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Reviewed, UniProtKB/Swiss-Prot P24058 (ARLY2_ANAPL)

Last modified June 16, 2009. Version 76. 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-2 crystallin
    Delta crystallin II
Gene names
Name: ASL2
OrganismAnas platyrhynchos (Domestic duck) (Anas boschas)
Taxonomic identifier8839 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Anseriformes › Anatidae › Anas

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Protein attributes

Sequence length468 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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Catalytic activity

2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Pathway

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

Subunit structure

Homotetramer. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Tissue specificity

Eye lens. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.1

Miscellaneous

Each of the four substrate binding sites present in the homotetrameric assembly are shared between three of the four subunits.

Sequence similarities

Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.05 mM for N(omega)-(L-arginino)succinate

Vmax=1.10 µmol/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.8

Inferred from direct assay. Source: UniProtKB

structural constituent of eye lens Ref.7

Traceable author statement. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 468468Argininosuccinate lyase
PRO_0000137717

Regions

Region114 – 1163Substrate binding

Sites

Active site1621Proton acceptor; shared with tetrameric partner 2
Active site2831Proton acceptor; shared with tetrameric partner 1
Active site2961Charge relay system; shared with tetrameric partner 1
Binding site291Substrate
Binding site911Substrate
Binding site1611Substrate; shared with tetrameric partner 2
Binding site2891Substrate; shared with tetrameric partner 1
Binding site3231Substrate
Binding site3281Substrate
Binding site3311Substrate

Experimental info

Mutagenesis111W → A: 98% decrease in catalytic efficiency. Ref.3
Mutagenesis111W → F: 90% decrease in catalytic efficiency. Ref.3
Mutagenesis111W → M: 99% decrease in catalytic efficiency. Ref.3
Mutagenesis111W → R: 97% decrease in catalytic efficiency. Ref.3
Mutagenesis111W → Y: 50% decrease in catalytic efficiency. Ref.3
Mutagenesis291S → A: 10% decrease in catalytic efficiency. Ref.7
Mutagenesis331D → N: 99% decrease in catalytic efficiency. Ref.7
Mutagenesis891D → N: Loss of activity. Ref.7
Mutagenesis911H → N: 90% decrease in catalytic activity with 10-fold decrease in substrate affinity.
Mutagenesis1161N → D: 99% decrease in catalytic efficiency. Ref.7
Mutagenesis1171D → A: 55% decrease in catalytic efficiency. Ref.3
Mutagenesis1171D → E: 58% decrease in catalytic efficiency. Ref.3
Mutagenesis1611T → A: Loss of activity. Ref.7 Ref.8
Mutagenesis1611T → D: Loss of activity. Ref.7 Ref.8
Mutagenesis1611T → S: 30% decrease in catalytic efficiency. Ref.7 Ref.8
Mutagenesis1611T → V: Loss of activity. Ref.7 Ref.8
Mutagenesis1621H → E: Loss of activity. Ref.7
Mutagenesis2381R → Q: Loss of activity. Ref.7
Mutagenesis2811T → V: 80% decrease in catalytic efficiency. Ref.7
Mutagenesis2831S → A: Loss of activity. Ref.7
Mutagenesis2831S → C: Loss of activity. Ref.7
Mutagenesis2831S → D: Loss of activity. Ref.7
Mutagenesis2831S → H: Loss of activity. Ref.7
Mutagenesis2831S → T: Loss of activity. Ref.7
Mutagenesis2911N → L: Loss of activity. Ref.7
Mutagenesis2931D → N: 99% decrease in catalytic efficiency. Ref.7
Mutagenesis2961E → D: Loss of activity. Ref.7
Mutagenesis3251K → N: 99% decrease in catalytic efficiency. Ref.7
Mutagenesis3301D → N: Loss of activity. Ref.7
Mutagenesis3311K → Q: Loss of activity. Ref.7

Secondary structure

1 ............................................................... 468
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P24058-1 [UniParc].

Last modified May 30, 2000. Version 4.
Checksum: FBFD26EDC762E7BC

FASTA46851,710
        10         20         30         40         50         60 
MASEARGDKL WGGRFSGSTD PIMEKLNSSI AYDQRLSEVD IQGSMAYAKA LEKAGILTKT 

        70         80         90        100        110        120 
ELEKILSGLE KISEEWSKGV FVVKQSDEDI HTANERRLKE LIGDIAGKLH TGRSRNDQVV 

       130        140        150        160        170        180 
TDLKLFMKNS LSIISTHLLQ LIKTLVERAA IEIDVILPGY THLQKAQPIR WSQFLLSHAV 

       190        200        210        220        230        240 
ALTRDSERLG EVKKRINVLP LGSGALAGNP LDIDREMLRS ELEFASISLN SMDAISERDF 

       250        260        270        280        290        300 
VVEFLSFATL LMIHLSKMAE DLIIYSTSEF GFLTLSDAFS TGSSLMPQKK NPDSLELIRS 

       310        320        330        340        350        360 
KAGRVFGRLA SILMVLKGLP STYNKDLQED KEAVFDVVDT LTAVLQVATG VISTLQISKE 

       370        380        390        400        410        420 
NMEKALTPEM LATDLALYLV RKGVPFRQAH TASGKAVHLA ETKGITINKL SLEDLKSISP 

       430        440        450        460 
QFSSDVSQVF NFVNSVEQYT ALAGTAKSSV TTQIEQLREL MKKQKEQA

« Hide

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References

[1]"Gene conversion and splice-site slippage in the argininosuccinate lyases/delta-crystallins of the duck lens: members of an enzyme superfamily."
Wistow G.J., Piatigorsky J.
Gene 96:263-270(1990) [PubMed: 2269436] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Lens.
[2]Graham C., Wistow G.J.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 246-247.
[3]"Recovery of argininosuccinate lyase activity in duck delta1 crystallin."
Tsai M., Koo J., Howell P.L.
Biochemistry 44:9034-9044(2005) [PubMed: 15966727] [Abstract]
Cited for: MUTAGENESIS OF TRP-11 AND ASP-117.
[4]"Structural comparison of the enzymatically active and inactive forms of delta crystallin and the role of histidine 91."
Abu-Abed M., Turner M.A., Vallee F., Simpson A., Slingsby C., Howell P.L.
Biochemistry 36:14012-14022(1997) [PubMed: 9369472] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT ASN-91, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY.
[5]"Crystal structure of an inactive duck delta II crystallin mutant with bound argininosuccinate."
Vallee F., Turner M.A., Lindley P.L., Howell P.L.
Biochemistry 38:2425-2434(1999) [PubMed: 10029536] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ASN-162 IN COMPLEX WITH ARGINOSUCCINATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY.
[6]"Structural studies of duck delta 1 and delta 2 crystallin suggest conformational changes occur during catalysis."
Sampaleanu L.M., Vallee F., Slingsby C., Howell P.L.
Biochemistry 40:2732-2742(2001) [PubMed: 11258884] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY.
[7]"Mutational analysis of duck delta 2 crystallin and the structure of an inactive mutant with bound substrate provide insight into the enzymatic mechanism of argininosuccinate lyase."
Sampaleanu L.M., Yu B., Howell P.L.
J. Biol. Chem. 277:4166-4175(2002) [PubMed: 11698398] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF MUTANT ALA-283 IN COMPLEX WITH ARGINOSUCCINATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY, MUTAGENESIS OF SER-29; ASP-33; ASP-89; ASN-116; THR-161; HIS-162; ARG-238; THR-281; SER-283; ASN-291; ASP-293; GLU-296; LYS-325; ASP-330 AND LYS-331.
[8]"Structural studies of duck delta2 crystallin mutants provide insight into the role of Thr161 and the 280s loop in catalysis."
Sampaleanu L.M., Codding P.W., Lobsanov Y.D., Tsai M., Smith G.D., Horvatin C., Howell P.L.
Biochem. J. 384:437-447(2004) [PubMed: 15320872] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANTS ASP-161 AND SER-161, CATALYTIC ACTIVITY, MUTAGENESIS OF THR-161, FUNCTION, SUBUNIT, TISSUE SPECIFICITY.

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Cross-references

Sequence databases

M35132 mRNA. Translation: AAC31658.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AUWX-ray2.50A/B/C/D1-468[»]
1DCNX-ray2.30A/B/C/D19-465[»]
1HY1X-ray2.30A/B/C/D1-468[»]
1K7WX-ray1.96A/B/C/D1-468[»]
1TJUX-ray2.10A/B/C/D1-468[»]
1TJVX-ray2.00A/B/C/D1-468[»]
1TJWX-ray2.00A/B/C/D1-468[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENP24058.

Enzyme and pathway databases

BRENDA4.3.2.1. 3217.

Family and domain databases

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

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Entry information

Entry nameARLY2_ANAPL
AccessionPrimary (citable) accession number: P24058
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: May 30, 2000
Last modified: June 16, 2009
This is version 76 of the entry and version 4 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