ARLY_COLLI
ID ARLY_COLLI Reviewed; 466 AA.
AC Q01592;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-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; Synonyms=DELTAP;
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Lens;
RX PubMed=1397328; DOI=10.1016/0014-5793(92)81119-7;
RA Lin C.-W., Chiou S.-H.;
RT "Sequence analysis of pigeon delta-crystallin gene and its deduced primary
RT structure. Comparison of avian delta-crystallins with and without
RT endogenous argininosuccinate lyase activity.";
RL FEBS Lett. 311:276-280(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-100, CATALYTIC ACTIVITY, SUBUNIT, BLOCKAGE
RP OF N-TERMINUS, AND TISSUE SPECIFICITY.
RC TISSUE=Lens;
RX PubMed=1477105; DOI=10.1016/0167-4838(92)90094-t;
RA Chiou S.-H., Hung C.-C., Lin C.-W.;
RT "Biochemical characterization of crystallins from pigeon lenses: structural
RT and sequence analysis of pigeon delta-crystallin.";
RL Biochim. Biophys. Acta 1160:317-324(1992).
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, but it has a low
CC activity.
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; Evidence={ECO:0000269|PubMed:1477105};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:1477105}.
CC -!- TISSUE SPECIFICITY: Eye lens. {ECO:0000269|PubMed:1397328,
CC ECO:0000269|PubMed:1477105}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000305}.
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DR EMBL; X66404; CAA47031.1; -; mRNA.
DR PIR; S29247; S29247.
DR RefSeq; NP_001302456.1; NM_001315527.1.
DR AlphaFoldDB; Q01592; -.
DR SMR; Q01592; -.
DR GeneID; 102086394; -.
DR KEGG; clv:102086394; -.
DR OrthoDB; 1074729at2759; -.
DR UniPathway; UPA00068; UER00114.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
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 Amino-acid biosynthesis; Arginine biosynthesis; Eye lens protein; Lyase.
FT CHAIN 1..466
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137721"
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"
SQ SEQUENCE 466 AA; 51086 MW; 86EBBD1E19D9627E CRC64;
MASEGDKMLG GRFVGSTDPV MEMLSASITI DQRLAEVDIQ GSMAYAKALE KAGILSKSEL
EKTLSGLEKI SEEWSKGVFV VTPTDEDIHT ANERRLKELI GDIAGKLHTG RSRNDQVVTD
LKLFMKNSLS VISTHLLQLI KTLVERAAIE VDVILPGYTH LQKTQPIRWS QFLLSHAVAL
TRDSERLGEI KKRINILPLG SGALAGNPLE IDRELLRSEL DFASISLNSM DAVRQRDSVV
EFLSVAALLM IHLSKMAEDL IIYSTSEFGF LTLSDTYCTG SSVMPQKKNP DSLELIRSKA
GRVFGRLAAI LMVLKGLPST YNKDLQEDKE AVFDVVDTLN AVLQVATGVI STLQINKENM
EKALSPEILS SDLALYLVHK GMPFRQAHVA SGKAVHLAES KGITLNNLSL DDLKSISPLF
GSDVSQVFNV VNSVEQYTAL GGTAKSSVTA QIEQLRELLK RHKEQA
