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Protein

Deoxyribose-phosphate aldolase

Gene

deoC

Organism
Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC SS700)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.UniRule annotation

Catalytic activityi

2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei153 – 1531Schiff-base intermediate with acetaldehydeUniRule annotation
Active sitei182 – 1821UniRule annotation

GO - Molecular functioni

  1. deoxyribose-phosphate aldolase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. carbohydrate catabolic process Source: UniProtKB-HAMAP
  2. deoxyribonucleotide catabolic process Source: InterPro
  3. deoxyribose phosphate catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciSAGA205921:GHD7-2010-MONOMER.
UniPathwayiUPA00002; UER00468.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxyribose-phosphate aldolaseUniRule annotation (EC:4.1.2.4UniRule annotation)
Short name:
DERAUniRule annotation
Alternative name(s):
2-deoxy-D-ribose 5-phosphate aldolaseUniRule annotation
PhosphodeoxyriboaldolaseUniRule annotation
Short name:
DeoxyriboaldolaseUniRule annotation
Gene namesi
Name:deoCUniRule annotation
Ordered Locus Names:SAK_2009
OrganismiStreptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC SS700)
Taxonomic identifieri205921 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000002701: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 223223Deoxyribose-phosphate aldolasePRO_0000231567Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi205921.SAK_2009.

Structurei

3D structure databases

ProteinModelPortaliQ3JYQ4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0274.
HOGENOMiHOG000241645.
KOiK01619.
OMAiKHVDHTL.
OrthoDBiEOG6QZMW5.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00114. DeoC_type1.
InterProiIPR013785. Aldolase_TIM.
IPR011343. DeoC.
IPR002915. DeoC/FbaB/lacD_aldolase.
IPR028581. DeoC_typeI.
[Graphical view]
PANTHERiPTHR10889. PTHR10889. 1 hit.
PfamiPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFiPIRSF001357. DeoC. 1 hit.
TIGRFAMsiTIGR00126. deoC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q3JYQ4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEVKDILKTV DHTLLATTAT WPEIQTILDD AMAYETASAC IPASYVKKAA
60 70 80 90 100
EYVSGKLAIC TVIGFPNGYS TTAAKVFECQ DAIKNGADEI DMVINLTDVK
110 120 130 140 150
NGDFDTVEEE IRQIKAACQD HILKVIVETC QLTKEELIEL CGVVTRSGAD
160 170 180 190 200
FIKTSTGFST AGATFEDVEV MAKYVGEGVK IKAAGGISSL EDAEKFIALG
210 220
ASRLGTSRII KIVKNQKVEE GTY
Length:223
Mass (Da):24,017
Last modified:November 8, 2005 - v1
Checksum:i1629FF6D96E11EEC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000114 Genomic DNA. Translation: ABA44945.1.
RefSeqiYP_330599.1. NC_007432.1.

Genome annotation databases

EnsemblBacteriaiABA44945; ABA44945; SAK_2009.
GeneIDi3685469.
KEGGisak:SAK_2009.
PATRICi19635370. VBIStrAga82541_1987.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000114 Genomic DNA. Translation: ABA44945.1.
RefSeqiYP_330599.1. NC_007432.1.

3D structure databases

ProteinModelPortaliQ3JYQ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi205921.SAK_2009.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA44945; ABA44945; SAK_2009.
GeneIDi3685469.
KEGGisak:SAK_2009.
PATRICi19635370. VBIStrAga82541_1987.

Phylogenomic databases

eggNOGiCOG0274.
HOGENOMiHOG000241645.
KOiK01619.
OMAiKHVDHTL.
OrthoDBiEOG6QZMW5.

Enzyme and pathway databases

UniPathwayiUPA00002; UER00468.
BioCyciSAGA205921:GHD7-2010-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00114. DeoC_type1.
InterProiIPR013785. Aldolase_TIM.
IPR011343. DeoC.
IPR002915. DeoC/FbaB/lacD_aldolase.
IPR028581. DeoC_typeI.
[Graphical view]
PANTHERiPTHR10889. PTHR10889. 1 hit.
PfamiPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFiPIRSF001357. DeoC. 1 hit.
TIGRFAMsiTIGR00126. deoC. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome analysis of multiple pathogenic isolates of Streptococcus agalactiae: implications for the microbial 'pan-genome'."
    Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D., Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T., Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D., Hauser C.R., Sundaram J.P.
    , Nelson W.C., Madupu R., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H., Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D., Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O., Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L., Wessels M.R., Rappuoli R., Fraser C.M.
    Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27591 / A909 / CDC SS700.

Entry informationi

Entry nameiDEOC_STRA1
AccessioniPrimary (citable) accession number: Q3JYQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 8, 2005
Last modified: January 7, 2015
This is version 65 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

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.