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UniProtKB/Swiss-Prot entry Q9JSQ9

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DYR_NEIMA
Primary accession number Q9JSQ9
Secondary accession number A1IU05
Integrated into Swiss-Prot on August 29, 2001
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 41)
Name and origin of the protein
Protein name Dihydrofolate reductase
Synonym EC 1.5.1.3
Gene name
Name: folA
OrderedLocusNames: NMA2179
From
Neisseria meningitidis serogroup A [TaxID: 65699] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; Neisseria.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Z2491 / Serogroup A / Serotype 4A;
DOI=10.1038/35006655; PubMed=10761919 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M., Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A., Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G., Barrell B.G.;
"Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491.";
Nature 404:502-506(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AL157959; CAM09274.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H81790; H81790.
3D structure databases
HSSP O33305; 1DF7. [HSSP ENTRY / PDB]
ModBase Q9JSQ9.
Enzyme and pathway databases
BioCyc NMEN122587:NMA2179-MON; -.
Ontologies
GO
GO:0004146; Molecular function: dihydrofolate reductase activity (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0006545; Biological process: glycine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0009165; Biological process: nucleotide biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006730; Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR012259; DHFR.
IPR001796; DHFR_reg.
Graphical view of domain structure.
PANTHER PTHR11549:SF1; DHFR; 1.
Pfam PF00186; DHFR_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00070; DHFR.
PROSITE PS00075; DHFR_1; 1.
PS51330; DHFR_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9JSQ9.
ProtoNet Q9JSQ9.
Genome annotation databases
GenomeReviews AL157959_GR; NMA2179.
KEGG nma:NMA2179; -.
Phylogenomic databases
HOGENOM Q9JSQ9; -.
Genome annotation databases
CMR Q9JSQ9; NMA2179.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NADP; One-carbon metabolism; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom To Length Description FTId
CHAIN   1   162  162     Dihydrofolate reductase. PRO_0000186402
DOMAIN   3   161  159     DHFR. 
Sequence information
Length: 162 AA [This is the length of the unprocessed precursor] Molecular weight: 17682 Da [This is the MW of the unprocessed precursor] CRC64: B5EAF03CEABB8F62 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLKITLIAAC AENLCIGAGN AMPWHIPEDF AFFKAYTLGK PVIMGRKTWE SLPVKPLPGR 

        70         80         90        100        110        120 
RNIVISRQAD YCAAGAETAA SLEAALALCA GAEEAVIMGG AQIYGQAMPL ATDLRITEVD 

       130        140        150        160 
LSVEGDAFFP AIDRTHWKEA ERTERRVSSK GTSYAFVHYL RY
Q9JSQ9 in FASTA format

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