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

dfrA

Organism
Bacillus anthracis
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 (dfrD), Dihydrofolate reductase (ABW01_29240), Dihydrofolate reductase (dfrA)
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 sitei8NADP; via amide nitrogen and carbonyl oxygenCombined sources1
Binding sitei15NADP; via carbonyl oxygenCombined sources1
Binding sitei79NADPCombined sources1
Metal bindingi108Calcium; via carbonyl oxygenCombined sources1
Metal bindingi110CalciumCombined sources1
Metal bindingi147CalciumCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 20NADPCombined sources2
Nucleotide bindingi45 – 47NADPCombined sources3
Nucleotide bindingi63 – 65NADPCombined sources3
Nucleotide bindingi98 – 101NADPCombined sources4

GO - Molecular functioni

  • dihydrofolate reductase activity Source: TIGR
  • metal ion binding Source: UniProtKB-KW
  • NADP binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationImported

Keywords - Biological processi

One-carbon metabolismUniRule annotation

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources, NADPUniRule annotationCombined sources, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciANTHRA:DFRA-MONOMER.
BRENDAi1.5.1.3. 634.
UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductaseUniRule annotation (EC:1.5.1.3UniRule annotation)
Gene namesi
Name:dfrAImported
Ordered Locus Names:GBAA_2237Imported
ORF Names:A8C77_11125Imported
OrganismiBacillus anthracisImported
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome
  • UP000077577 Componenti: Chromosome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5270.

Interactioni

Protein-protein interaction databases

STRINGi198094.BA_2237.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KGKNMR-A1-162[»]
2QK8X-ray2.40A1-162[»]
3DATX-ray2.30A1-162[»]
3E0BX-ray2.25A/B1-162[»]
3FL8X-ray2.29A/B/C/D/E/F/G/H1-162[»]
3FL9X-ray2.40A/B/C/D/E/F/G/H1-162[»]
3JVXX-ray2.25A/B1-162[»]
3JW3X-ray2.57A/B1-162[»]
3JW5X-ray2.89A/B1-162[»]
3JWCX-ray2.57A/B1-162[»]
3JWFX-ray2.57A/B1-162[»]
3JWKX-ray2.08A/B1-162[»]
3JWMX-ray2.57A/B1-162[»]
3S9UX-ray1.90A/B1-162[»]
3SA1X-ray2.50A/B1-162[»]
3SA2X-ray2.25A/B1-162[»]
3SAIX-ray2.25A/B1-162[»]
4ELBX-ray2.60A/B/C/D/E/F/G/H1-162[»]
4ELEX-ray2.35A/B/C/D/E/F/G/H1-162[»]
4ELFX-ray2.30A/B/C/D/E/F/G/H1-162[»]
4ELGX-ray2.10A/B/C/D/E/F/G/H1-162[»]
4ELHX-ray2.10A/B/C/D/E/F/G/H1-162[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 160DHFR (dihydrofolate reductase)InterPro annotationAdd BLAST159

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108YYV. Bacteria.
COG0262. LUCA.
KOiK00287.
OMAiKDNDLPW.

Family and domain databases

CDDicd00209. DHFR. 1 hit.
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.

Q81R22-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVSFMVAMD ENRVIGKDNN LPWRLPSELQ YVKKTTMGHP LIMGRKNYEA
60 70 80 90 100
IGRPLPGRRN IIVTRNEGYH VEGCEVAHSV EEVFELCKNE EEIFIFGGAQ
110 120 130 140 150
IYDLFLPYVD KLYITKIHHA FEGDTFFPEM DMTNWKEVFV EKGLTDEKNP
160
YTYYYHVYEK QQ
Length:162
Mass (Da):19,125
Last modified:June 1, 2003 - v1
Checksum:i4259925DD9A1365A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017334 Genomic DNA. Translation: AAT31357.1.
AY569129 Genomic DNA. Translation: AAT40581.1.
CP015779 Genomic DNA. Translation: ANH86423.1.
RefSeqiWP_000637198.1. NZ_LHUO01000023.1.

