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Protein

Argininosuccinate lyase

Gene

ASL2

Organism
Anas platyrhynchos (Mallard) (Anas boschas)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

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

Keywordsi

Molecular functionEye lens protein, Lyase
Biological processAmino-acid biosynthesis, Arginine biosynthesis

Enzyme and pathway databases

SABIO-RKiP24058
UniPathwayi
UPA00068;UER00114

Protein family/group databases

MoonProtiP24058

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeAnseriformesAnatidaeAnatinaeAnas
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

3D structure databases

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, 2 hits
HAMAPiMF_00006 Arg_succ_lyase, 1 hit
InterProiView protein in InterPro
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
PANTHERiPTHR43814 PTHR43814, 1 hit
PfamiView protein in Pfam
PF14698 ASL_C2, 1 hit
PF00206 Lyase_1, 1 hit
PRINTSiPR00149 FUMRATELYASE
SUPFAMiSSF48557 SSF48557, 1 hit
TIGRFAMsiTIGR00838 argH, 1 hit
PROSITEiView protein in PROSITE
PS00163 FUMARATE_LYASES, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiARLY2_ANAPL
AccessioniPrimary (citable) accession number: P24058
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: May 30, 2000
Last modified: April 25, 2018
This is version 114 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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