ARLY_CHLRE
ID ARLY_CHLRE Reviewed; 473 AA.
AC P22675; O81953;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Argininosuccinate lyase;
DE Short=ASAL;
DE EC=4.3.2.1;
DE AltName: Full=Arginosuccinase;
GN Name=ARG7;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=137c / CC-125;
RX DOI=10.1080/09670269500650901;
RA Purton S., Rochaix J.-D.;
RT "Characterisation of the ARG7 gene of Chlamydomonas reinhardtii and its
RT application to nuclear transformation.";
RL Eur. J. Phycol. 30:141-148(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=137c / CC-125;
RX PubMed=10071206; DOI=10.1007/s004380050937;
RA Auchincloss A.H., Loroch A.I., Rochaix J.-D.;
RT "The argininosuccinate lyase gene of Chlamydomonas reinhardtii: cloning of
RT the cDNA and its characterization as a selectable shuttle marker.";
RL Mol. Gen. Genet. 261:21-30(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-46; 77-121; 241-304 AND 372-398.
RC STRAIN=137c / CC-125;
RX PubMed=2583083; DOI=10.1002/j.1460-2075.1989.tb08426.x;
RA Debuchy R., Purton S., Rochaix J.-D.;
RT "The argininosuccinate lyase gene of Chlamydomonas reinhardtii: an
RT important tool for nuclear transformation and for correlating the genetic
RT and molecular maps of the ARG7 locus.";
RL EMBO J. 8:2803-2809(1989).
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 -!- MISCELLANEOUS: Often used in tagging mutagenesis schemes to generate
CC new mutants.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA34615.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ010110; CAA09001.1; -; mRNA.
DR EMBL; X16619; CAA34615.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P22675; -.
DR SMR; P22675; -.
DR STRING; 3055.EDP09253; -.
DR PRIDE; P22675; -.
DR ProMEX; P22675; -.
DR EnsemblPlants; PNW88251; PNW88251; CHLRE_01g021251v5.
DR Gramene; PNW88251; PNW88251; CHLRE_01g021251v5.
DR eggNOG; KOG1316; Eukaryota.
DR SABIO-RK; P22675; -.
DR UniPathway; UPA00068; UER00114.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Lyase.
FT CHAIN 1..473
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137723"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT ACT_SITE 289
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 34
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 121
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 166
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 297
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 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 BINDING 334
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 302
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000250|UniProtKB:P24058"
SQ SEQUENCE 473 AA; 52038 MW; 202A3ED446B5171A CRC64;
MAQAAAAPAD NTKKLWGGRF TGKTDPLMEK FNESLPFDKR LWAEDIKGSQ AYAKALAKAG
ILAHDEAVTI VEGLAKVAEE WKAGAFVIKA GDEDIHTANE RRLTELVGAV GGKLHTGRSR
NDQVATDYRL WLVGQVEVMR SEVGELMRVA ADRSEAEVEV LMPGFTHLQN AMTVRWSHWL
MSHAAAWQRD DMRLRDLLPR VATLPLGSGA LAGNPFLVDR QFIAKELGFG GGVCPNSMDA
VSDRDFVIET VFAASLLCVH LSRWAEDLII YSSGPFGYVQ CSDAYATGSS LMPQKKNPDA
LELIRGKGGR VQGNLMGVMA VLKGTPTTYN KDFQECWELL FDTVDTVHDV VRIATGVLST
LRIKPDRMKA GLSADMLATD LAEYLVRKGV PFRETHHHSG AAVKMAEDRG CTLFDLTVDD
LKTIHPLFTD DVAAVWDFNR SAEMRDTEGG TSKRSVLEQV QKMRTYLAAE GQH
