ID ARLY_ANSAN Reviewed; 466 AA. AC P33110; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 02-SEP-2026, entry version 113. DE RecName: Full=Argininosuccinate lyase; DE Short=ASAL; DE EC=4.3.2.1; DE AltName: Full=Arginosuccinase; DE AltName: Full=Delta crystallin; GN Name=ASL; OS Anser anser anser (Western greylag goose). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae; OC Anserinae; Anser. OX NCBI_TaxID=8844; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Lens; RX PubMed=8484796; DOI=10.1006/bbrc.1993.1507; RA Yu C.W., Chiou S.-H.; RT "Facile cloning and sequence analysis of goose delta-crystallin gene based RT on polymerase chain reaction."; RL Biochem. Biophys. Res. Commun. 192:948-953(1993). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-466, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16101585; DOI=10.1042/bj20050860; RA Lee H.J., Lai Y.H., Wu S.Y., Chen Y.H.; RT "The effect of N-terminal truncation on double-dimer assembly of goose RT delta-crystallin."; RL Biochem. J. 392:545-554(2005). CC -!- FUNCTION: Delta crystallin, the principal crystallin in embryonic lens, CC is found only in birds and reptiles. This protein also functions as an CC enzymatically active argininosuccinate lyase. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine; CC Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682, CC ChEBI:CHEBI:57472; EC=4.3.2.1; CC Evidence={ECO:0000269|PubMed:16101585}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Vmax=19 nmol/min/mg enzyme {ECO:0000269|PubMed:16101585}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine CC from L-ornithine and carbamoyl phosphate: step 3/3. CC -!- SUBUNIT: Homotetramer. CC -!- TISSUE SPECIFICITY: Eye lens. {ECO:0000269|PubMed:8484796}. CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X70855; CAA50208.1; -; mRNA. DR PIR; JN0486; JN0486. DR PDB; 1XWO; X-ray; 2.80 A; A/B/C/D=2-466. DR AlphaFoldDB; P33110; -. DR SMR; P33110; -. DR UniPathway; UPA00068; UER00114. DR EvolutionaryTrace; P33110; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004056; F:argininosuccinate lyase activity; IDA:UniProtKB. DR GO; GO:0005212; F:structural constituent of eye lens; TAS:UniProtKB. DR GO; GO:0006526; P:L-arginine biosynthetic process; TAS:UniProtKB. DR CDD; cd01359; Argininosuccinate_lyase; 1. DR FunFam; 1.10.275.10:FF:000002; Argininosuccinate lyase; 1. DR FunFam; 1.10.40.30:FF:000001; Argininosuccinate lyase; 1. DR FunFam; 1.20.200.10:FF:000002; Argininosuccinate lyase; 1. DR FunFam; 1.20.200.10:FF:000015; argininosuccinate lyase isoform X2; 1. DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1. DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1. DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1. DR HAMAP; MF_00006; Arg_succ_lyase; 1. DR InterPro; IPR029419; Arg_succ_lyase_C. DR InterPro; IPR009049; Argininosuccinate_lyase. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR NCBIfam; TIGR00838; argH; 1. DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1. DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1. DR Pfam; PF14698; ASL_C2; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00145; ARGSUCLYASE. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; L-aspartase-like; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. DR PDBsum; 1XWO; -. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; KW Eye lens protein; Lyase. FT CHAIN 1..466 FT /note="Argininosuccinate lyase" FT /id="PRO_0000137718" FT ACT_SITE 160 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P24058" FT ACT_SITE 281 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P24058" FT BINDING 27 FT /ligand="2-(N(omega)-L-arginino)succinate" FT /ligand_id="ChEBI:CHEBI:57472" FT /ligand_note="ligand shared between tetrameric partners" FT /note="in chain A" FT /evidence="ECO:0000250|UniProtKB:P24058" FT BINDING 114 FT /ligand="2-(N(omega)-L-arginino)succinate" FT /ligand_id="ChEBI:CHEBI:57472" FT /ligand_note="ligand shared between