Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q66G70 (ARLY_YERPS) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Argininosuccinate lyase

Short name=ASAL
EC=4.3.2.1
Alternative name(s):
Arginosuccinase
Gene names
Name:argH
Ordered Locus Names:YPTB0112
OrganismYersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]
Taxonomic identifier273123 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. HAMAP-Rule MF_00006

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. HAMAP-Rule MF_00006

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00006.

Sequence similarities

Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginine biosynthetic process via ornithine

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionargininosuccinate lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Argininosuccinate lyase HAMAP-Rule MF_00006
PRO_0000137856

Sequences

Sequence LengthMass (Da)Tools
Q66G70 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 939A81896A427A09

FASTA45750,099
        10         20         30         40         50         60 
MALWGGRFSQ AADQRFKQFN DSLRFDYRLA EQDIIGSVAW SKALVTVGVL NADEQQQLEQ 

        70         80         90        100        110        120 
ALSVLLEEVQ ANPHAILASD AEDIHSWVET KLIDKVGDLG KKLHTGRSRN DQVATDLKLW 

       130        140        150        160        170        180 
CKFQITELQT AVQQLQQALV MTAEANQDAV MPGYTHLQRA QPVTFAHWCL AYVEMLSRDE 

       190        200        210        220        230        240 
SRLQDTLKRL DVSPLGCGAL AGTAYAIDRE QLAGWLGFAS ATRNSLDSVS DRDHVLELLS 

       250        260        270        280        290        300 
DASIGMVHLS RFAEDLIFFN SGEAAFVDLS DRVTSGSSLM PQKKNPDALE LIRGKCGRVQ 

       310        320        330        340        350        360 
GALTGMTMTL KGLPLAYNKD MQEDKEGLFD ALNTWLDCLH MAALVLDGIQ VKRPRCKEAA 

       370        380        390        400        410        420 
EQGYANATEL ADYLVAKGVP FREAHHIVGE AVVEAIRQGK ALEALALSDL QQFSSVIGDD 

       430        440        450 
VYPILALQSC LDKRVAKGGV SPQQVASAIA EAKARLF 

« Hide

References

[1]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX936398 Genomic DNA. Translation: CAH19352.1.
RefSeqYP_068661.1. NC_006155.1.

3D structure databases

ProteinModelPortalQ66G70.
SMRQ66G70. Positions 3-456.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273123.YPTB0112.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH19352; CAH19352; YPTB0112.
GeneID2955217.
KEGGyps:YPTB0112.
PATRIC18638280. VBIYerPse22266_0263.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0165.
HOGENOMHOG000242744.
KOK01755.
OMAKEGIFDA.
OrthoDBEOG6P5ZF8.

Enzyme and pathway databases

BioCycYPSE273123:GI1M-118-MONOMER.
UniPathwayUPA00068; UER00114.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00006. Arg_succ_lyase.
InterProIPR029419. Arg_succ_lyase_C.
IPR009049. Argininosuccinate_lyase.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERPTHR11444. PTHR11444. 1 hit.
PTHR11444:SF3. PTHR11444:SF3. 1 hit.
PfamPF14698. ASL_C2. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR00838. argH. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARLY_YERPS
AccessionPrimary (citable) accession number: Q66G70
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 11, 2004
Last modified: June 11, 2014
This is version 73 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

PATHWAY comments

Index of metabolic and biosynthesis pathways