Genome annotation databases

EnsemblBacteriaiAAT31357; AAT31357; GBAA_2237.
AJH87338; AJH87338; BF27_5333.
KOM58895; KOM58895; AB168_28915.
KOM66226; KOM66226; AB166_16715.
KOM74197; KOM74197; AB165_04300.
KOM79752; KOM79752; AB167_04225.
KOM85569; KOM85569; AB164_02910.
KOM93257; KOM93257; AB169_10700.
KON02731; KON02731; AB170_26990.
KON19647; KON19647; AB171_05210.
KON23462; KON23462; AB163_12585.
KOR56368; KOR56368; ADT21_25245.
KOR64627; KOR64627; ADT20_24640.
KOS28334; KOS28334; ADK17_12095.
KOS28650; KOS28650; ADK18_10920.
KEGGibanh:HYU01_11160.
bar:GBAA_2237.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017334 Genomic DNA. Translation: AAT31357.1.
AY569129 Genomic DNA. Translation: AAT40581.1.
CP015779 Genomic DNA. Translation: ANH86423.1.
RefSeqiWP_000637198.1. NZ_LHUO01000023.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KGKNMR-A1-162[»]
2QK8X-ray2.40A1-162[»]
3DATX-ray2.30A1-162[»]
3E0BX-ray2.25A/B1-162[»]
3FL8X-ray2.29A/B/C/D/E/F/G/H1-162[»]
3FL9X-ray2.40A/B/C/D/E/F/G/H1-162[»]
3JVXX-ray2.25A/B1-162[»]
3JW3X-ray2.57A/B1-162[»]
3JW5X-ray2.89A/B1-162[»]
3JWCX-ray2.57A/B1-162[»]
3JWFX-ray2.57A/B1-162[»]
3JWKX-ray2.08A/B1-162[»]
3JWMX-ray2.57A/B1-162[»]
3S9UX-ray1.90A/B1-162[»]
3SA1X-ray2.50A/B1-162[»]
3SA2X-ray2.25A/B1-162[»]
3SAIX-ray2.25A/B1-162[»]
4ELBX-ray2.60A/B/C/D/E/F/G/H1-162[»]
4ELEX-ray2.35A/B/C/D/E/F/G/H1-162[»]
4ELFX-ray2.30A/B/C/D/E/F/G/H1-162[»]
4ELGX-ray2.10A/B/C/D/E/F/G/H1-162[»]
4ELHX-ray2.10A/B/C/D/E/F/G/H1-162[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198094.BA_2237.

Chemistry databases

ChEMBLiCHEMBL5270.

Protocols and materials databases

DNASUi1085515.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT31357; AAT31357; GBAA_2237.
AJH87338; AJH87338; BF27_5333.
KOM58895; KOM58895; AB168_28915.
KOM66226; KOM66226; AB166_16715.
KOM74197; KOM74197; AB165_04300.
KOM79752; KOM79752; AB167_04225.
KOM85569; KOM85569; AB164_02910.
KOM93257; KOM93257; AB169_10700.
KON02731; KON02731; AB170_26990.
KON19647; KON19647; AB171_05210.
KON23462; KON23462; AB163_12585.
KOR56368; KOR56368; ADT21_25245.
KOR64627; KOR64627; ADT20_24640.
KOS28334; KOS28334; ADK17_12095.
KOS28650; KOS28650; ADK18_10920.
KEGGibanh:HYU01_11160.
bar:GBAA_2237.

Phylogenomic databases

eggNOGiENOG4108YYV. Bacteria.
COG0262. LUCA.
KOiK00287.
OMAiKDNDLPW.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.
BioCyciANTHRA:DFRA-MONOMER.
BRENDAi1.5.1.3. 634.

Family and domain databases

CDDicd00209. DHFR. 1 hit.
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...

Entry informationi

Entry nameiQ81R22_BACAN
AccessioniPrimary (citable) accession number: Q81R22
Secondary accession number(s): E9R6R2
, E9R6R3, E9R6R4, Q68SA0, Q6HZ92, Q6KT86
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.