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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

Pathwayi: L-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)DescriptionActionsGraphical viewLength
Binding sitei29Substrate1
Binding sitei91Substrate1
Binding sitei161Substrate; shared with tetrameric partner 21
Active sitei162Proton acceptor; shared with tetrameric partner 21
Active sitei283Proton acceptor; shared with tetrameric partner 11
Binding sitei289Substrate; shared with tetrameric partner 11
Active sitei296Charge relay system; shared with tetrameric partner 11
Binding sitei323Substrate1
Binding sitei328Substrate1
Binding sitei331Substrate1

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
Proteomesi
  • UP000016666 Componenti: Unassembled WGS sequence

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi11W → A: 98% decrease in catalytic efficiency. 1 Publication1
Mutagenesisi11W → F: 90% decrease in catalytic efficiency. 1 Publication1
Mutagenesisi11W → M: 99% decrease in catalytic efficiency. 1 Publication1
Mutagenesisi11W → R: 97% decrease in catalytic efficiency. 1 Publication1
Mutagenesisi11W → Y: 50% decrease in catalytic efficiency. 1 Publication1
Mutagenesisi29S → A: 10% decrease in catalytic efficiency. 1 Publication1
Mutagenesisi33D → N: 99% decrease in catalytic efficiency. 1 Publication1
Mutagenesisi89D → N: Loss of activity. 1 Publication1
Mutagenesisi91H → N: 90% decrease in catalytic activity with 10-fold decrease in substrate affinity. 1
Mutagenesisi116N → D: 99% decrease in catalytic efficiency. 1 Publication1
Mutagenesisi117D → A: 55% decrease in catalytic efficiency. 1 Publication1
Mutagenesisi117D → E: 58% decrease in catalytic efficiency. 1 Publication1
Mutagenesisi161T → A: Loss of activity. 2 Publications1
Mutagenesisi161T → D: Loss of activity. 2 Publications1
Mutagenesisi161T → S: 30% decrease in catalytic efficiency. 2 Publications1
Mutagenesisi161T → V: Loss of activity. 2 Publications1
Mutagenesisi162H → E: Loss of activity. 1 Publication1
Mutagenesisi238R → Q: Loss of activity. 1 Publication1
Mutagenesisi281T → V: 80% decrease in catalytic efficiency. 1 Publication1
Mutagenesisi283S → A: Loss of activity. 1 Publication1
Mutagenesisi283S → C: Loss of activity. 1 Publication1
Mutagenesisi283S → D: Loss of activity. 1 Publication1
Mutagenesisi283S → H: Loss of activity. 1 Publication1
Mutagenesisi283S → T: Loss of activity. 1 Publication1
Mutagenesisi291N → L: Loss of activity. 1 Publication1
Mutagenesisi293D → N: 99% decrease in catalytic efficiency. 1 Publication1
Mutagenesisi296E → D: Loss of activity. 1 Publication1
Mutagenesisi325K → N: 99% decrease in catalytic efficiency. 1 Publication1
Mutagenesisi330D → N: Loss of activity. 1 Publication1
Mutagenesisi331K → Q: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001377171 – 468Argininosuccinate lyaseAdd BLAST468

Expressioni

Tissue specificityi

Eye lens.6 Publications

Interactioni

Subunit structurei

Homotetramer.5 Publications

Structurei

Secondary structure

1468
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 27Combined sources7
Helixi30 – 33Combined sources4
Helixi34 – 36Combined sources3
Helixi37 – 53Combined sources17
Helixi59 – 77Combined sources19
Helixi90 – 102Combined sources13
Helixi104 – 110Combined sources7
Helixi115 – 151Combined sources37
Turni152 – 154Combined sources3
Beta strandi156 – 161Combined sources6
Beta strandi164 – 170Combined sources7
Helixi171 – 196Combined sources26
Beta strandi197 – 199Combined sources3
Turni204 – 207Combined sources4
Helixi215 – 222Combined sources8
Beta strandi225 – 227Combined sources3
Helixi231 – 236Combined sources6
Helixi239 – 265Combined sources27
Turni268 – 270Combined sources3
Beta strandi272 – 274Combined sources3
Helixi277 – 279Combined sources3
Beta strandi281 – 283Combined sources3
Beta strandi286 – 291Combined sources6
Helixi293 – 316Combined sources24
Beta strandi321 – 323Combined sources3
Helixi325 – 329Combined sources5
Helixi330 – 354Combined sources25
Helixi359 – 364Combined sources6
Helixi368 – 371Combined sources4
Helixi372 – 380Combined sources9
Turni381 – 383Combined sources3
Helixi386 – 401Combined sources16
Turni402 – 404Combined sources3
Helixi407 – 409Combined sources3
Helixi412 – 418Combined sources7
Helixi424 – 429Combined sources6
Helixi432 – 436Combined sources5
Beta strandi444 – 446Combined sources3
Helixi447 – 465Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24058.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni114 – 116Substrate binding3

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG004281.

Family and domain databases

CDDicd01359. Argininosuccinate_lyase. 1 hit.
Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00006. Arg_succ_lyase. 1 hit.
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
PDB 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.
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

CDDicd01359. Argininosuccinate_lyase. 1 hit.
Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00006. Arg_succ_lyase. 1 hit.
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...

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: November 2, 2016
This is version 109 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

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 one 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.