tetrameric partners" FT /note="in chain A" FT /evidence="ECO:0000250|UniProtKB:P24058" FT BINDING 159 FT /ligand="2-(N(omega)-L-arginino)succinate" FT /ligand_id="ChEBI:CHEBI:57472" FT /ligand_note="ligand shared between tetrameric partners" FT /note="in chain C" FT /evidence="ECO:0000250|UniProtKB:P24058" FT BINDING 289 FT /ligand="2-(N(omega)-L-arginino)succinate" FT /ligand_id="ChEBI:CHEBI:57472" FT /ligand_note="ligand shared between tetrameric partners" FT /note="in chain B" FT /evidence="ECO:0000250|UniProtKB:P24058" FT BINDING 321 FT /ligand="2-(N(omega)-L-arginino)succinate" FT /ligand_id="ChEBI:CHEBI:57472" FT /ligand_note="ligand shared between tetrameric partners" FT /note="in chain A" FT /evidence="ECO:0000250|UniProtKB:P24058" FT BINDING 326 FT /ligand="2-(N(omega)-L-arginino)succinate" FT /ligand_id="ChEBI:CHEBI:57472" FT /ligand_note="ligand shared between tetrameric partners" FT /note="in chain A" FT /evidence="ECO:0000250|UniProtKB:P24058" FT BINDING 329 FT /ligand="2-(N(omega)-L-arginino)succinate" FT /ligand_id="ChEBI:CHEBI:57472" FT /ligand_note="ligand shared between tetrameric partners" FT /note="in chain A" FT /evidence="ECO:0000250|UniProtKB:P24058" FT SITE 294 FT /note="Increases basicity of active site His" FT /evidence="ECO:0000250|UniProtKB:P24058" FT HELIX 21..23 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 28..31 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 32..34 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 35..52 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 57..76 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 79..82 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 88..100 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 103..108 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 113..149 FT /evidence="ECO:0007829|PDB:1XWO" FT TURN 150..152 FT /evidence="ECO:0007829|PDB:1XWO" FT STRAND 154..159 FT /evidence="ECO:0007829|PDB:1XWO" FT STRAND 162..168 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 169..194 FT /evidence="ECO:0007829|PDB:1XWO" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:1XWO" FT TURN 202..205 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 213..219 FT /evidence="ECO:0007829|PDB:1XWO" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 229..234 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 237..263 FT /evidence="ECO:0007829|PDB:1XWO" FT TURN 266..268 FT /evidence="ECO:0007829|PDB:1XWO" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 275..277 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 291..314 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 323..327 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 328..352 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 357..362 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 366..369 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 370..378 FT /evidence="ECO:0007829|PDB:1XWO" FT TURN 379..381 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 384..401 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 405..407 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 410..416 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 424..427 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 430..435 FT /evidence="ECO:0007829|PDB:1XWO" FT STRAND 442..444 FT /evidence="ECO:0007829|PDB:1XWO" FT HELIX 445..461 FT /evidence="ECO:0007829|PDB:1XWO" SQ SEQUENCE 466 AA; 51372 MW; 2D346902B8821C10 CRC64; MASEGDKLMG GRFVGSTDPI MQMLSTSMST EQRLSEVDIQ ASIAYAKALE KAGILTKTEL EKILSGLEKI SEEWSKGVFV VTQSDEDIHT ANERRLKELI GDIAGKLNTG RSRNEQVVTD LKLFMKNSLS VISTHLLQLI KTLVERAAIE IDVILPGYTH LQKAQPIRWS QFLLSHAVAL TRDSERLGEV KRRINVLPLG SGALAGNPLD IDREMLRSEL DFASISLNSM DAISERDFVV EFLSVATLLM IHLSKMAEDL IIYSTSEFGF LTLSDAFSTG SSLMPQKKNP DSLELIRSKA GRVFGRLASI LMVLKGLPST YNKDLQEDKE AVFDVVDTLT AVLQVATGVI STLQISKENM EKALTPEMLS TDLALYLVRK GMPFRQAHTA SGKAVHLAET KGITINNLTL EDLKSISPLF SSDVSQVFNF VNSVEQYTAM GGTAKSSVTT QIEHLRELMK KQKEQA //