P0A6L2 (DAPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-hydroxy-tetrahydrodipicolinate synthase
Short name=HTPA synthase
EC=4.3.3.7

Gene names

Name:	dapA
Ordered Locus Names:	b2478, JW2463

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	292 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). Ref.15 Ref.18
Catalytic activity	Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H2O. Ref.15 Ref.18
Enzyme regulation	Is allosterically regulated by the feedback inhibitor (S)-lysine. Is inhibited by pyruvate analogs such as 3-fluoropyruvate, 2-ketobutyrate, glyoxylate, and beta-hydroxypyruvate. Is not inhibited by its substrate, (S)-ASA. Ref.12 Ref.13 Ref.26
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. HAMAP-Rule MF_00418
Subunit structure	Homotetramer; dimer of dimers. Ref.20 Ref.24 Ref.25
Subcellular location	Cytoplasm HAMAP-Rule MF_00418.
Sequence similarities	Belongs to the DapA family.
Caution	Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown (Ref.18 and Ref.15) that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB (Ref.15).
Biophysicochemical properties	Kinetic parameters: kcat is 124 sec(-1). KM=0.26 mM for pyruvate Ref.13 Ref.19 KM=0.11 mM for L-aspartate-4-semialdehyde Vmax=0.58 µmol/sec/mg enzyme
Mass spectrometry	Molecular mass is 31272±1 Da from positions 1 - 292. Determined by ESI. Ref.13 Molecular mass is 31270 Da from positions 1 - 292. Determined by ESI. Ref.26

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Cellular component	Cytoplasm
Ligand	Schiff base
Molecular function	Lyase
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	diaminopimelate biosynthetic process Inferred from direct assay PubMed 4910051. Source: EcoliWiki lysine biosynthetic process via diaminopimelate Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	4-hydroxy-tetrahydrodipicolinate synthase Inferred from direct assay PubMed 4910051. Source: EcoliWiki amine-lyase 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 – 292

292

4-hydroxy-tetrahydrodipicolinate synthase HAMAP-Rule MF_00418

PRO_0000103110

Sites

Active site

133

1

Proton donor/acceptor Ref.8 Ref.27

Active site

161

1

Schiff-base intermediate with substrate Ref.8 Ref.27

Binding site

45

1

Pyruvate

Binding site

203

1

Pyruvate; via carbonyl oxygen

Site

44

1

Part of a proton relay during catalysis

Site

49

1

L-lysine inhibitor binding; via carbonyl oxygen

Site

80

1

L-lysine inhibitor binding

Site

84

1

L-lysine inhibitor binding

Site

106

1

L-lysine inhibitor binding

Site

107

1

Part of a proton relay during catalysis

Experimental info

Mutagenesis

44

1

T → S: 8% of wild-type activity. 4-fold decrease in affinity for pyruvate, but nearly no change in that for (S)-ASA. Ref.19 Ref.27

Mutagenesis

44

1

T → V: Reduced kcat by 99.9%. Ref.19 Ref.27

Mutagenesis

107

1

Y → F: Reduced kcat by 90%. Ref.19 Ref.24

Mutagenesis

107

1

Y → W: Reduced activity by 95%. Reduced affinity for both substrates. Exists as a mixture of monomer, dimer and tetramer in solution. Has significantly lower thermal stability than the wild-type enzyme. Ref.19 Ref.24

Mutagenesis

133

1

Y → F: Reduced kcat by 99.7%. Reduced affinity for both substrates. Ref.19

Mutagenesis

138

1

R → A or H: Strongly increased KM for L-aspartate 4-semialdehyde. No effect on KM for pyruvate. Reduced activity by 99.7%. Ref.21

Mutagenesis

161

1

K → A: 0.1% of wild-type activity. 3-fold decrease in affinity for pyruvate, and 2-fold decrease in that for (S)-ASA. Ref.28

Mutagenesis

161

1

K → R: 0.35% of wild-type activity. 3-fold decrease in affinity for pyruvate, but nearly no change in that for (S)-ASA. Ref.28

Mutagenesis

197

1

L → Y or D: 1.4 to 2.5% of wild-type activity. Decrease in affinity for pyruvate, but nearly no change in that for (S)-ASA. Exists as a dimer in solution. Ref.25

Sequence conflict

207

1

A → T in AAA23665. Ref.1

Sequence conflict

224

1

G → E in AAA23665. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

292

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Beta strand

17 – 19

3

Helix

21 – 34

14

Beta strand

38 – 43

6

Turn

44 – 47

4

Helix

48 – 50

3

Helix

53 – 67

15

Beta strand

73 – 76

4

Helix

82 – 91

10

Turn

92 – 94

3

Beta strand

98 – 103

6

Helix

112 – 123

12

Beta strand

130 – 133

4

Helix

136 – 139

4

Helix

145 – 152

8

Beta strand

157 – 160

4

Helix

169 – 174

6

Beta strand

181 – 186

6

Helix

188 – 190

3

Helix

191 – 196

6

Beta strand

201 – 205

5

Helix

206 – 208

3

Helix

211 – 222

12

Helix

226 – 242

17

Beta strand

245 – 247

3

Helix

250 – 258

9

Beta strand

261 – 263

3

Helix

276 – 288

13

Sequences

	Sequence		Length	Mass (Da)
	P0A6L2 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: 3970543296A77C08	FASTA	292	31,270
	10 20 30 40 50 60 MFTGSIVAIV TPMDEKGNVC RASLKKLIDY HVASGTSAIV SVGTTGESAT LNHDEHADVV 70 80 90 100 110 120 MMTLDLADGR IPVIAGTGAN ATAEAISLTQ RFNDSGIVGC LTVTPYYNRP SQEGLYQHFK 130 140 150 160 170 180 AIAEHTDLPQ ILYNVPSRTG CDLLPETVGR LAKVKNIIGI KEATGNLTRV NQIKELVSDD 190 200 210 220 230 240 FVLLSGDDAS ALDFMQLGGH GVISVTANVA ARDMAQMCKL AAEGHFAEAR VINQRLMPLH 250 260 270 280 290 NKLFVEPNPI PVKWACKELG LVATDTLRLP MTPITDSGRE TVRAALKHAG LL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Chromosomal location and nucleotide sequence of the Escherichia coli dapA gene." Richaud F., Richaud C., Ratet P., Patte J.-C. J. Bacteriol. 166:297-300(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F. Submitted (FEB-1996) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-11. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.
[7]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-4. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization." Laber B., Gomis-Rueth F.-X., Romao M.J., Huber R. Biochem. J. 288:691-695(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 156-167, ACTIVE SITE.
[9]	"DNA sequence of the purC gene encoding 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide synthetase and organization of the dapA-purC region of Escherichia coli K-12." Tiedemann A.A., Demarini D.J., Parker J., Smith J.M. J. Bacteriol. 172:6035-6041(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 288-292. Strain: K12.
[10]	"A gene for a new lipoprotein in the dapA-purC interval of the Escherichia coli chromosome." Bouvier J., Pugsley A.P., Stragier P. J. Bacteriol. 173:5523-5531(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 288-292. Strain: K12.
[11]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[12]	"Dihydrodipicolinate synthase from Escherichia coli: pH dependent changes in the kinetic mechanism and kinetic mechanism of allosteric inhibition by L-lysine." Karsten W.E. Biochemistry 36:1730-1739(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[13]	"Dihydrodipicolinate synthase is not inhibited by its substrate, (S)-aspartate beta-semialdehyde." Dobson R.C., Gerrard J.A., Pearce F.G. Biochem. J. 377:757-762(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, KINETIC PARAMETERS, MASS SPECTROMETRY.
[14]	"Irreversible inhibition of dihydrodipicolinate synthase by 4-oxo-heptenedioic acid analogues." Boughton B.A., Griffin M.D., O'Donnell P.A., Dobson R.C., Perugini M.A., Gerrard J.A., Hutton C.A. Bioorg. Med. Chem. 16:9975-9983(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SYNTHETIC INHIBITORS.
[15]	"NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase." Devenish S.R., Blunt J.W., Gerrard J.A. J. Med. Chem. 53:4808-4812(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF HTPA AS REACTION PRODUCT, SUBSTRATE SPECIFICITY.
[16]	"1,3-Phenylene bis(ketoacid) derivatives as inhibitors of Escherichia coli dihydrodipicolinate synthase." Boughton B.A., Hor L., Gerrard J.A., Hutton C.A. Bioorg. Med. Chem. 20:2419-2426(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SYNTHETIC INHIBITORS.
[17]	"The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5-A resolution." Mirwaldt C., Korndoerfer I., Huber R. J. Mol. Biol. 246:227-239(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[18]	"Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy." Blicking S., Renner C., Laber B., Pohlenz H.-D., Holak T.A., Huber R. Biochemistry 36:24-33(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF HTPA AS REACTION PRODUCT, CATALYTIC MECHANISM.
