(data stored in ACNUC7421 zone)

SWISSPROT: C3MGJ1_SINFN

ID   C3MGJ1_SINFN            Unreviewed;       299 AA.
AC   C3MGJ1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   30-AUG-2017, entry version 63.
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=folD2 {ECO:0000313|EMBL:ACP24106.1};
GN   Synonyms=folD {ECO:0000256|HAMAP-Rule:MF_01576};
GN   OrderedLocusNames=NGR_c03080 {ECO:0000313|EMBL:ACP24106.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24106.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24106.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP24106.1; -; Genomic_DNA.
DR   RefSeq; WP_012706891.1; NC_012587.1.
DR   RefSeq; YP_002824859.1; NC_012587.1.
DR   STRING; 394.NGR_c03080; -.
DR   EnsemblBacteria; ACP24106; ACP24106; NGR_c03080.
DR   GeneID; 7790886; -.
DR   KEGG; rhi:NGR_c03080; -.
DR   PATRIC; fig|394.7.peg.3111; -.
DR   eggNOG; ENOG4105CN0; Bacteria.
DR   eggNOG; COG0190; LUCA.
DR   HOGENOM; HOG000218242; -.
DR   KO; K01491; -.
DR   OMA; TRINAGR; -.
DR   OrthoDB; POG091H0041; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001054; 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; C3MGJ1.
DR   SWISS-2DPAGE; C3MGJ1.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576,
KW   ECO:0000256|SAAS:SAAS00730947};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
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:ACP24106.1};
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, ECO:0000313|EMBL:ACP24106.1};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576,
KW   ECO:0000256|SAAS:SAAS00730882};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN        4    120       THF_DHG_CYH. {ECO:0000259|Pfam:PF00763}.
FT   DOMAIN      123    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;  30857 MW;  0F4289FB61AD92C6 CRC64;
     MTTVIDGKAV AASVIETVKS ATQTLETETG VRAGLAVVIV GDDPASHAYV SAKSRMAKEC
     GFLSVQHTLP GETSQEELAA LVAELNADPS IHGILVQLPL PKHLQSEPII QSILPEKDVD
     GLHVVNAGKV ATGDLDGGLV SCTPAGAMVF VRRTHGGDLS GLNAVVIGRS NLFGKPMSAL
     LLAANATVTT AHSRTKDLAA VCRNADILVA AVGRPEMVKA DWVKPGALVI DVGINRVAAP
     ERGEGRTKLV GDVAFEECAK VASVITPVPG GVGPMTIAML MANTIIAAYR KAGQNPPKF
//

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