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Reviewed, UniProtKB/Swiss-Prot P33110 (ARLY_ANSAN)

Last modified September 22, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Argininosuccinate lyase
      Short name=ASAL
    EC=4.3.2.1
Alternative name(s):
    Arginosuccinase
    Delta crystallin
Gene names
Name: ASL
OrganismAnser anser anser (Western graylag goose)
Taxonomic identifier8844 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Anseriformes › Anatidae › Anser

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Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Delta crystallin, the principal crystallin in embryonic lens, is found only in birds and reptiles. This protein also functions as an enzymatically active argininosuccinate lyase.

Catalytic activity

2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. Ref.2

Pathway

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

Subunit structure

Homotetramer.

Tissue specificity

Eye lens. Ref.1

Sequence similarities

Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.

Biophysicochemical properties

Kinetic parameters:

Vmax=19 nmol/min/mg enzyme

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Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentEye lens protein
   Molecular functionLyase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processarginine biosynthetic process via ornithine

Inferred from electronic annotation. Source: InterPro

   Molecular functionargininosuccinate lyase activity Ref.2

Inferred from direct assay. Source: UniProtKB

structural constituent of eye lens Ref.2

Traceable author statement. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Argininosuccinate lyase
PRO_0000137718

Regions

Region112 – 1143Substrate binding By similarity

Sites

Active site1601Proton acceptor; shared with tetrameric partner 2 By similarity
Active site2811Proton acceptor; shared with tetrameric partner 1 By similarity
Active site2941Charge relay system; shared with tetrameric partner 1 By similarity
Binding site271Substrate By similarity
Binding site891Substrate By similarity
Binding site1591Substrate; shared with tetrameric partner 2 By similarity
Binding site2871Substrate; shared with tetrameric partner 1 By similarity
Binding site3211Substrate By similarity
Binding site3261Substrate By similarity
Binding site3291Substrate By similarity

Secondary structure

1 .............................................................. 466
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P33110-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 2D346902B8821C10

FASTA46651,372
        10         20         30         40         50         60 
MASEGDKLMG GRFVGSTDPI MQMLSTSMST EQRLSEVDIQ ASIAYAKALE KAGILTKTEL 

        70         80         90        100        110        120 
EKILSGLEKI SEEWSKGVFV VTQSDEDIHT ANERRLKELI GDIAGKLNTG RSRNEQVVTD 

       130        140        150        160        170        180 
LKLFMKNSLS VISTHLLQLI KTLVERAAIE IDVILPGYTH LQKAQPIRWS QFLLSHAVAL 

       190        200        210        220        230        240 
TRDSERLGEV KRRINVLPLG SGALAGNPLD IDREMLRSEL DFASISLNSM DAISERDFVV 

       250        260        270        280        290        300 
EFLSVATLLM IHLSKMAEDL IIYSTSEFGF LTLSDAFSTG SSLMPQKKNP DSLELIRSKA 

       310        320        330        340        350        360 
GRVFGRLASI LMVLKGLPST YNKDLQEDKE AVFDVVDTLT AVLQVATGVI STLQISKENM 

       370        380        390        400        410        420 
EKALTPEMLS TDLALYLVRK GMPFRQAHTA SGKAVHLAET KGITINNLTL EDLKSISPLF 

       430        440        450        460 
SSDVSQVFNF VNSVEQYTAM GGTAKSSVTT QIEHLRELMK KQKEQA

« Hide

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References

[1]"Facile cloning and sequence analysis of goose delta-crystallin gene based on polymerase chain reaction."
Yu C.W., Chiou S.-H.
Biochem. Biophys. Res. Commun. 192:948-953(1993) [PubMed: 8484796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Lens.
[2]"The effect of N-terminal truncation on double-dimer assembly of goose delta-crystallin."
Lee H.J., Lai Y.H., Wu S.Y., Chen Y.H.
Biochem. J. 392:545-554(2005) [PubMed: 16101585] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-466, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

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Cross-references

Sequence databases

X70855 mRNA. Translation: CAA50208.1.
PIRJN0486.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1XWOX-ray2.80A/B/C/D2-466[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENP33110.

Family and domain databases

InterProIPR009049. Argininosuccinate_lyase.
IPR003031. D_crystallin.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
[Graphical view]
PANTHERPTHR11444:SF3. argH. 1 hit.
PfamPF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.
TIGRFAMsTIGR00838. argH. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameARLY_ANSAN
AccessionPrimary (citable) accession number: P33110
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 22, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

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 and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents