(data stored in ACNUC7421 zone)

SWISSPROT: D4YYT3_SPHJU

ID   D4YYT3_SPHJU            Unreviewed;       297 AA.
AC   D4YYT3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   30-AUG-2017, entry version 50.
DE   RecName: Full=Bifunctional protein FolD {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};
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};
GN   Name=folD {ECO:0000256|HAMAP-Rule:MF_01576,
GN   ECO:0000313|EMBL:BAI95515.1};
GN   OrderedLocusNames=SJA_C1-06810 {ECO:0000313|EMBL:BAI95515.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95515.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95515.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: Catalyzes the oxidation of 5,10-
CC       methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and
CC       then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-
CC       formyltetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01576,
CC       ECO:0000256|SAAS:SAAS00730939}.
CC   -!- CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H(2)O = 10-
CC       formyltetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01576,
CC       ECO:0000256|SAAS:SAAS00020423}.
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NADP(+) =
CC       5,10-methenyltetrahydrofolate + NADPH. {ECO:0000256|HAMAP-
CC       Rule:MF_01576, ECO:0000256|SAAS:SAAS00730961}.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|HAMAP-Rule:MF_01576, ECO:0000256|SAAS:SAAS00730924}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01576,
CC       ECO:0000256|SAAS:SAAS00730963}.
CC   -!- SIMILARITY: Belongs to the tetrahydrofolate
CC       dehydrogenase/cyclohydrolase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01576, ECO:0000256|SAAS:SAAS00730920}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01576}.
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DR   EMBL; AP010803; BAI95515.1; -; Genomic_DNA.
DR   RefSeq; WP_013039205.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-06810; -.
DR   EnsemblBacteria; BAI95515; BAI95515; SJA_C1-06810.
DR   GeneID; 29272353; -.
DR   KEGG; sjp:SJA_C1-06810; -.
DR   eggNOG; ENOG4105CN0; Bacteria.
DR   eggNOG; COG0190; LUCA.
DR   HOGENOM; HOG000218242; -.
DR   KO; K01491; -.
DR   OMA; AGKLCGD; -.
DR   OrthoDB; POG091H0041; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-HAMAP.
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   HAMAP; MF_01576; THF_DHG_CYH; 1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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; PTHR10025; PTHR10025; 1.
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   PROSITE; PS00766; THF_DHG_CYH_1; 1.
DR   PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YYT3.
DR   SWISS-2DPAGE; D4YYT3.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576,
KW   ECO:0000256|SAAS:SAAS00730947};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576,
KW   ECO:0000256|SAAS:SAAS00730933};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01576,
KW   ECO:0000256|SAAS:SAAS00020439};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576,
KW   ECO:0000256|SAAS:SAAS00730931};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01576,
KW   ECO:0000256|SAAS:SAAS00020419};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01576, ECO:0000256|SAAS:SAAS00730866};
KW   One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_01576,
KW   ECO:0000256|SAAS:SAAS00020466};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01576,
KW   ECO:0000256|SAAS:SAAS00020431, ECO:0000313|EMBL:BAI95515.1};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576,
KW   ECO:0000256|SAAS:SAAS00730882};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   DOMAIN        6    122       THF_DHG_CYH. {ECO:0000259|Pfam:PF00763}.
FT   DOMAIN      125    287       THF_DHG_CYH_C. {ECO:0000259|Pfam:
FT                                PF02882}.
FT   NP_BIND     167    169       NADP. {ECO:0000256|HAMAP-Rule:MF_01576}.
FT   BINDING     192    192       NADP. {ECO:0000256|HAMAP-Rule:MF_01576}.
FT   BINDING     233    233       NADP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01576}.
SQ   SEQUENCE   297 AA;  30902 MW;  D8CDF3DE5AA07BD2 CRC64;
     MTIGKIIDGK AFAETLRGKV ADGVGAFIAK TGRKPGLAVV LVGEDPASSV YVRNKGKMTV
     AAGMESMEFK LPASIGEEEL LDLVEELNAD ERVDGILVQL PLPPHINEAS VIGTIDPAKD
     VDGFHVVNSG LLATGQEAMV PCTPLGCIML LKDELGDLSG LEAVVVGRSN IVGKPMSQLL
     LAENCTVTIA HSRTRDIASV VHRADIVVAA VGRAEMVKGE WIKPGATVID VGINRVTDTE
     DGKSRIVGDV ATAEALAHVR AITPVPGGVG PMTIAVLLRN TLVAAHARAG LPRPEGL
//

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