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THEMA:DYR

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Species (Taxon ID) Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099). (243274)
Gene Name(s) folA (synonyms: dyrA)
Protein Name(s) Dihydrofolate reductase

DHFR

External Links
UniProt Q60034
EMBL X81845
Y11021
AE000512
PIR A72231
RefSeq NP_229441.1
WP_004082129.1
WP_010865375.1
PDB 1CZ3
1D1G
PDBsum 1CZ3
1D1G
ProteinModelPortal Q60034
SMR Q60034
STRING 243274.TM1641
EnsemblBacteria AAD36708
GeneID 896828
KEGG tma:TM1641
tmi:THEMA_06040
tmw:THMA_1682
PATRIC 23938256
eggNOG ENOG41084X0
COG0262
InParanoid Q60034
KO K00287
OMA KGYERVA
OrthoDB EOG6KT2V2
BioCyc MetaCyc:MONOMER-461
TMAR243274:GC6P-1687-MONOMER
UniPathway UPA00077
EvolutionaryTrace Q60034
Proteomes UP000008183
GO GO:0004146
GO:0050661
GO:0006545
GO:0009165
GO:0006730
GO:0046654
Gene3D 3.40.430.10
InterPro IPR012259
IPR024072
IPR001796
Pfam PF00186
PRINTS PR00070
SUPFAM SSF53597
PROSITE PS51330

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004146

dihydrofolate reductase activity

PMID:10731419[1]

ECO:0000314

F

The enzyme does not show much structural changes when bound to its coenzyme NADPH and its inhibitor methotrexate. The enzyme also forms a homodimer, which contributes to its extreme stability.

complete
CACAO 11493

GO:0004146

dihydrofolate reductase activity

PMID:10413491[2]

ECO:0000314

F

The enzymes were not found to exist as monomers in equilibrium or while unfolding. This suggests that the protein is extremely stable throughout experimental temperatures from 5-70 degrees Celsius with a maximum stability at about 35 degrees C.

complete
CACAO 11495

enables

GO:0050661

NADP binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000167322
RGD:2500

F

Seeded From UniProt

complete

involved_in

GO:0046655

folic acid metabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000167322
RGD:2500
ZFIN:ZDB-GENE-010406-5

P

Seeded From UniProt

complete

involved_in

GO:0046654

tetrahydrofolate biosynthetic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000167322
RGD:2500
UniProtKB:P00374
UniProtKB:P9WNX1

P

Seeded From UniProt

complete

involved_in

GO:0046452

dihydrofolate metabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000167322
RGD:2500
UniProtKB:P00374

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10326
PANTHER:PTN000167378

C

Seeded From UniProt

complete

enables

GO:0004146

dihydrofolate reductase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10326
FB:FBgn0004087
MGI:MGI:94890
PANTHER:PTN000167322
PomBase:SPCC1223.08c
RGD:2500
UniProtKB:P00374
UniProtKB:P9WNX1
UniProtKB:Q86XF0
dictyBase:DDB_G0286755

F

Seeded From UniProt

complete

enables

GO:0004146

dihydrofolate reductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001796

F

Seeded From UniProt

complete

involved_in

GO:0046654

tetrahydrofolate biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001796

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001796

P

Seeded From UniProt

complete

enables

GO:0004146

dihydrofolate reductase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.5.1.3

F

Seeded From UniProt

complete

involved_in

GO:0006730

one-carbon metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0554

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

involved_in

GO:0046654

tetrahydrofolate biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00077

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Dams, T et al. (2000) The crystal structure of dihydrofolate reductase from Thermotoga maritima: molecular features of thermostability. J. Mol. Biol. 297 659-72 PubMed GONUTS page
  2. Dams, T & Jaenicke, R (1999) Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima. Biochemistry 38 9169-78 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 3.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page