Q3JYQ4 (DEOC_STRA1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Deoxyribose-phosphate aldolase
Short name=DERA
EC=4.1.2.4

Alternative name(s):
2-deoxy-D-ribose 5-phosphate aldolase
Phosphodeoxyriboaldolase
Short name=Deoxyriboaldolase

Gene names

Name:	deoC
Ordered Locus Names:	SAK_2009

Organism

Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC SS700) [Complete proteome] [HAMAP]

Taxonomic identifier

205921 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus agalactiae › Streptococcus agalactiae serogroup Ia

Protein attributes

Sequence length	223 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate By similarity. HAMAP-Rule MF_00114
Catalytic activity	2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. HAMAP-Rule MF_00114
Pathway	Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2. HAMAP-Rule MF_00114
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00114.
Sequence similarities	Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Schiff base
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	carbohydrate catabolic process Inferred from electronic annotation. Source: HAMAP deoxyribonucleotide catabolic process Inferred from electronic annotation. Source: InterPro deoxyribose phosphate catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	deoxyribose-phosphate aldolase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 223	223	Deoxyribose-phosphate aldolase HAMAP-Rule MF_00114		PRO_0000231567
Sites
	Active site	153	1	Schiff-base intermediate with acetaldehyde By similarity
	Active site	182	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3JYQ4 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 1629FF6D96E11EEC	FASTA	223	24,017
	10 20 30 40 50 60 MEVKDILKTV DHTLLATTAT WPEIQTILDD AMAYETASAC IPASYVKKAA EYVSGKLAIC 70 80 90 100 110 120 TVIGFPNGYS TTAAKVFECQ DAIKNGADEI DMVINLTDVK NGDFDTVEEE IRQIKAACQD 130 140 150 160 170 180 HILKVIVETC QLTKEELIEL CGVVTRSGAD FIKTSTGFST AGATFEDVEV MAKYVGEGVK 190 200 210 220 IKAAGGISSL EDAEKFIALG ASRLGTSRII KIVKNQKVEE GTY

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000114 Genomic DNA. Translation: ABA44945.1.
RefSeq	YP_330599.1. NC_007432.1.
3D structure databases
ProteinModelPortal	Q3JYQ4.
ModBase	Search...
Protein-protein interaction databases
STRING	205921.SAK_2009.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABA44945; ABA44945; SAK_2009.
GeneID	3685469.
KEGG	sak:SAK_2009.
PATRIC	19635370. VBIStrAga82541_1987.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0274.
HOGENOM	HOG000241645.
KO	K01619.
OMA	EEKIAMC.
ProtClustDB	PRK00507.
Enzyme and pathway databases
BioCyc	SAGA205921:GHD7-2010-MONOMER.
UniPathway	UPA00002; UER00468.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00114. DeoC_type1.
InterPro	IPR013785. Aldolase_TIM. IPR011343. DeoC. IPR002915. DeoC/FbaB/lacD_aldolase. [Graphical view]
PANTHER	PTHR10889. PTHR10889. 1 hit.
Pfam	PF01791. DeoC. 1 hit. [Graphical view]
PIRSF	PIRSF001357. DeoC. 1 hit.
TIGRFAMs	TIGR00126. deoC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DEOC_STRA1

Accession

Primary (citable) accession number: Q3JYQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	November 8, 2005
Last modified:	May 29, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program