ARLY_LITCT
ID ARLY_LITCT Reviewed; 467 AA.
AC P51464;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Argininosuccinate lyase;
DE Short=ASAL;
DE EC=4.3.2.1;
DE AltName: Full=Arginosuccinase;
GN Name=ASL;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=7841190; DOI=10.1016/0167-4781(94)00183-4;
RA Iwase K., Yamauchi K., Ishikawa K.;
RT "Cloning of cDNAs encoding argininosuccinate lyase and arginase from Rana
RT catesbeiana liver and regulation of their mRNAs during spontaneous and
RT thyroid hormone-induced metamorphosis.";
RL Biochim. Biophys. Acta 1260:139-146(1995).
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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3.
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-arginine and fumarate from
CC (N(omega)-L-arginino)succinate: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
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; D38302; BAA07421.1; -; Genomic_DNA.
DR PIR; S52133; S52133.
DR AlphaFoldDB; P51464; -.
DR SMR; P51464; -.
DR UniPathway; UPA00068; UER00114.
DR UniPathway; UPA00158; UER00273.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Lyase; Urea cycle.
FT CHAIN 1..467
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137722"
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 467 AA; 52258 MW; 9FEED654CFF7DC13 CRC64;
MASEGDKLWG GRFVGSIDPI MEMFNSSVSY DQRMWSADIR GSQAYVKALE KAGLVSPTEM
EHILTGLDQI HEEWSKGTFV LTKADEDIHT ANERRLKELI GEPAGKLHTG RSRNDQVVTD
MRLWLRDSCS ALHLHLTRLI RTMVDRAAIE IDILFPGYTH MQRAQPIRWS HWILSHAVAL
CRDAERLGEL RKRINVLPLG SGAIAGNPLG VDRELLRKEL EFDSVSLNSM DATSERDFIA
EFLFWASLCM THLSKMSEDL IIYSTKEFSF VTLSDSYSTG SSLMPQKKNP DSLELIRSKA
GRVFGRCSGF LMTLKGLPST YNKDLQEDKE AMFDVYDTVC AVLQVASGVI STLQINKEGM
EKALSPDMLA TDIAYYLVRK GMPFRQAHGL SGKVVQLAET KGIALNKLSL EDLKSISPLF
SNDVSKVWNY TNSVEQYTAA GGTAKSCVVA QVEQLRTWLK KTQESVI
