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A8A0E8 (FOLM_ECOHS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrofolate reductase FolM

Short name=DHFR
EC=1.5.1.3
Gene names
Name:folM
Ordered Locus Names:EcHS_A1681
OrganismEscherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]
Taxonomic identifier331112 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reduction of dihydrofolate to tetrahydrofolate By similarity.

Catalytic activity

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

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family. FolM subfamily.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processone-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiondihydrofolate reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 240240Dihydrofolate reductase FolM
PRO_0000339397

Sites

Active site1521Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
A8A0E8 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 73B942EE144E2CC3

FASTA24026,348
        10         20         30         40         50         60 
MGKTQPLPIL ITGGGRRIGL ALAWHFINQK QPVIVSYRTH YPAIDGLINA GAQCIQADFS 

        70         80         90        100        110        120 
TNDGVMAFAD EVLKSTHGLR AILHNASAWM AEKPGAPLAD VLACMMQIHV NTPYLLNHAL 

       130        140        150        160        170        180 
ERLLRGHGHA ASDIIHFTDY VVERGSDKHI AYAASKAALD NMTRSFARKL APEVKVNSIA 

       190        200        210        220        230        240 
PSLILFNEHD DAEYRQQALN KSLMKTAPGE KEVIDLVDYL LTSCFVTGRS FPLDGGRHLR 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000802 Genomic DNA. Translation: ABV06002.1.
RefSeqYP_001458385.1. NC_009800.1.

3D structure databases

ProteinModelPortalA8A0E8.
SMRA8A0E8. Positions 8-240.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING331112.EcHS_A1681.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV06002; ABV06002; EcHS_A1681.
GeneID5592664.
KEGGecx:EcHS_A1681.
PATRIC18313352. VBIEscCol77814_1649.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1028.
KOK13938.
OMAMKIAPGE.
OrthoDBEOG6WDSG3.

Enzyme and pathway databases

BioCycECOL331112:GHHI-1671-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFOLM_ECOHS
AccessionPrimary (citable) accession number: A8A0E8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families