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Protein

Argininosuccinate lyase

Gene

ASL2

Organism
Anas platyrhynchos (Mallard) (Anas boschas)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

2-(N(omega)-L-arginino)succinate = fumarate + L-arginine.5 Publications

Kineticsi

  1. KM=0.05 mM for N(omega)-(L-arginino)succinate1 Publication
  1. Vmax=1.10 µmol/min/mg enzyme1 Publication

Pathway:iL-arginine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. Argininosuccinate lyase (ASL2)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei29 – 291Substrate
Binding sitei91 – 911Substrate
Binding sitei161 – 1611Substrate; shared with tetrameric partner 2
Active sitei162 – 1621Proton acceptor; shared with tetrameric partner 2
Active sitei283 – 2831Proton acceptor; shared with tetrameric partner 1
Binding sitei289 – 2891Substrate; shared with tetrameric partner 1
Active sitei296 – 2961Charge relay system; shared with tetrameric partner 1
Binding sitei323 – 3231Substrate
Binding sitei328 – 3281Substrate
Binding sitei331 – 3311Substrate

GO - Molecular functioni

  • argininosuccinate lyase activity Source: UniProtKB
  • structural constituent of eye lens Source: UniProtKB

GO - Biological processi

  • arginine biosynthetic process Source: UniProtKB
  • arginine biosynthetic process via ornithine Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein, Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Enzyme and pathway databases

SABIO-RKP24058.
UniPathwayiUPA00068; UER00114.

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate lyase (EC:4.3.2.1)
Short name:
ASAL
Alternative name(s):
Arginosuccinase
Delta crystallin II
Delta-2 crystallin
Gene namesi
Name:ASL2
OrganismiAnas platyrhynchos (Mallard) (Anas boschas)
Taxonomic identifieri8839 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeAnseriformesAnatidaeAnas
ProteomesiUP000016666 Componenti: Unassembled WGS sequence

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111W → A: 98% decrease in catalytic efficiency. 1 Publication
Mutagenesisi11 – 111W → F: 90% decrease in catalytic efficiency. 1 Publication
Mutagenesisi11 – 111W → M: 99% decrease in catalytic efficiency. 1 Publication
Mutagenesisi11 – 111W → R: 97% decrease in catalytic efficiency. 1 Publication
Mutagenesisi11 – 111W → Y: 50% decrease in catalytic efficiency. 1 Publication
Mutagenesisi29 – 291S → A: 10% decrease in catalytic efficiency. 1 Publication
Mutagenesisi33 – 331D → N: 99% decrease in catalytic efficiency. 1 Publication
Mutagenesisi89 – 891D → N: Loss of activity. 1 Publication
Mutagenesisi91 – 911H → N: 90% decrease in catalytic activity with 10-fold decrease in substrate affinity.
Mutagenesisi116 – 1161N → D: 99% decrease in catalytic efficiency. 1 Publication
Mutagenesisi117 – 1171D → A: 55% decrease in catalytic efficiency. 1 Publication
Mutagenesisi117 – 1171D → E: 58% decrease in catalytic efficiency. 1 Publication
Mutagenesisi161 – 1611T → A: Loss of activity. 2 Publications
Mutagenesisi161 – 1611T → D: Loss of activity. 2 Publications
Mutagenesisi161 – 1611T → S: 30% decrease in catalytic efficiency. 2 Publications
Mutagenesisi161 – 1611T → V: Loss of activity. 2 Publications
Mutagenesisi162 – 1621H → E: Loss of activity. 1 Publication
Mutagenesisi238 – 2381R → Q: Loss of activity. 1 Publication
Mutagenesisi281 – 2811T → V: 80% decrease in catalytic efficiency. 1 Publication
Mutagenesisi283 – 2831S → A: Loss of activity. 1 Publication
Mutagenesisi283 – 2831S → C: Loss of activity. 1 Publication
Mutagenesisi283 – 2831S → D: Loss of activity. 1 Publication
Mutagenesisi283 – 2831S → H: Loss of activity. 1 Publication
Mutagenesisi283 – 2831S → T: Loss of activity. 1 Publication
Mutagenesisi291 – 2911N → L: Loss of activity. 1 Publication
Mutagenesisi293 – 2931D → N: 99% decrease in catalytic efficiency. 1 Publication
Mutagenesisi296 – 2961E → D: Loss of activity. 1 Publication
Mutagenesisi325 – 3251K → N: 99% decrease in catalytic efficiency. 1 Publication
Mutagenesisi330 – 3301D → N: Loss of activity. 1 Publication
Mutagenesisi331 – 3311K → Q: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Argininosuccinate lyasePRO_0000137717Add
BLAST

