ARLY_ANSAN
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 03-AUG-2022, entry version 104.
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}.
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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 PDBsum; 1XWO; -.
DR AlphaFoldDB; P33110; -.
DR SMR; P33110; -.
DR UniPathway; UPA00068; UER00114.
DR EvolutionaryTrace; P33110; -.
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:arginine biosynthetic process; TAS:UniProtKB.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR Gene3D; 1.10.275.10; -; 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 PANTHER; PTHR43814; PTHR43814; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00838; argH; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
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..51
FT /evidence="ECO:0007829|PDB:1XWO"
FT HELIX 57..75
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
