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Protein

Dihydrofolate reductase FolM

Gene

folM

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the reduction of dihydrofolate to tetrahydrofolate.By similarity

Catalytic activityi

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

Sites

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

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: UniProtKB-EC

GO - Biological processi

  1. one-carbon metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase FolM (EC:1.5.1.3)
Short name:
DHFR
Gene namesi
Name:folM
Ordered Locus Names:SF1627, S1759
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000002673 Componenti: Chromosome UP000001006 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 240240Dihydrofolate reductase FolMPRO_0000339401Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi198214.SF1627.

Structurei

3D structure databases

ProteinModelPortaliQ83RC9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1028.
KOiK13938.
OMAiAVIHNAS.
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.

Q83RC9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKTQPLPIL ITGGGRRIGL ALAWHFINQK QPVIVSYRTH YPAIDGLINA
60 70 80 90 100
GAQCIQADFS TNDGVMAFAD EVLKTTHGLR AILHNASAWI AEKPGAPLAD
110 120 130 140 150
VLACMMQIHV NTPYLLNHAL ERLLRGHGHA ASDIIHFTDY VVERGSDKHV
160 170 180 190 200
AYAASKAALD NMTRSFARKL APEVKVNSIA PSLILFNEHD DAEYRQQALN
210 220 230 240
KSLMKTAPGE KEVIDLVDYL LTSCFVTGRS FPLDGGRHLR
Length:240
Mass (Da):26,330
Last modified:May 31, 2003 - v1
Checksum:i1A227307B826086A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN43210.1.
AE014073 Genomic DNA. Translation: AAP17098.1.
RefSeqiNP_707503.1. NC_004337.2.
NP_837291.1. NC_004741.1.
WP_000520806.1. NZ_JMRK01000045.1.

Genome annotation databases

EnsemblBacteriaiAAN43210; AAN43210; SF1627.
AAP17098; AAP17098; S1759.
GeneIDi1024813.
1078448.
KEGGisfl:SF1627.
sfx:S1759.
PATRICi18704899. VBIShiFle31049_1948.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN43210.1.
AE014073 Genomic DNA. Translation: AAP17098.1.
RefSeqiNP_707503.1. NC_004337.2.
NP_837291.1. NC_004741.1.
WP_000520806.1. NZ_JMRK01000045.1.

3D structure databases

ProteinModelPortaliQ83RC9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF1627.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN43210; AAN43210; SF1627.
AAP17098; AAP17098; S1759.
GeneIDi1024813.
1078448.
KEGGisfl:SF1627.
sfx:S1759.
PATRICi18704899. VBIShiFle31049_1948.

Phylogenomic databases

eggNOGiCOG1028.
KOiK13938.
OMAiAVIHNAS.
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]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiFOLM_SHIFL
AccessioniPrimary (citable) accession number: Q83RC9
Secondary accession number(s): Q7C1H7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 9, 2008
Last sequence update: May 31, 2003
Last modified: January 6, 2015
This is version 79 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.