Expressioni

Tissue specificityi

Eye lens.6 Publications

Interactioni

Subunit structurei

Homotetramer.5 Publications

Structurei

Secondary structure

1
468
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 277Combined sources
Helixi30 – 334Combined sources
Helixi34 – 363Combined sources
Helixi37 – 5317Combined sources
Helixi59 – 7719Combined sources
Helixi90 – 10213Combined sources
Helixi104 – 1107Combined sources
Helixi115 – 15137Combined sources
Turni152 – 1543Combined sources
Beta strandi156 – 1616Combined sources
Beta strandi164 – 1707Combined sources
Helixi171 – 19626Combined sources
Beta strandi197 – 1993Combined sources
Turni204 – 2074Combined sources
Helixi215 – 2228Combined sources
Beta strandi225 – 2273Combined sources
Helixi231 – 2366Combined sources
Helixi239 – 26527Combined sources
Turni268 – 2703Combined sources
Beta strandi272 – 2743Combined sources
Helixi277 – 2793Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi286 – 2916Combined sources
Helixi293 – 31624Combined sources
Beta strandi321 – 3233Combined sources
Helixi325 – 3295Combined sources
Helixi330 – 35425Combined sources
Helixi359 – 3646Combined sources
Helixi368 – 3714Combined sources
Helixi372 – 3809Combined sources
Turni381 – 3833Combined sources
Helixi386 – 40116Combined sources
Turni402 – 4043Combined sources
Helixi407 – 4093Combined sources
Helixi412 – 4187Combined sources
Helixi424 – 4296Combined sources
Helixi432 – 4365Combined sources
Beta strandi444 – 4463Combined sources
Helixi447 – 46519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP24058.
SMRiP24058. Positions 19-467.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24058.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni114 – 1163Substrate binding

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG004281.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00006. Arg_succ_lyase.
InterProiIPR029419. 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]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PTHR11444:SF3. PTHR11444:SF3. 1 hit.
PfamiPF14698. ASL_C2. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00838. argH. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P24058-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASEARGDKL WGGRFSGSTD PIMEKLNSSI AYDQRLSEVD IQGSMAYAKA
60 70 80 90 100
LEKAGILTKT ELEKILSGLE KISEEWSKGV FVVKQSDEDI HTANERRLKE
110 120 130 140 150
LIGDIAGKLH TGRSRNDQVV TDLKLFMKNS LSIISTHLLQ LIKTLVERAA
160 170 180 190 200
IEIDVILPGY THLQKAQPIR WSQFLLSHAV ALTRDSERLG EVKKRINVLP
210 220 230 240 250
LGSGALAGNP LDIDREMLRS ELEFASISLN SMDAISERDF VVEFLSFATL
260 270 280 290 300
LMIHLSKMAE DLIIYSTSEF GFLTLSDAFS TGSSLMPQKK NPDSLELIRS
310 320 330 340 350
KAGRVFGRLA SILMVLKGLP STYNKDLQED KEAVFDVVDT LTAVLQVATG
360 370 380 390 400
VISTLQISKE NMEKALTPEM LATDLALYLV RKGVPFRQAH TASGKAVHLA
410 420 430 440 450
ETKGITINKL SLEDLKSISP QFSSDVSQVF NFVNSVEQYT ALAGTAKSSV
460
TTQIEQLREL MKKQKEQA
Length:468
Mass (Da):51,710
Last modified:May 30, 2000 - v4
Checksum:iFBFD26EDC762E7BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35132 mRNA. Translation: AAC31658.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35132 mRNA. Translation: AAC31658.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP24058.
SMRiP24058. Positions 19-467.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004281.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00114.
SABIO-RKP24058.

Miscellaneous databases

EvolutionaryTraceiP24058.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00006. Arg_succ_lyase.
InterProiIPR029419. 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]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PTHR11444:SF3. PTHR11444:SF3. 1 hit.
PfamiPF14698. ASL_C2. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00838. argH. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiARLY2_ANAPL
AccessioniPrimary (citable) accession number: P24058
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: May 30, 2000
Last modified: May 27, 2015
This is version 105 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.