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Protein

1-deoxy-D-xylulose 5-phosphate reductoisomerase

Gene

dxr

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
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. 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH)
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)DescriptionActionsGraphical viewLength
Binding sitei122SubstrateUniRule annotation1
Metal bindingi147Divalent metal cationUniRule annotation1
Metal bindingi149Divalent metal cationUniRule annotation1
Binding sitei149SubstrateUniRule annotation1
Binding sitei173SubstrateUniRule annotation1
Binding sitei196SubstrateUniRule annotation1
Metal bindingi218Divalent metal cationUniRule annotation1
Binding sitei218SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi7 – 36NADPUniRule annotationAdd BLAST30

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

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:BH2421
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001258 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001636081 – 3821-deoxy-D-xylulose 5-phosphate reductoisomeraseAdd BLAST382

Interactioni

Protein-protein interaction databases

STRINGi272558.BH2421.

Structurei

3D structure databases

ProteinModelPortaliQ9KA69.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DXR family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEA. Bacteria.
COG0743. LUCA.
HOGENOMiHOG000007220.
KOiK00099.
OMAiWPDMKLP.
OrthoDBiPOG091H0052.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00183. DXP_reductoisom. 1 hit.
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.

Q9KA69-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGISVLGAT GSIGTQTLDV LANHRDKFRL VAMSVGKNLT LAEEQIHQFK
60 70 80 90 100
PPLVSVMTDE DRKTLASKVP EGTRVVCGEE GLIEVATAEK AEILVNAVIG
110 120 130 140 150
SVGLAPTLAA IEAKKTIALA NKETLVTAGH LVTEKAREHG VKLLPVDSEH
160 170 180 190 200
SAIFQALQGE RMDRLHRIII TASGGSFRDK SRDELNGVTV EDALKHPNWS
210 220 230 240 250
MGAKITIDSA TMMNKGLEVI EAHWLFNLPY EKIDVLLHKE SIIHSMVEFV
260 270 280 290 300
DRSVIAQLGT PDMRVPIQYA LSYPDRLEFH EGQQLNLWEV GKLHFAPLDM
310 320 330 340 350
ERFRCMAFAY ESGKQGGTMP TVLNAANEEA VELFLNNQLS FLGIEDVIEK
360 370 380
ALERHERIDS PSLADILHVD QETRAFVHSL IK
Length:382
Mass (Da):42,208
Last modified:February 21, 2001 - v2
Checksum:i65EEAC0B018757BB
GO

Sequence cautioni

The sequence BAB06140 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB06140.1. Different initiation.
PIRiE83952.
RefSeqiWP_010898574.1. NC_002570.2.

Genome annotation databases

EnsemblBacteriaiBAB06140; BAB06140; BAB06140.
KEGGibha:BH2421.
PATRICi18942030. VBIBacHal18977_2528.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB06140.1. Different initiation.
PIRiE83952.
RefSeqiWP_010898574.1. NC_002570.2.

3D structure databases

ProteinModelPortaliQ9KA69.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272558.BH2421.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB06140; BAB06140; BAB06140.
KEGGibha:BH2421.
PATRICi18942030. VBIBacHal18977_2528.

Phylogenomic databases

eggNOGiENOG4105CEA. Bacteria.
COG0743. LUCA.
HOGENOMiHOG000007220.
KOiK00099.
OMAiWPDMKLP.
OrthoDBiPOG091H0052.

Enzyme and pathway databases

UniPathwayiUPA00056; UER00092.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00183. DXP_reductoisom. 1 hit.
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...

Entry informationi

Entry nameiDXR_BACHD
AccessioniPrimary (citable) accession number: Q9KA69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: February 21, 2001
Last modified: November 2, 2016
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.