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P24058

- ARLY2_ANAPL

UniProt

P24058 - ARLY2_ANAPL

Protein

Argininosuccinate lyase

Gene

ASL2

Organism
Anas platyrhynchos (Domestic duck) (Anas boschas)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 4 (30 May 2000)
      Previous versions | rss
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    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

    Vmax=1.10 µmol/min/mg enzyme1 Publication

    Pathwayi

    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

    1. argininosuccinate lyase activity Source: UniProtKB
    2. structural constituent of eye lens Source: UniProtKB

    GO - Biological processi

    1. arginine biosynthetic process Source: UniProtKB
    2. arginine biosynthetic process via ornithine Source: InterPro

    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 (Domestic duck) (Anas boschas)
    Taxonomic identifieri8839 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeAnseriformesAnatidaeAnas
    ProteomesiUP000016666: Unplaced

    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 – 277
    Helixi30 – 334
    Helixi34 – 363
    Helixi37 – 5317
    Helixi59 – 7719
    Helixi90 – 10213
    Helixi104 – 1107
    Helixi115 – 15137
    Turni152 – 1543
    Beta strandi156 – 1616
    Beta strandi164 – 1707
    Helixi171 – 19626
    Beta strandi197 – 1993
    Turni204 – 2074
    Helixi215 – 2228
    Beta strandi225 – 2273
    Helixi231 – 2366
    Helixi239 – 26527
    Turni268 – 2703
    Beta strandi272 – 2743
    Helixi277 – 2793
    Beta strandi281 – 2833
    Beta strandi286 – 2916
    Helixi293 – 31624
    Beta strandi321 – 3233
    Helixi325 – 3295
    Helixi330 – 35425
    Helixi359 – 3646
    Helixi368 – 3714
    Helixi372 – 3809
    Turni381 – 3833
    Helixi386 – 40116
    Turni402 – 4043
    Helixi407 – 4093
    Helixi412 – 4187
    Helixi424 – 4296
    Helixi432 – 4365
    Beta strandi444 – 4463
    Helixi447 – 46519

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MASEARGDKL WGGRFSGSTD PIMEKLNSSI AYDQRLSEVD IQGSMAYAKA    50
    LEKAGILTKT ELEKILSGLE KISEEWSKGV FVVKQSDEDI HTANERRLKE 100
    LIGDIAGKLH TGRSRNDQVV TDLKLFMKNS LSIISTHLLQ LIKTLVERAA 150
    IEIDVILPGY THLQKAQPIR WSQFLLSHAV ALTRDSERLG EVKKRINVLP 200
    LGSGALAGNP LDIDREMLRS ELEFASISLN SMDAISERDF VVEFLSFATL 250
    LMIHLSKMAE DLIIYSTSEF GFLTLSDAFS TGSSLMPQKK NPDSLELIRS 300
    KAGRVFGRLA SILMVLKGLP STYNKDLQED KEAVFDVVDT LTAVLQVATG 350
    VISTLQISKE NMEKALTPEM LATDLALYLV RKGVPFRQAH TASGKAVHLA 400
    ETKGITINKL SLEDLKSISP QFSSDVSQVF NFVNSVEQYT ALAGTAKSSV 450
    TTQIEQLREL MKKQKEQA 468
    Length:468
    Mass (Da):51,710
    Last modified:May 30, 2000 - v4
    Checksum:iFBFD26EDC762E7BC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M35132 mRNA. Translation: AAC31658.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M35132 mRNA. Translation: AAC31658.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AUW X-ray 2.50 A/B/C/D 1-468 [» ]
    1DCN X-ray 2.30 A/B/C/D 19-465 [» ]
    1HY1 X-ray 2.30 A/B/C/D 1-468 [» ]
    1K7W X-ray 1.96 A/B/C/D 1-468 [» ]
    1TJU X-ray 2.10 A/B/C/D 1-468 [» ]
    1TJV X-ray 2.00 A/B/C/D 1-468 [» ]
    1TJW X-ray 2.00 A/B/C/D 1-468 [» ]
    ProteinModelPortali P24058.
    SMRi P24058. Positions 19-467.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG004281.

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00114 .
    SABIO-RK P24058.

    Miscellaneous databases

    EvolutionaryTracei P24058.

    Family and domain databases

    Gene3Di 1.10.275.10. 1 hit.
    HAMAPi MF_00006. Arg_succ_lyase.
    InterProi IPR029419. 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 ]
    PANTHERi PTHR11444. PTHR11444. 1 hit.
    PTHR11444:SF3. PTHR11444:SF3. 1 hit.
    Pfami PF14698. ASL_C2. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00149. FUMRATELYASE.
    SUPFAMi SSF48557. SSF48557. 1 hit.
    TIGRFAMsi TIGR00838. argH. 1 hit.
    PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 100 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