[19]	"The crystal structure of three site-directed mutants of Escherichia coli dihydrodipicolinate synthase: further evidence for a catalytic triad." Dobson R.C.J., Valegaard K., Gerrard J.A. J. Mol. Biol. 338:329-339(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF MUTANTS VAL-44; PHE-107 AND PHE-133, KINETIC PARAMETERS, MUTAGENESIS OF THR-44; TYR-107 AND TYR-133, REACTION MECHANISM.
[20]	"The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance." Dobson R.C.J., Griffin M.D.W., Jameson G.B., Gerrard J.A. Acta Crystallogr. D 61:1116-1124(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH ALLOSTERIC INHIBITOR (S)-LYSINE, SUBUNIT.
[21]	"Role of arginine 138 in the catalysis and regulation of Escherichia coli dihydrodipicolinate synthase." Dobson R.C.J., Devenish S.R.A., Turner L.A., Clifford V.R., Pearce F.G., Jameson G.B., Gerrard J.A. Biochemistry 44:13007-13013(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF MUTANTS ALA-138 AND HIS-138, MUTAGENESIS OF ARG-138.
[22]	"The co-crystallisation of (S)-lysine-bound dihydrodipicolinate synthase from E. coli indicates that domain movements are not responsible for (S)-lysine inhibition." Devenish S.R.A., Dobson R.C.J., Jameson G.B., Gerrard J.A. Submitted (AUG-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH LYSINE INHIBITOR.
[23]	"The high-resolution structure of dihydrodipicolinate synthase from Escherichia coli bound to its first substrate, pyruvate." Devenish S.R., Gerrard J.A., Jameson G.B., Dobson R.C. Acta Crystallogr. F 64:1092-1095(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
[24]	"Mutating the tight-dimer interface of dihydrodipicolinate synthase disrupts the enzyme quaternary structure: toward a monomeric enzyme." Pearce F.G., Dobson R.C., Weber A., Lane L.A., McCammon M.G., Squire M.A., Perugini M.A., Jameson G.B., Robinson C.V., Gerrard J.A. Biochemistry 47:12108-12117(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT TRP-107, SUBUNIT, MUTAGENESIS OF TYR-107.
[25]	"Evolution of quaternary structure in a homotetrameric enzyme." Griffin M.D., Dobson R.C., Pearce F.G., Antonio L., Whitten A.E., Liew C.K., Mackay J.P., Trewhella J., Jameson G.B., Perugini M.A., Gerrard J.A. J. Mol. Biol. 380:691-703(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT TYR-197, SUBUNIT, MUTAGENESIS OF LEU-197.
[26]	"Conserved main-chain peptide distortions: a proposed role for Ile203 in catalysis by dihydrodipicolinate synthase." Dobson R.C., Griffin M.D., Devenish S.R., Pearce F.G., Hutton C.A., Gerrard J.A., Jameson G.B., Perugini M.A. Protein Sci. 17:2080-2090(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), ENZYME REGULATION, MASS SPECTROMETRY.
[27]	"Specificity versus catalytic potency: The role of threonine 44 in Escherichia coli dihydrodipicolinate synthase mediated catalysis." Dobson R.C., Perugini M.A., Jameson G.B., Gerrard J.A. Biochimie 91:1036-1044(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT SER-44, MUTAGENESIS OF THR-44, ACTIVE SITES, REACTION MECHANISM.
[28]	"How essential is the 'essential' active-site lysine in dihydrodipicolinate synthase?" Soares da Costa T.P., Muscroft-Taylor A.C., Dobson R.C., Devenish S.R., Jameson G.B., Gerrard J.A. Biochimie 92:837-845(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANTS ALA-161 AND ARG-161 OF NATIVE PROTEIN AND IN COMPLEX WITH PYRUVATE, MUTAGENESIS OF LYS-161.
[29]	"The crystal structure of dihydrodipicolinate synthase from Escherichia coli with bound pyruvate and succinic acid semialdehyde: unambiguous resolution of the stereochemistry of the condensation product." Boughton B.A., Dobson R.C., Hutton C.A. Proteins 80:2117-2122(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH PYRUVATE AND SUBSTRATE ANALOG INHIBITOR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M12844 Genomic DNA. Translation: AAA23665.1.
U00096 Genomic DNA. Translation: AAC75531.1.
AP009048 Genomic DNA. Translation: BAA16355.1.
M33928 Genomic DNA. No translation available.
X57402 Genomic DNA. Translation: CAA40660.1.

PIR

SYECDP. E65023.

RefSeq

NP_416973.1. NC_000913.2.
YP_490706.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DHP	X-ray	2.30	A/B	1-292	[»]
1S5T	X-ray	2.30	A/B	1-292	[»]
1S5V	X-ray	2.35	A/B	1-292	[»]
1S5W	X-ray	2.32	A/B	1-292	[»]
1YXC	X-ray	1.90	A/B	1-292	[»]
1YXD	X-ray	2.00	A/B	1-292	[»]
2A6L	X-ray	2.05	A/B	1-292	[»]
2A6N	X-ray	1.94	A/B	1-292	[»]
2ATS	X-ray	1.90	A/B	1-292	[»]
2OJP	X-ray	1.70	A/B	1-292	[»]
2PUR	X-ray	1.70	A/B	1-292	[»]
3C0J	X-ray	2.40	A/B	1-292	[»]
3DEN	X-ray	2.20	A/B	1-292	[»]
3DU0	X-ray	2.00	A/B	1-292	[»]
3I7Q	X-ray	2.00	A/B	1-292	[»]
3I7R	X-ray	2.10	A/B	1-292	[»]
3I7S	X-ray	2.30	A/B	1-292	[»]
4EOU	X-ray	2.30	A/B	1-292	[»]

ProteinModelPortal

P0A6L2.

SMR

P0A6L2. Positions 1-292.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6L2. 3 interactions.

STRING

511145.b2478.

2D gel databases

SWISS-2DPAGE

P0A6L2.

Proteomic databases

PaxDb

P0A6L2.

PRIDE

P0A6L2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75531; AAC75531; b2478.
BAA16355; BAA16355; BAA16355.

GeneID

12932974.
946952.

KEGG

ecj:Y75_p2431.
eco:b2478.

PATRIC

32120343. VBIEscCol129921_2574.

Organism-specific databases

EchoBASE

EB0201.

EcoGene

EG10205. dapA.

Phylogenomic databases

eggNOG

COG0329.

HOGENOM

HOG000173604.

KO

K01714.

OMA

ADAILCV.

ProtClustDB

PRK03170.

Enzyme and pathway databases

BioCyc

EcoCyc:DIHYDRODIPICSYN-MONOMER.
ECOL316407:JW2463-MONOMER.
MetaCyc:DIHYDRODIPICSYN-MONOMER.

SABIO-RK

P0A6L2.

UniPathway

UPA00034; UER00017.

Gene expression databases

Genevestigator

P0A6L2.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

HAMAP

MF_00418. DapA.

InterPro

IPR013785. Aldolase_TIM.
IPR002220. Dihydrodipicolinate_synth-like.
IPR020625. Dihydrodipicolinate_synth_AS.
IPR020624. Dihydrodipicolinate_synth_CS.
IPR005263. Dihydrodipicolinate_synth_DapA.
[Graphical view]

PANTHER

PTHR12128. PTHR12128. 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. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P0A6L2.

ChEMBL

CHEMBL4083.

EvolutionaryTrace

P0A6L2.

Entry information

Entry name

DAPA_ECOLI

Accession

Primary (citable) accession number: P0A6L2
Secondary accession number(s): P05640, P78223

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program