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Protein

Dihydromonapterin reductase

Gene

folM

Organism
Escherichia coli (strain UTI89 / UPEC)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the reduction of dihydromonapterin to tetrahydromonapterin. Also has lower activity with dihydrofolate.By similarity

Catalytic activityi

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.By similarity
5,6,7,8-tetrahydromonapterin + NADP+ = 7,8-dihydromonapterin + NADPH.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei152 – 1521Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciECOL364106:GHPQ-1780-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydromonapterin reductase (EC:1.5.1.-)
Short name:
H(2)-MPt reductase
Alternative name(s):
Dihydrofolate reductase (EC:1.5.1.3)
Short name:
DHFR
Gene namesi
Name:folM
Ordered Locus Names:UTI89_C1794
OrganismiEscherichia coli (strain UTI89 / UPEC)
Taxonomic identifieri364106 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001952 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 240240Dihydromonapterin reductasePRO_0000339392Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ1RBJ2.
SMRiQ1RBJ2. Positions 6-240.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1028.
KOiK13938.
OMAiPALLMFN.
OrthoDBiEOG6WDSG3.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1RBJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKTQSLPIL ITGGGRRIGL ALAWHFINQK QPVIVSYRTH YPAIDGLIKA
60 70 80 90 100
GAQCIQADFS TNDGVMAFAD EVLKSTHGLR AILHNASAWM AEKPGAPLTD
110 120 130 140 150
VLACMMQIHV NTPYLLNHAL ERLLRGHGHA ASDIIHFTDY VVERGSDKHI
160 170 180 190 200
AYAASKAALD NMTRSFARKL APEVKVNSIA PSLILFNEHD DAEYRQQALN
210 220 230 240
KSLMKTAPGE KEVIDLVDYL LTSCFVTGRS FPLDGGRHLR
Length:240
Mass (Da):26,382
Last modified:May 16, 2006 - v1
Checksum:i72A10AE1D7EB6C4C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000243 Genomic DNA. Translation: ABE07272.1.
RefSeqiWP_000520811.1. NC_007946.1.

Genome annotation databases

EnsemblBacteriaiABE07272; ABE07272; UTI89_C1794.
KEGGieci:UTI89_C1794.
PATRICi18453180. VBIEscCol42261_1839.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000243 Genomic DNA. Translation: ABE07272.1.
RefSeqiWP_000520811.1. NC_007946.1.

3D structure databases

ProteinModelPortaliQ1RBJ2.
SMRiQ1RBJ2. Positions 6-240.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE07272; ABE07272; UTI89_C1794.
KEGGieci:UTI89_C1794.
PATRICi18453180. VBIEscCol42261_1839.

Phylogenomic databases

eggNOGiCOG1028.
KOiK13938.
OMAiPALLMFN.
OrthoDBiEOG6WDSG3.

Enzyme and pathway databases

BioCyciECOL364106:GHPQ-1780-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
    Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
    Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UTI89 / UPEC.

Entry informationi

Entry nameiFOLM_ECOUT
AccessioniPrimary (citable) accession number: Q1RBJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: May 16, 2006
Last modified: July 22, 2015
This is version 58 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.