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Q60034

- DYR_THEMA

UniProt

Q60034 - DYR_THEMA

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Protein
Dihydrofolate reductase
Gene
folA, dyrA, TM_1641
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 4 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 By similarity.

Catalytic activityi

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

Temperature dependencei

Highly thermostable.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei7 – 71Substrate; via carbonyl oxygen
Binding sitei9 – 91NADP; via amide nitrogen and carbonyl oxygen
Binding sitei16 – 161NADP; via carbonyl oxygen
Binding sitei28 – 281Substrate
Binding sitei59 – 591Substrate By similarity
Binding sitei81 – 811NADP; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi46 – 516NADP
Nucleotide bindingi65 – 673NADP
Nucleotide bindingi103 – 1053NADP

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. dihydrofolate reductase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. glycine biosynthetic process Source: InterPro
  2. nucleotide biosynthetic process Source: InterPro
  3. one-carbon metabolic process Source: UniProtKB-KW
  4. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-461.
TMAR243274:GC6P-1687-MONOMER.
UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Short name:
DHFR
Gene namesi
Name:folA
Synonyms:dyrA
Ordered Locus Names:TM_1641
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 169169Dihydrofolate reductase
PRO_0000186418Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi243274.TM1641.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108
Beta strandi15 – 173
Helixi26 – 3914
Beta strandi41 – 455
Helixi46 – 527
Beta strandi59 – 646
Beta strandi76 – 794
Helixi83 – 9210
Beta strandi96 – 1027
Helixi104 – 1129
Beta strandi117 – 1237
Beta strandi125 – 1306
Beta strandi132 – 1354
Beta strandi141 – 15111
Beta strandi153 – 1553
Beta strandi158 – 1647

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CZ3X-ray2.10A/B2-169[»]
1D1GX-ray2.10A/B2-169[»]
ProteinModelPortaliQ60034.
SMRiQ60034. Positions 2-169.

Miscellaneous databases

EvolutionaryTraceiQ60034.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 169167DHFR
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0262.
KOiK00287.
OMAiKGYERVA.
OrthoDBiEOG6KT2V2.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR001796. DHFR_dom.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS51330. DHFR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60034-1 [UniParc]FASTAAdd to Basket

« Hide

MAKVIFVLAM DVSGKIASSV ESWSSFEDRK NFRKITTEIG NVVMGRITFE    50
EIGRPLPERL NVVLTRRPKT SNNPSLVFFN GSPADVVKFL EGKGYERVAV 100
IGGKTVFTEF LREKLVDELF VTVEPYVFGK GIPFFDEFEG YFPLKLLEMR 150
RLNERGTLFL KYSVEKSHR 169
Length:169
Mass (Da):19,367
Last modified:November 1, 1997 - v1
Checksum:iF5DA22C978E2C39D
GO

Sequence cautioni

The sequence AAD36708.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 8114PKTSN…VFFNG → TQNFQQSFTRFFQR1 Publication
Add
BLAST
Sequence conflicti108 – 1081T → S1 Publication
Sequence conflicti138 – 1392FE → LQ1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X81845 Genomic DNA. Translation: CAA57437.1.
Y11021 Genomic DNA. Translation: CAA71903.1.
AE000512 Genomic DNA. Translation: AAD36708.1. Different initiation.
PIRiA72231.
RefSeqiNP_229441.1. NC_000853.1.
YP_007977999.1. NC_021214.1.

Genome annotation databases

EnsemblBacteriaiAAD36708; AAD36708; TM_1641.
GeneIDi896828.
KEGGitma:TM1641.
tmm:Tmari_1650.
PATRICi23938256. VBITheMar51294_1660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X81845 Genomic DNA. Translation: CAA57437.1 .
Y11021 Genomic DNA. Translation: CAA71903.1 .
AE000512 Genomic DNA. Translation: AAD36708.1 . Different initiation.
PIRi A72231.
RefSeqi NP_229441.1. NC_000853.1.
YP_007977999.1. NC_021214.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CZ3 X-ray 2.10 A/B 2-169 [» ]
1D1G X-ray 2.10 A/B 2-169 [» ]
ProteinModelPortali Q60034.
SMRi Q60034. Positions 2-169.
ModBasei Search...

Protein-protein interaction databases

STRINGi 243274.TM1641.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD36708 ; AAD36708 ; TM_1641 .
GeneIDi 896828.
KEGGi tma:TM1641.
tmm:Tmari_1650.
PATRICi 23938256. VBITheMar51294_1660.

Phylogenomic databases

eggNOGi COG0262.
KOi K00287.
OMAi KGYERVA.
OrthoDBi EOG6KT2V2.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .
BioCyci MetaCyc:MONOMER-461.
TMAR243274:GC6P-1687-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q60034.

Family and domain databases

Gene3Di 3.40.430.10. 1 hit.
InterProi IPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR001796. DHFR_dom.
[Graphical view ]
Pfami PF00186. DHFR_1. 1 hit.
[Graphical view ]
PRINTSi PR00070. DHFR.
SUPFAMi SSF53597. SSF53597. 1 hit.
PROSITEi PS51330. DHFR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The dihydrofolate reductase-encoding gene dyrA of the hyperthermophilic bacterium Thermotoga maritima."
    van de Casteele M., Legrain C., Wilquet V., Glansdorff N.
    Gene 158:101-105(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Homo-dimeric recombinant dihydrofolate reductase from Thermotoga maritima shows extreme intrinsic stability."
    Dams T., Schurig H., Jaenicke R.
    Biol. Chem. 379:367-371(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  4. "The crystal structure of dihydrofolate reductase from Thermotoga maritima: molecular features of thermostability."
    Dams T., Auerbach G., Bader G., Jacob U., Ploom T., Huber R., Jaenicke R.
    J. Mol. Biol. 297:659-672(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH METHOTREXATE AND NADPH.

Entry informationi

Entry nameiDYR_THEMA
AccessioniPrimary (citable) accession number: Q60034
Secondary accession number(s): P96109
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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