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Q0C1B5 (Q0C1B5_HYPNA) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP-Rule MF_00183
Short name=DXP reductoisomerase HAMAP-Rule MF_00183
EC=1.1.1.267 HAMAP-Rule MF_00183
Alternative name(s):
1-deoxyxylulose-5-phosphate reductoisomerase HAMAP-Rule MF_00183
2-C-methyl-D-erythritol 4-phosphate synthase HAMAP-Rule MF_00183
Gene names
Name:dxr HAMAP-Rule MF_00183
Ordered Locus Names:HNE_1774
OrganismHyphomonas neptunium (strain ATCC 15444) [Complete proteome] [HAMAP] EMBL ABI77423.1
Taxonomic identifier228405 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Hyphomonadaceae › Hyphomonas ›

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP) By similarity. HAMAP-Rule MF_00183 SAAS SAAS026877

Catalytic activity

2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH. HAMAP-Rule MF_00183 SAAS SAAS026877

Cofactor

Divalent cation By similarity. HAMAP-Rule MF_00183 SAAS SAAS026877

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. HAMAP-Rule MF_00183 SAAS SAAS026877

Sequence similarities

Belongs to the DXR family. HAMAP-Rule MF_00183

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding8 – 4134NADP By similarity HAMAP-Rule MF_00183

Sites

Metal binding1521Divalent metal cation By similarity HAMAP-Rule MF_00183
Metal binding1541Divalent metal cation By similarity HAMAP-Rule MF_00183
Metal binding2211Divalent metal cation By similarity HAMAP-Rule MF_00183
Binding site1271Substrate By similarity HAMAP-Rule MF_00183
Binding site1541Substrate By similarity HAMAP-Rule MF_00183
Binding site1761Substrate By similarity HAMAP-Rule MF_00183
Binding site1991Substrate By similarity HAMAP-Rule MF_00183
Binding site2211Substrate By similarity HAMAP-Rule MF_00183

Sequences

Sequence LengthMass (Da)Tools
Q0C1B5 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: F6B2C52039B97DD0

FASTA39741,525
        10         20         30         40         50         60 
MVRKVSIFGS TGSIGRSAID VICNANETGA AEFSVEALAA GRDVEGLASQ ALKLKPKIAV 

        70         80         90        100        110        120 
IADESRKVEL AALLAGSGIE VAAGEGALNE AAARPCDRVL AAIVGAAGLG STLAAIKAGN 

       130        140        150        160        170        180 
DIAIANKESI VCGGQLMLGE ARQSGARIFP VDSEHSAIFQ CIGDGRSLEN LTITASGGPF 

       190        200        210        220        230        240 
RNWSLEQMAT ATPAQAAAHP VWSMGIKNSI DSASLMNKAL EFIEAAVLFD VAADHINVLV 

       250        260        270        280        290        300 
HPQSIIHGMA HFDDGSVIAQ LGCPDMRTPI SYALGWPDRI PTTVDRLNLA QISNLEFFEV 

       310        320        330        340        350        360 
DEERFASIRL AREAMGAGPA ARVVLNCANE AAVSAFIAGE CGFLDISRLV EAALERFSSG 

       370        380        390 
NFASSKCETL EEIAEISRYG RFLVSQWLNN APSRAGG

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References

[1]"Comparative genomic evidence for a close relationship between the dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter crescentus."
Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R., Brinkac L.M. expand/collapse author list , Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N., Ward N.L.
J. Bacteriol. 188:6841-6850(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15444.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000158 Genomic DNA. Translation: ABI77423.1.
RefSeqYP_760478.1. NC_008358.1.

3D structure databases

ProteinModelPortalQ0C1B5.
ModBaseSearch...

Protein-protein interaction databases

STRING228405.HNE_1774.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI77423; ABI77423; HNE_1774.
GeneID4289919.
KEGGhne:HNE_1774.
PATRIC32216375. VBIHypNep17450_1776.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0743.
HOGENOMHOG000007221.
KOK00099.
OMAFIDGSVM.
ProtClustDBPRK05447.

Enzyme and pathway databases

BioCycHNEP228405:GI69-1802-MONOMER.
UniPathwayUPA00056; UER00092.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00183. DXP_reductoisom.
InterProIPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
IPR026877. DXPR_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR30525. PTHR30525. 1 hit.
PfamPF08436. DXP_redisom_C. 1 hit.
PF02670. DXP_reductoisom. 1 hit.
PF13288. DXPR_C. 1 hit.
[Graphical view]
PIRSFPIRSF006205. Dxp_reductismrs. 1 hit.
SUPFAMSSF69055. SSF69055. 1 hit.
TIGRFAMsTIGR00243. Dxr. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ0C1B5_HYPNA
AccessionPrimary (citable) accession number: Q0C1B5
Entry history
Integrated into UniProtKB/TrEMBL: October 17, 2006
Last sequence update: October 17, 2006
Last modified: May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info