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P0A6L2 (DAPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxy-tetrahydrodipicolinate synthase

Short name=HTPA synthase
EC=4.3.3.7
Gene names
Name:dapA
Ordered Locus Names:b2478, JW2463
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Protein existenceEvidence 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 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.18, 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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-907527,EBI-907527

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2922924-hydroxy-tetrahydrodipicolinate synthase HAMAP-Rule MF_00418
PRO_0000103110

Sites

Active site1331Proton donor/acceptor Ref.8 Ref.27
Active site1611Schiff-base intermediate with substrate Ref.8 Ref.27
Binding site451Pyruvate
Binding site2031Pyruvate; via carbonyl oxygen
Site441Part of a proton relay during catalysis
Site491L-lysine inhibitor binding; via carbonyl oxygen
Site801L-lysine inhibitor binding
Site841L-lysine inhibitor binding
Site1061L-lysine inhibitor binding
Site1071Part of a proton relay during catalysis

Experimental info

Mutagenesis441T → 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
Mutagenesis441T → V: Reduced kcat by 99.9%. Ref.19 Ref.27
Mutagenesis1071Y → F: Reduced kcat by 90%. Ref.19 Ref.24
Mutagenesis1071Y → 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
Mutagenesis1331Y → F: Reduced kcat by 99.7%. Reduced affinity for both substrates. Ref.19
Mutagenesis1381R → A or H: Strongly increased KM for L-aspartate 4-semialdehyde. No effect on KM for pyruvate. Reduced activity by 99.7%. Ref.21
Mutagenesis1611K → 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
Mutagenesis1611K → 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
Mutagenesis1971L → 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 conflict2071A → T in AAA23665. Ref.1
Sequence conflict2241G → E in AAA23665. Ref.1

Secondary structure

.................................................... 292
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6L2 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 3970543296A77C08

FASTA29231,270
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 277:1453-1462(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.
+Additional computationally mapped references.

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.
PIRSYECDP. E65023.
RefSeqNP_416973.1. NC_000913.3.
YP_490706.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DHPX-ray2.30A/B1-292[»]
1S5TX-ray2.30A/B1-292[»]
1S5VX-ray2.35A/B1-292[»]
1S5WX-ray2.32A/B1-292[»]
1YXCX-ray1.90A/B1-292[»]
1YXDX-ray2.00A/B1-292[»]
2A6LX-ray2.05A/B1-292[»]
2A6NX-ray1.94A/B1-292[»]
2ATSX-ray1.90A/B1-292[»]
2OJPX-ray1.70A/B1-292[»]
2PURX-ray1.70A/B1-292[»]
3C0JX-ray2.40A/B1-292[»]
3DENX-ray2.20A/B1-292[»]
3DU0X-ray2.00A/B1-292[»]
3I7QX-ray2.00A/B1-292[»]
3I7RX-ray2.10A/B1-292[»]
3I7SX-ray2.30A/B1-292[»]
4EOUX-ray2.30A/B1-292[»]
ProteinModelPortalP0A6L2.
SMRP0A6L2. Positions 1-292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0A6L2. 3 interactions.
STRING511145.b2478.

Chemistry

BindingDBP0A6L2.
ChEMBLCHEMBL4083.

2D gel databases

SWISS-2DPAGEP0A6L2.

Proteomic databases

PaxDbP0A6L2.
PRIDEP0A6L2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75531; AAC75531; b2478.
BAA16355; BAA16355; BAA16355.
GeneID12932974.
946952.
KEGGecj:Y75_p2431.
eco:b2478.
PATRIC32120343. VBIEscCol129921_2574.

Organism-specific databases

EchoBASEEB0201.
EcoGeneEG10205. dapA.

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHOG000173604.
KOK01714.
OMAMLYSGDD.
OrthoDBEOG6W7235.
PhylomeDBP0A6L2.

Enzyme and pathway databases

BioCycEcoCyc:DIHYDRODIPICSYN-MONOMER.
ECOL316407:JW2463-MONOMER.
MetaCyc:DIHYDRODIPICSYN-MONOMER.
SABIO-RKP0A6L2.
UniPathwayUPA00034; UER00017.

Gene expression databases

GenevestigatorP0A6L2.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00418. DapA.
InterProIPR013785. Aldolase_TIM.
IPR005263. DapA.
IPR002220. DapA-like.
IPR020625. Dihydrodipicolinate_synth_AS.
IPR020624. Dihydrodipicolinate_synth_CS.
[Graphical view]
PANTHERPTHR12128. PTHR12128. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFPIRSF001365. DHDPS. 1 hit.
PRINTSPR00146. DHPICSNTHASE.
TIGRFAMsTIGR00674. dapA. 1 hit.
PROSITEPS00665. DHDPS_1. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A6L2.
PROP0A6L2.

Entry information

Entry nameDAPA_ECOLI
AccessionPrimary (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 14, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene