Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111NADP; via amide nitrogen and carbonyl oxygenCombined sources
Binding sitei18 – 181NADP; via carbonyl oxygenCombined sources
Binding sitei22 – 221NADP; via carbonyl oxygenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 536NADPCombined sources
Nucleotide bindingi70 – 723NADPCombined sources
Nucleotide bindingi104 – 1074NADPCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationImported

Keywords - Biological processi

One-carbon metabolismUniRule annotation

Keywords - Ligandi

NADPUniRule 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

ChEMBLiCHEMBL5457.

Interactioni

Protein-protein interaction databases

STRINGi262316.MAP2868c.

Chemistry

BindingDBiO30463.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W3VX-ray1.89A1-167[»]
2W3WX-ray1.60A1-167[»]
ProteinModelPortaliO30463.
SMRiO30463. Positions 6-166.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO30463.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 166162DHFR (dihydrofolate reductase)InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108YYV. Bacteria.
COG0262. LUCA.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000194. DHFR. 1 hit.
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W3VX-ray1.89A1-167[»]
2W3WX-ray1.60A1-167[»]
ProteinModelPortaliO30463.
SMRiO30463. Positions 6-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262316.MAP2868c.

Chemistry

BindingDBiO30463.
ChEMBLiCHEMBL5457.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108YYV. Bacteria.
COG0262. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.
BRENDAi1.5.1.3. 3492.

Miscellaneous databases

EvolutionaryTraceiO30463.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000194. DHFR. 1 hit.
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification and cloning of the Mycobacterium avium folA gene, required for dihydrofolate reductase activity."
    Zywno-van Ginkel S., Dooley T.P., Suling W.J., Barrow W.W.
    FEMS Microbiol. Lett. 156:69-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Structural Basis for Selective Inhibition of Mycobacterium Avium Dihydrofolate Reductase by a Lipophilic Antifolate."
    Leung A.K.W., Ross L.J., Zywno-Van Ginkel S., Reynolds R.C., Seitz L.E., Pathak V., Barrow W.W., White E.L., Suling W.J., Piper J.R., Borhani D.W.
    Submitted (NOV-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 1-167 IN COMPLEX WITH NADP, X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-167 IN COMPLEX WITH NADP.

Entry informationi

Entry nameiO30463_MYCAV
AccessioniPrimary (citable) accession number: O30463
Entry historyi
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.