NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
DOI=10.1101/gr.1285603; PubMed=12840036 [NCBI, ExPASy, EBI, Israel, Japan]
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens.";
Genome Res. 13:1572-1579(2003).

Comments

CATALYTIC ACTIVITY: 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde.
PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-D-ribose 1-phosphate: step 2/2 .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the deoC/fbaB aldolase family. DeoC type 1 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000035; BAC17211.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_737011.1; -.

3D structure databases

ModBase

Q8FSJ0.

Enzyme and pathway databases

BioCyc

CEFF196164:CE0401-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004139;	Molecular function: deoxyribose-phosphate aldolase activity (inferred from electronic annotation from HAMAP).
GO:0016052;	Biological process: carbohydrate catabolic process (inferred from electronic annotation from HAMAP).
GO:0009264;	Biological process: deoxyribonucleotide catabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_00114; -; 1.
PBIL [Tree]

InterPro

IPR013785; Aldolase_TIM.
IPR011343; DeoC.
IPR002915; DeoC/AroFGH_arch.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

PANTHER

PTHR10889; DeoC; 1.

Pfam

PF01791; DeoC; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001357; DeoC; 1.

TIGRFAMs

TIGR00126; deoC; 1.

Genome annotation databases

1032522; -.

BA000035_GR; CE0401.

cef:CE0401; -.

fig|196164.1.peg.401; -.

Phylogenomic databases

HOGENOM

Q8FSJ0; -.

Genome annotation databases

CMR

Q8FSJ0; CE0401.

Other

ProtoNet

Q8FSJ0.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Lyase; Schiff base.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 222`	`222`	`Deoxyribose-phosphate aldolase.`	`PRO_0000057229`
`ACT_SITE`	`156 156`		`Schiff-base intermediate with acetaldehyde (By similarity).`
`ACT_SITE`	`186 186`		`By similarity.`

Sequence information

Length: 222 AA [This is the length of the unprocessed precursor]

Molecular weight: 22539 Da [This is the MW of the unprocessed precursor]

CRC64: E56DB37B09819089 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTITRAEMAS ILDYTLLGPE VTTADLQALI DDALTLGVPT ICIPPSMMNA TKRAQDAGLR 

        70         80         90        100        110        120 
IATVAGFPHG KSAPLVKAAE ARLAVQYGAS EVDVVLDIAA VKAADDNALL AEMVAIREAL 

       130        140        150        160        170        180 
ASPVTLKFIV ESAVVDDVAL EVATHAARAA GADFIKTSTG FHPAGGATVE AVRVLAGAAQ 

       190        200        210        220 
GQIGVKASGG IRTWEQAVAM VEAGATRIGT SNARAILEGA PA

Q8FSJ0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools