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Protein

1-deoxy-D-xylulose 5-phosphate reductoisomerase

Gene

dxr

Organism
Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).UniRule annotation

Catalytic activityi

2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH.UniRule annotation

Cofactori

a divalent metal cationUniRule annotation

Pathwayi: isopentenyl diphosphate biosynthesis via DXP pathway

This protein is involved in step 1 of the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr)
  2. 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD)
  3. 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE)
  4. 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF)
  5. 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG)
  6. no protein annotated in this organism
This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via DXP pathway, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate, the pathway isopentenyl diphosphate biosynthesis via DXP pathway and in Isoprenoid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei124 – 1241SubstrateUniRule annotation
Metal bindingi149 – 1491Divalent metal cationUniRule annotation
Metal bindingi151 – 1511Divalent metal cationUniRule annotation
Binding sitei151 – 1511SubstrateUniRule annotation
Binding sitei174 – 1741SubstrateUniRule annotation
Binding sitei197 – 1971SubstrateUniRule annotation
Metal bindingi219 – 2191Divalent metal cationUniRule annotation
Binding sitei219 – 2191SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 3730NADPUniRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Isoprene biosynthesis

Keywords - Ligandi

Metal-binding, NADP

Enzyme and pathway databases

BioCyciPGIN431947:GC9J-1185-MONOMER.
UniPathwayiUPA00056; UER00092.

Names & Taxonomyi

Protein namesi
Recommended name:
1-deoxy-D-xylulose 5-phosphate reductoisomeraseUniRule annotation (EC:1.1.1.267UniRule annotation)
Short name:
DXP reductoisomeraseUniRule annotation
Alternative name(s):
1-deoxyxylulose-5-phosphate reductoisomeraseUniRule annotation
2-C-methyl-D-erythritol 4-phosphate synthaseUniRule annotation
Gene namesi
Name:dxrUniRule annotation
Ordered Locus Names:PGN_1151
OrganismiPorphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Taxonomic identifieri431947 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas
Proteomesi
  • UP000008842 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3853851-deoxy-D-xylulose 5-phosphate reductoisomerasePRO_1000098508Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi431947.PGN_1151.

Structurei

3D structure databases

ProteinModelPortaliB2RJX5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DXR family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEA. Bacteria.
COG0743. LUCA.
HOGENOMiHOG000007221.
KOiK00099.
OMAiGFCPLSE.
OrthoDBiEOG6R2H04.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00183. DXP_reductoisom.
InterProiIPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
IPR026877. DXPR_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR30525. PTHR30525. 1 hit.
PfamiPF08436. DXP_redisom_C. 1 hit.
PF02670. DXP_reductoisom. 1 hit.
PF13288. DXPR_C. 1 hit.
[Graphical view]
PIRSFiPIRSF006205. Dxp_reductismrs. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF69055. SSF69055. 1 hit.
TIGRFAMsiTIGR00243. Dxr. 1 hit.

Sequencei

Sequence statusi: Complete.

B2RJX5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKNIAILGS TGSIGTQTLD IIHLNPDLFD VYLLTANNNV DLLIRQAREY
60 70 80 90 100
RPEIVVIAND QKYHLIQEAL ADLPIKVWCG AEAIADAVTA PDIDMVVTAM
110 120 130 140 150
VGYSGLLPTI KAIEARKMIA LANKETLVVA GELIMRLAQD NQVPILPVDS
160 170 180 190 200
EHSAIFQALL GERQRPEKIL LTASGGPFLH LTAEELQHAT REQALRHPNW
210 220 230 240 250
NMGAKVTIDS ASLMNKGFEM IEAKWLFEMQ PDEIEILVHP QSIIHSMVQF
260 270 280 290 300
RDGSVKAQLG IPDMRLPISY ALGITHRIPN DYPRVDFTAT PLTFERPDLE
310 320 330 340 350
RFPNLSYAFD AIRLGGNAPC ALNAANEIAV TAFLRDEISF TDMSRLLYEV
360 370 380
MEKHELFREV SLPTFIETDS NTRRVAESLL PKFRR
Length:385
Mass (Da):43,104
Last modified:July 1, 2008 - v1
Checksum:iB656A6080FB243E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009380 Genomic DNA. Translation: BAG33670.1.
RefSeqiWP_005874315.1. NC_010729.1.

Genome annotation databases

EnsemblBacteriaiBAG33670; BAG33670; PGN_1151.
GeneIDi2551565.
KEGGipgn:PGN_1151.
PATRICi22975266. VBIPorGin26334_1143.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009380 Genomic DNA. Translation: BAG33670.1.
RefSeqiWP_005874315.1. NC_010729.1.

3D structure databases

ProteinModelPortaliB2RJX5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi431947.PGN_1151.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAG33670; BAG33670; PGN_1151.
GeneIDi2551565.
KEGGipgn:PGN_1151.
PATRICi22975266. VBIPorGin26334_1143.

Phylogenomic databases

eggNOGiENOG4105CEA. Bacteria.
COG0743. LUCA.
HOGENOMiHOG000007221.
KOiK00099.
OMAiGFCPLSE.
OrthoDBiEOG6R2H04.

Enzyme and pathway databases

UniPathwayiUPA00056; UER00092.
BioCyciPGIN431947:GC9J-1185-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00183. DXP_reductoisom.
InterProiIPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
IPR026877. DXPR_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR30525. PTHR30525. 1 hit.
PfamiPF08436. DXP_redisom_C. 1 hit.
PF02670. DXP_reductoisom. 1 hit.
PF13288. DXPR_C. 1 hit.
[Graphical view]
PIRSFiPIRSF006205. Dxp_reductismrs. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF69055. SSF69055. 1 hit.
TIGRFAMsiTIGR00243. Dxr. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Determination of the genome sequence of Porphyromonas gingivalis strain ATCC 33277 and genomic comparison with strain W83 revealed extensive genome rearrangements in P. gingivalis."
    Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H., Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T., Nakayama K.
    DNA Res. 15:215-225(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561.

Entry informationi

Entry nameiDXR_PORG3
AccessioniPrimary (citable) accession number: B2RJX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: June 8, 2016
This is version 53 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.