Q6G468 (DAPA_BARHE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	dapA
Ordered Locus Names:	BH05000

Organism

Bartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea henselae) [Complete proteome] [HAMAP]

Taxonomic identifier

283166 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length	294 AA.
Sequence status	Complete.
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 Probable. Ref.2
Subcellular location	Cytoplasm By similarity HAMAP MF_00418.
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: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dihydrodipicolinate synthase activity Inferred from electronic annotation. Source: EC
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_1000050166

Regions

Region

48 – 49

2

Pyruvate binding By similarity

Sites

Active site

162

1

Schiff-base intermediate with substrate By similarity

Binding site

106

1

Pyruvate By similarity

Site

133

1

Involved in proton transfer during cleavage By similarity

Secondary structure

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294

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Helix

21 – 33

13

Beta strand

37 – 40

4

Turn

44 – 47

4

Helix

48 – 50

3

Helix

53 – 67

15

Beta strand

73 – 76

4

Helix

82 – 94

13

Beta strand

98 – 103

6

Helix

112 – 125

14

Beta strand

130 – 134

5

Helix

136 – 139

4

Helix

145 – 154

10

Beta strand

158 – 163

6

Helix

169 – 178

10

Beta strand

180 – 187

8

Helix

189 – 191

3

Helix

192 – 197

6

Beta strand

202 – 206

5

Helix

207 – 209

3

Helix

212 – 223

12

Helix

227 – 243

17

Beta strand

246 – 248

3

Helix

251 – 259

9

Helix

276 – 288

13

Sequences

	Sequence		Length	Mass (Da)
	Q6G468 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: CDD074F2CDE871AE	FASTA	294	31,483
	10 20 30 40 50 60 MLKGAVTALI TPFDDNGAID EKAFCNFVEW QITQGINGVS PVGTTGESPT LTHEEHKRII 70 80 90 100 110 120 ELCVEQVAKR VPVVAGAGSN STSEAVELAK HAEKAGADAV LVVTPYYNRP NQRGLYTHFS 130 140 150 160 170 180 SIAKAISIPI IIYNIPSRSV IDMAVETMRD LCRDFKNIIG VKDATGKIER ASEQREKCGK 190 200 210 220 230 240 DFVQLSGDDC TALGFNAHGG VGCISVSSNV APKLCAQLHA ACLCSDYKTA LKLNDLLMPL 250 260 270 280 290 NRAVFIEPSP AGIKYAAAKL GLCGTIVRSP IVPLSDTTKK IIDEALYHAG LLKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae." Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E. Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49882 / Houston 1.
[2]	"Crystal structure of dihydrodipicolinate synthase from Bartonella henselae." New York structural genomix research consortium (NYSGXRC) Submitted (JUN-2011) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX897699 Genomic DNA. Translation: CAF27308.1.

RefSeq

YP_033336.1. NC_005956.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3SI9	X-ray	2.10	A/B/C/D	1-294	[»]

ProteinModelPortal

Q6G468.

SMR

Q6G468. Positions 1-288.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

2864503.

GenomeReviews

Gene locus BH05000 in contig BX897699_GR.

KEGG

bhe:BH05000.

NMPDR

fig|283166.1.peg.464.

PATRIC

20544783. VBIBarHen29080_0544.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG358848.

OMA

HFKAVHD.

PhylomeDB

Q6G468.

ProtClustDB

PRK03170.

Enzyme and pathway databases

BioCyc

BHEN283166:BH05000-MONOMER.

Family and domain databases

HAMAP

MF_00418. DapA.
[Tree]

InterPro

IPR013785. Aldolase_TIM.
IPR002220. Dihydrodipicolinate_synth-like.
IPR020625. Dihydrodipicolinate_synth_AS.
IPR005263. Dihydrodipicolinate_synth_DapA.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

KO

K01714.

PANTHER

PTHR12128. DHDPS. 1 hit.

Pfam

PF00701. DHDPS. 1 hit.
[Graphical view]

PIRSF

PIRSF001365. DHDPS. 1 hit.

PRINTS

PR00146. DHPICSNTHASE.

TIGRFAMs

TIGR00674. DapA. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

DAPA_BARHE

Accession

Primary (citable) accession number: Q6G468

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program