQLLLN
AKATVTTCHR FTTDLKSHTT KADILIVAVG KPNFITADMV KEGAVVIDVG INHVDGKIVG
DVDFAAVKDK VAAITPVPGG VGPMTITELL YNTFQCAQEL NR
