ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P43791


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DYR_HAEIN
Primary accession number P43791
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 58)
Name and origin of the protein
Protein name Dihydrofolate reductase
Synonym EC 1.5.1.3
Gene name
Name: folA
Synonyms: folH
OrderedLocusNames: HI0899
From
Haemophilus influenzae [TaxID: 727] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Haemophilus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
PubMed=7542800 [NCBI, ExPASy, EBI, Israel, Japan]
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd.";
Science 269:496-512(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Isolate R1042, Isolate R1047, and Isolate R906;
de Groot R.;
Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
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
L42023; AAC22559.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X84207; CAA58993.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X84205; CAA58991.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X84206; CAA58992.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C64101; C64101.
S52336; S52336.
S52337; S52337.
S52338; S52338.
RefSeq NP_439060.1; -.
3D structure databases
HSSP P00379; 1DHI. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase P43791.
Enzyme and pathway databases
BioCyc HINF71421:HI_0899-MON; -.
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 P43791.
Genome annotation databases
GeneID 949905; -.
GenomeReviews L42023_GR; HI0899.
KEGG hin:HI0899; -.
TIGR HI0899; -.
Phylogenomic databases
HOGENOM P43791; -.
Other
ProtoNet P43791.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antibiotic resistance; Complete proteome; NADP; One-carbon metabolism; Oxidoreductase; Trimethoprim resistance.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   160  160     Dihydrofolate reductase. PRO_0000186391
DOMAIN   2   159  158     DHFR. 
VARIANT   13    13  1     N -> S (in strain: Isolate R1042 and Isolate R1047). 
VARIANT   21    21  1     M -> I (in strain: Isolate R1047). 
VARIANT   54    54  1     P -> A (in strain: Isolate R1047). 
VARIANT   56    56  1     P -> A (in strain: Isolate R906). 
VARIANT   67    67  1     L -> P (in strain: Isolate R1042). 
VARIANT   69    69  1     E -> K (in strain: Isolate R1042). 
VARIANT   74    74  1     I -> V (in strain: Isolate R1042). 
VARIANT   77    77  1     D -> N (in strain: Isolate R1042). 
VARIANT   79    79  1     F -> L (in strain: Isolate R1042). 
VARIANT   95    95  1     I -> L (in strain: Isolate R1047). 
VARIANT   135   135  1     E -> K (in strain: Isolate R1042). 
VARIANT   142   142  1     R -> H (in strain: Isolate R1042). 
VARIANT   154   154  1     F -> S (in strain: Isolate R1042). 
Sequence information
Length: 160 AA [This is the length of the unprocessed precursor] Molecular weight: 18913 Da [This is the MW of the unprocessed precursor] CRC64: 384A1D64092B8C4F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTFSLIVATT LNNVIGKDNQ MPWHLPADLA WFRQNTTGKP VIMGRKTFES IGRPLPKRTN 

        70         80         90        100        110        120 
IVLSRQLFEH EGVIWKDSFE SAVNFVRDFD EIMLIGGGEL FKQYLPKADK LYLTQIQTEL 

       130        140        150        160 
DGDTFFPQLN WEEWEIEFDE YRKADEQNRY DCRFLILTRK 

P43791 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!