Reviewed, UniProtKB/Swiss-Prot Q9X1P5 (DEOC_THEMA)

Names and origin

Protein names

Recommended name:
    Deoxyribose-phosphate aldolase
    EC=4.1.2.4
Alternative name(s):
    Phosphodeoxyriboaldolase
      Short name=Deoxyriboaldolase
      Short name=DERA

Gene names

Name:	deoC
Ordered Locus Names:	TM_1559

Organism

Thermotoga maritima [Complete proteome] [HAMAP]

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. HAMAP MF_00114
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. HAMAP MF_00114
Subcellular location	Cytoplasm By similarity.
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	3D-structure 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
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 – 248

248

Deoxyribose-phosphate aldolase HAMAP MF_00114

PRO_0000057280

Sites

Active site

179

1

Schiff-base intermediate with acetaldehyde By similarity

Active site

208

1

By similarity

Secondary structure

1

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248

Helix Strand Turn

Details...

Helix

1 – 16

16

Beta strand

22 – 24

3

Helix

28 – 34

7

Beta strand

35 – 39

5

Helix

46 – 59

14

Beta strand

62 – 66

5

Helix

68 – 70

3

Helix

71 – 78

8

Beta strand

84 – 90

7

Turn

91 – 93

3

Helix

98 – 111

14

Beta strand

114 – 119

6

Helix

122 – 126

5

Helix

130 – 143

14

Turn

144 – 146

3

Beta strand

147 – 152

6

Helix

155 – 157

3

Helix

160 – 172

13

Beta strand

176 – 179

4

Beta strand

183 – 186

4

Helix

191 – 201

11

Beta strand

205 – 212

8

Helix

216 – 224

9

Beta strand

228 – 233

6

Helix

235 – 245

11

Sequences

	Sequence		Length	Mass (Da)
	Q9X1P5-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 7236D2ECA2CA1951	FASTA	248	27,285
	10 20 30 40 50 60 MIEYRIEEAV AKYREFYEFK PVRESAGIED VKSAIEHTNL KPFATPDDIK KLCLEARENR 70 80 90 100 110 120 FHGVCVNPCY VKLAREELEG TDVKVVTVVG FPLGANETRT KAHEAIFAVE SGADEIDMVI 130 140 150 160 170 180 NVGMLKAKEW EYVYEDIRSV VESVKGKVVK VIIETCYLDT EEKIAACVIS KLAGAHFVKT 190 200 210 220 230 240 STGFGTGGAT AEDVHLMKWI VGDEMGVKAS GGIRTFEDAV KMIMYGADRI GTSSGVKIVQ GGEERYGG

References

[1]

"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE000512 Genomic DNA. Translation: AAD36625.1.

PIR

B72240.

RefSeq

NP_229359.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O0Y	X-ray	1.90	A/B	1-248	[»]

ModBase

Search...

Genome annotation databases

GeneID

897566.

GenomeReviews

Gene locus TM_1559 in contig AE000512_GR.

KEGG

tma:TM1559.

NMPDR

fig|243274.1.peg.1543.

TIGR

TM_1559.

Phylogenomic databases

HOGENOM

Q9X1P5.

OMA

Q9X1P5. AKMIDHT.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_1559-MON.

BRENDA

4.1.2.4. 16699.

Family and domain databases

HAMAP

MF_00114.
[Tree]

InterPro

IPR013785. Aldolase_TIM.
IPR011343. DeoC.
IPR002915. DeoC/AroFGH_arch.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

PANTHER

PTHR10889. DeoC. 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_THEMA

Accession

Primary (citable) accession number: Q9X1P5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)