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Protein

Dihydrofolate reductase

Gene

folA

Organism
Mycobacterium avium
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.UniRule annotation

Catalytic activityi

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.UniRule annotation

Pathwayi: tetrahydrofolate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Dihydrofolate reductase (folA)
This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei11NADP; via amide nitrogen and carbonyl oxygenCombined sources1
Binding sitei18NADP; via carbonyl oxygenCombined sources1
Binding sitei22NADP; via carbonyl oxygenCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi48 – 53NADPCombined sources6
Nucleotide bindingi70 – 72NADPCombined sources3
Nucleotide bindingi104 – 107NADPCombined sources4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductaseUniRule annotationImported
Biological processOne-carbon metabolismUniRule annotation
LigandNADPUniRule annotationCombined sources, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BRENDAi1.5.1.3. 3492.
UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductaseUniRule annotation (EC:1.5.1.3UniRule annotation)
Gene namesi
Name:folAImported
OrganismiMycobacterium aviumImported
Taxonomic identifieri1764 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5457.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2W3VX-ray1.89A1-167[»]
2W3WX-ray1.60A1-167[»]
ProteinModelPortaliO30463.
SMRiO30463.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO30463.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 166DHFRInterPro annotationAdd BLAST162

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108YYV. Bacteria.
COG0262. LUCA.

Family and domain databases

CDDicd00209. DHFR. 1 hit.
Gene3Di3.40.430.10. 2 hits.
InterProiView protein in InterPro
IPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
PfamiView protein in Pfam
PF00186. DHFR_1. 1 hit.
PIRSFiPIRSF000194. DHFR. 1 hit.
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiView protein in PROSITE
PS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.

Sequencei

Sequence statusi: Complete.

O30463-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRAEVGLVW AQSTSGVIGR GGDIPWSVPE DLTRFKEVTM GHTVIMGRRT
60 70 80 90 100
WESLPAKVRP LPGRRNVVVS RRPDFVAEGA RVAGSLEAAL AYAGSDPAPW
110 120 130 140 150
VIGGAQIYLL ALPHATRCEV TEIEIDLRRD DDDALAPALD DSWVGETGEW
160 170 180
LASRSGLRYR FHSYRRDPRS SVRGCSPSRP S
Length:181
Mass (Da):19,882
Last modified:January 1, 1998 - v1
Checksum:i753DFF3FE87E30B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006616 Genomic DNA. Translation: AAC45841.1.

Similar proteinsi

Entry informationi

Entry nameiO30463_MYCAV
AccessioniPrimary (citable) accession number: O30463
Entry historyiIntegrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: September 27, 2017
This is version 87 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources