NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29342 / M129;
DOI=10.1093/nar/24.22.4420; PubMed=8948633 [NCBI, ExPASy, EBI, Israel, Japan]
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
"Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae.";
Nucleic Acids Res. 24:4420-4449(1996).

Comments

CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH.
PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1 .
MISCELLANEOUS: The reaction catalyzed by this enzyme represents an essential step for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
SIMILARITY: Belongs to the dihydrofolate reductase family.
SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) domain.

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

U00089; AAB96163.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S73841; S73841.

RefSeq

NP_110009.1; -.

3D structure databases

ModBase

P78028.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-579; -.
MPNE272634:MPN321-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

P78028.

Genome annotation databases

GeneID

876943; -.

GenomeReviews

U00089_GR; MPN_321.

KEGG

mpn:MPN321; -.

Phylogenomic databases

HOGENOM

P78028; -.

Genome annotation databases

CMR

P78028; MPN_321.

Other

ProtoNet

P78028.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; NADP; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 160`	`160`	`Dihydrofolate reductase.`	`PRO_0000186396`
`DOMAIN`	`1 160`	`160`	`DHFR.`

Sequence information

Length: 160 AA [This is the length of the unprocessed precursor]

Molecular weight: 18511 Da [This is the MW of the unprocessed precursor]

CRC64: 87C323433A3FABA4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVKAIWAMDQ NGLIGNGNSL PWRIKAELQH FRQTTLHQDV LMGSATYLSL PPVFSERNVY 

        70         80         90        100        110        120 
ILTRNLNFNP PDKGCLTKVI HEYENFIQPY LHHPDKHLYI CGGAQVYEQL IPRCDALIVS 

       130        140        150        160 
TIFGKYTGDK YLKVDFSPFE LTKEISFAEF KVAYYHKIAR

P78028 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools