Adenylosuccinate lyase - Escherichia coli (strain K12)

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P0AB89 (PUR8_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Adenylosuccinate lyase
Short name=ASL
EC=4.3.2.2

Alternative name(s):
Adenylosuccinase
Short name=ASase

Gene names

Name:	purB
Ordered Locus Names:	b1131, JW1117

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity

N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.

(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.

Sequence similarities

Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	IMP biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity Inferred from electronic annotation. Source: EC N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Inferred from direct assay. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 456

456

Adenylosuccinate lyase

PRO_0000137878

Sites

Active site

Proton donor By similarity

Active site

171

Proton acceptor By similarity

Amino acid modifications

Modified residue

N6-acetyllysine Ref.7

Modified residue

366

N6-acetyllysine Ref.7

Experimental info

Sequence conflict

145

P → A in AAA92731. Ref.1

Sequence conflict

154

I → L in AAA92731. Ref.1

Secondary structure

456

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AB89 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 8D1F4546B66795BC
Show »

FASTA

456

51,543

        10         20         30         40         50         60 
MELSSLTAVS PVDGRYGDKV SALRGIFSEY GLLKFRVQVE VRWLQKLAAH AAIKEVPAFA 

        70         80         90        100        110        120 
ADAIGYLDAI VASFSEEDAA RIKTIERTTN HDVKAVEYFL KEKVAEIPEL HAVSEFIHFA 

       130        140        150        160        170        180 
CTSEDINNLS HALMLKTARD EVILPYWRQL IDGIKDLAVQ YRDIPLLSRT HGQPATPSTI 

       190        200        210        220        230        240 
GKEMANVAYR MERQYRQLNQ VEILGKINGA VGNYNAHIAA YPEVDWHQFS EEFVTSLGIQ 

       250        260        270        280        290        300 
WNPYTTQIEP HDYIAELFDC VARFNTILID FDRDVWGYIA LNHFKQKTIA GEIGSSTMPH 

       310        320        330        340        350        360 
KVNPIDFENS EGNLGLSNAV LQHLASKLPV SRWQRDLTDS TVLRNLGVGI GYALIAYQST 

       370        380        390        400        410        420 
LKGVSKLEVN RDHLLDELDH NWEVLAEPIQ TVMRRYGIEK PYEKLKELTR GKRVDAEGMK 

       430        440        450 
QFIDGLALPE EEKARLKAMT PANYIGRAIT MVDELK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Escherichia coli purB gene: cloning, nucleotide sequence, and regulation by purR." He B., Smith J.M., Zalkin H. J. Bacteriol. 174:130-136(1992) [PubMed: 1729205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6. Strain: K12.
[2]	Green S.M., Drabble W.T. Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Molecular analysis of the Escherichia coli phoP-phoQ operon." Kasahara M., Nakata A., Shinagawa H. J. Bacteriol. 174:492-498(1992) [PubMed: 1729240] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-456. Strain: K12.
[7]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94 AND LYS-366, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M74924 Genomic DNA. Translation: AAA92731.1.
X59307 Genomic DNA. Translation: CAA41996.1.
U00096 Genomic DNA. Translation: AAC74215.1.
AP009048 Genomic DNA. Translation: BAA35953.1.

PIR

S19212.

RefSeq

NP_415649.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PTQ	X-ray	2.00	A/B	1-456	[»]
2PTR	X-ray	1.85	A/B	1-456	[»]
2PTS	X-ray	2.00	A	1-456	[»]

ProteinModelPortal

P0AB89.

SMR

P0AB89. Positions 2-456.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AB89. 11 interactions.

MINT

MINT-1253735.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000823; EBESCP00000000823; EBESCG00000000686.
EBESCT00000014780; EBESCP00000014071; EBESCG00000013840.

GeneID

945695.

GenomeReviews

Gene locus JW1117 in contig AP009048_GR.
Gene locus b1131 in contig U00096_GR.

KEGG

ecj:JW1117.
eco:b1131.

PATRIC

32117511. VBIEscCol129921_1178.

Organism-specific databases

EchoBASE

EB1290.

EcoGene

EG11314. purB.

Phylogenomic databases

eggNOG

COG0015.

GeneTree

EBGT00050000009426.

HOGENOM

HBG290028.

OMA

KVSEFIH.

PhylomeDB

P0AB89.

ProtClustDB

PRK09285.

Enzyme and pathway databases

BioCyc

EcoCyc:ASL-MONOMER.
MetaCyc:ASL-MONOMER.

Gene expression databases

Genevestigator

P0AB89.

Family and domain databases

InterPro

IPR013539. AdenyloSucc_lyase_C_pln.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR008948. L-Aspartase-like.
IPR024083. L-Aspartase-like_N.
IPR022761. Lyase1_N.
IPR004769. Pur_lyase.
[Graphical view]

Gene3D

G3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.

K01756.

PANTHER

PTHR11444:SF2. PTHR11444:SF2. 1 hit.

Pfam

PF08328. ASL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]

PRINTS

PR00149. FUMRATELYASE.

SUPFAM

SSF48557. L-Aspartase-like. 1 hit.

TIGRFAMs

TIGR00928. PurB. 1 hit.

PROSITE

PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PUR8_ECOLI

Accession

Primary (citable) accession number: P0AB89
Secondary accession number(s): P25739

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents