(data stored in ACNUC7421 zone)

SWISSPROT: C6B1H7_RHILS

ID   C6B1H7_RHILS            Unreviewed;       299 AA.
AC   C6B1H7;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   30-AUG-2017, entry version 65.
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   OrderedLocusNames=Rleg_0385 {ECO:0000313|EMBL:ACS54696.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54696.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54696.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54696.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(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; CP001622; ACS54696.1; -; Genomic_DNA.
DR   RefSeq; WP_012756088.1; NC_012850.1.
DR   ProteinModelPortal; C6B1H7; -.
DR   EnsemblBacteria; ACS54696; ACS54696; Rleg_0385.
DR   KEGG; rlg:Rleg_0385; -.
DR   HOGENOM; HOG000218242; -.
DR   KO; K01491; -.
DR   OMA; TRINAGR; -.
DR   OrthoDB; POG091H0041; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002256; Chromosome.
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; PS00767; THF_DHG_CYH_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B1H7.
DR   SWISS-2DPAGE; C6B1H7.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576,
KW   ECO:0000256|SAAS:SAAS00730947};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
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, ECO:0000313|EMBL:ACS54696.1};
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};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576,
KW   ECO:0000256|SAAS:SAAS00730882}.
FT   DOMAIN        4    120       THF_DHG_CYH. {ECO:0000259|Pfam:PF00763}.
FT   DOMAIN      125    290       THF_DHG_CYH_C. {ECO:0000259|Pfam:
FT                                PF02882}.
FT   NP_BIND     168    170       NADP. {ECO:0000256|HAMAP-Rule:MF_01576}.
FT   BINDING     193    193       NADP. {ECO:0000256|HAMAP-Rule:MF_01576}.
FT   BINDING     234    234       NADP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01576}.
SQ   SEQUENCE   299 AA;  30788 MW;  307CF39A2E30A67C CRC64;
     MTTVIDGKNV AASVIQTVKS ATAALEKSSG VTTGLAVVIV GDDPASHAYV GSKGRMAKEC
     GFKSVQHTLP AETKQEDLAA LVASLNADPS IHGILVQLPL PKPLDSEAII QSILPEKDVD
     GLSVVNAGKL ATGDLKTGLV SCTPAGAMVF VRRTHGEDLS GLNAVVIGRS NLFGKPMAQL
     LLNANATVTI AHSRTKNLAE VCRNADILVA AVGRPEMVRA DWVKPGATVI DVGINRVAAP
     ERGEGKTRLV GDVAFEEVSA VASTITPVPG GVGPMTIAML MANTVIAAHR TAGQTPPQF
//

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