Reviewed, UniProtKB/Swiss-Prot Q9X1K9 (DAPA_THEMA)

Names and origin

Protein names

Recommended name:
    Dihydrodipicolinate synthase
      Short name=DHDPS
    EC=4.2.1.52

Gene names

Name:	dapA
Ordered Locus Names:	TM_1521

Organism

Thermotoga maritima [Complete proteome] [HAMAP]

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	294 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + 2 H2O. HAMAP MF_00418
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. HAMAP MF_00418
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the DHDPS family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Cellular component	Cytoplasm
Ligand	Schiff base
Molecular function	Lyase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	diaminopimelate biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dihydrodipicolinate synthase 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 – 294

294

Dihydrodipicolinate synthase HAMAP MF_00418

PRO_0000103175

Regions

Region

47 – 48

2

Pyruvate binding By similarity

Sites

Active site

161

1

Schiff-base intermediate with substrate By similarity

Binding site

105

1

Pyruvate By similarity

Site

132

1

Involved in proton transfer during cleavage By similarity

Secondary structure

1

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294

Helix Strand Turn

Details...

Helix

20 – 32

13

Helix

47 – 49

3

Helix

52 – 66

15

Helix

81 – 93

13

Beta strand

100 – 102

3

Helix

115 – 122

8

Beta strand

130 – 133

4

Helix

144 – 153

10

Helix

167 – 180

14

Helix

191 – 193

3

Helix

194 – 199

6

Helix

209 – 211

3

Helix

214 – 225

12

Helix

229 – 245

17

Beta strand

248 – 250

3

Helix

253 – 261

9

Helix

278 – 290

13

Sequences

	Sequence		Length	Mass (Da)
	Q9X1K9-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 64C93C64734A351D	FASTA	294	32,390
	10 20 30 40 50 60 MFRGVGTAIV TPFKNGELDL ESYERLVRYQ LENGVNALIV LGTTGESPTV NEDEREKLVS 70 80 90 100 110 120 RTLEIVDGKI PVIVGAGTNS TEKTLKLVKQ AEKLGANGVL VVTPYYNKPT QEGLYQHYKY 130 140 150 160 170 180 ISERTDLGIV VYNVPGRTGV NVLPETAARI AADLKNVVGI KEANPDIDQI DRTVSLTKQA 190 200 210 220 230 240 RSDFMVWSGN DDRTFYLLCA GGDGVISVVS NVAPKQMVEL CAEYFSGNLE KSREVHRKLR 250 260 270 280 290 PLMKALFVET NPIPVKAALN LMGFIENELR LPLVPASEKT VELLRNVLKE SGLL

References

	« Hide 'large scale' referencesShow 'large scale' 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.
[2]	"Crystal structure of dihydrodipicolinate synthase (TM1521) from Thermotoga maritima at 1.80 A resolution." Joint center for structural genomics (JCSG) Submitted (MAR-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE000512 Genomic DNA. Translation: AAD36588.1.

PIR

B72246.

RefSeq

NP_229321.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O5K	X-ray	1.80	A/B	1-294	[»]

SMR

Q9X1K9. Positions 1-294.

ModBase

Search...

Genome annotation databases

GeneID

897344.

GenomeReviews

Gene locus TM_1521 in contig AE000512_GR.

KEGG

tma:TM1521.

NMPDR

fig|243274.1.peg.1505.

TIGR

TM_1521.

Phylogenomic databases

HOGENOM

Q9X1K9.

OMA

EGTDGIV

Enzyme and pathway databases

BioCyc

TMAR243274:TM_1521-MON.

BRENDA

4.2.1.52. 16699.

Family and domain databases

HAMAP

MF_00418.
[Tree]

InterPro

IPR013785. Aldolase_TIM.
IPR005263. DapA_synth.
IPR002220. Dihydrodipicolinate_synth.
IPR020625. Dihydrodipicolinate_synth_AS.
IPR020624. Dihydrodipicolinate_synth_CS.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

PANTHER

PTHR12128. DHDPS. 1 hit.

Pfam

PF00701. DHDPS. 1 hit.
[Graphical view]

PRINTS

PR00146. DHPICSNTHASE.

TIGRFAMs

TIGR00674. dapA. 1 hit.

PROSITE

PS00665. DHDPS_1. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DAPA_THEMA

Accession

Primary (citable) accession number: Q9X1K9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	November 24, 2009
This is version 67 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)