SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P24058

- ARLY2_ANAPL

UniProt

P24058 - ARLY2_ANAPL

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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.5 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 enzyme

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
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 (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 lyaseUniRule annotation
PRO_0000137717Add
BLAST

Expressioni

Tissue specificityi

Eye lens.6 Publications

Interactioni

Subunit structurei

Homotetramer.5 Publications

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP24058.

Family & Domainsi

Region

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

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: June 11, 2014
This is version 99 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

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