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P24058 (ARLY2_ANAPL) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Delta crystallin II
Delta-2 crystallin
Gene names
Name:ASL2
OrganismAnas platyrhynchos (Domestic duck) (Anas boschas) [Complete proteome]
Taxonomic identifier8839 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeAnseriformesAnatidaeAnas

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. HAMAP-Rule MF_00006

Subunit structure

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

Tissue specificity

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

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 Ref.7

Vmax=1.10 µmol/min/mg enzyme

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 468468Argininosuccinate lyase HAMAP-Rule MF_00006
PRO_0000137717

Regions

Region114 – 1163Substrate binding HAMAP-Rule MF_00006

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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P24058 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M35132 mRNA. Translation: AAC31658.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP24058.
SMRP24058. Positions 19-467.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004281.

Enzyme and pathway databases

SABIO-RKP24058.
UniPathwayUPA00068; UER00114.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00006. Arg_succ_lyase.
InterProIPR009049. 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.
PfamPF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR00838. argH. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP24058.

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: March 19, 2014
This is version 98 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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