ID ARLY_SYNY3 Reviewed; 461 AA. AC P73257; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 02-SEP-2026, entry version 164. DE RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006, ECO:0000303|PubMed:35583703}; DE Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006}; DE EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006, ECO:0000269|PubMed:35583703}; DE AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006}; DE AltName: Full=SyArgH {ECO:0000303|PubMed:35583703}; GN Name=argH {ECO:0000255|HAMAP-Rule:MF_00006, GN ECO:0000303|PubMed:38478146}; OrderedLocusNames=slr1133; OS Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Merismopediaceae; Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa; RX PubMed=35583703; DOI=10.1007/s11103-022-01280-x; RA Katayama N., Osanai T.; RT "Arginine inhibition of the argininosuccinate lyases is conserved among RT three orders in cyanobacteria."; RL Plant Mol. Biol. 110:13-22(2022). RN [3] RP OVEREXPRESSION. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa; RX PubMed=38478146; DOI=10.1007/s11103-024-01416-1; RA Katayama N., Osanai T.; RT "Arginine inhibits the arginine biosynthesis rate-limiting enzyme and leads RT to the accumulation of intracellular aspartate in Synechocystis sp. PCC RT 6803."; RL Plant Mol. Biol. 114:27-27(2024). CC -!- FUNCTION: Catalyzes the last step of arginine biosynthesis, the CC conversion of argininosuccinate into L-arginine and fumarate. CC {ECO:0000269|PubMed:35583703}. 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:0000255|HAMAP- CC Rule:MF_00006, ECO:0000269|PubMed:35583703}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24021; CC Evidence={ECO:0000269|PubMed:35583703}; CC -!- ACTIVITY REGULATION: Strongly inhibited by L-arginine CC (PubMed:35583703). Inhibitory effects are lowered at pH 7.0 compared to CC those at pH 8.0 (PubMed:35583703). At 45 degrees Celsius and pH 8.0, CC activity decreases to 94%, 74% and 37% in the presence of 0.6 mM, 2.8 CC mM and 10 mM arginine, respectively (PubMed:35583703). Activity also CC decreases to 86% in the presence of 10 mM sodium succinate or sodium CC citrate (PubMed:35583703). Activity does not decrease in the presence CC of 1 mM or 10 mM L-lysine, which has a similar structure to arginine CC (PubMed:35583703). {ECO:0000269|PubMed:35583703}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.182 mM for argininosuccinate (at 45 degrees Celsius and pH 8.0) CC {ECO:0000269|PubMed:35583703}; CC Note=kcat is 6.78 sec(-1) with argininosuccinate as substrate. CC {ECO:0000269|PubMed:35583703}; CC pH dependence: CC Optimum pH is 8.0 (PubMed:35583703). Shows more than 35% enzymatic CC activity in terms of relative activity at pH 7.5-9.5 CC (PubMed:35583703). {ECO:0000269|PubMed:35583703}; CC Temperature dependence: CC Optimum temperature is 45 degrees Celsius (PubMed:35583703). Shows CC more than 35% enzymatic activity in terms of relative activity at CC 20-50 degrees Celsius (PubMed:35583703). Inactive above 55 degrees CC Celsius (PubMed:35583703). {ECO:0000269|PubMed:35583703}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine CC from L-ornithine and carbamoyl phosphate: step 3/3. {ECO:0000255|HAMAP- CC Rule:MF_00006}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}. CC -!- MISCELLANEOUS: A mutant overexpressing this enzyme grows faster than CC the wild-type strain under photoautotrophic conditions with 5 mM CC NaNO(3) as a nitrogen source (PubMed:38478146). In contrast, the growth CC of the mutant is similar under photoautotrophic conditions with 5 mM CC arginine as a nitrogen source (PubMed:38478146). CC {ECO:0000269|PubMed:38478146}. CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}. 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; BA000022; BAA17284.1; -; Genomic_DNA. DR PIR; S77437; S77437. DR AlphaFoldDB; P73257; -. DR SMR; P73257; -. DR FunCoup; P73257; 398. DR IntAct; P73257; 1. DR STRING; 1148.gene:10498147; -. DR PaxDb; 1148-gene:10498147; -. DR EnsemblBacteria; BAA17284; BAA17284; BAA17284. DR KEGG; syn:slr1133; -. DR eggNOG; COG0165; Bacteria. DR InParanoid; P73257; -. DR PhylomeDB; P73257; -. DR BRENDA; 4.3.2.1; 6192. DR UniPathway; UPA00068; UER00114. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004056; F:argininosuccinate lyase activity; EXP:UniProtKB. DR GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniRule. 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: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. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase; KW Reference proteome. FT CHAIN 1..461 FT /note="Argininosuccinate lyase" FT /id="PRO_0000137841" SQ SEQUENCE 461 AA; 50948 MW; B6E8C81B1CFB5FE2 CRC64; MTKKTWSDRF EGTLHPAIAL FNASIGFDIE LIEYDLDGSI AHGKMLAKTG IISPGEAEQL VQGLEQIRQE YRAGNFNPGV DQEDVHFAVE RRLTELVGDV GKKLHTARSR NDQVGTDVRL YLRAQIDDIR QRLRDFQAVL LQLAETNVET LIPGYTHLQR AQPVSLAHHL LAYFQMAQRD WQRLGEIRAR TNVSPLGSGA LAGTTFPIDR HYSAELLGFA GVYANSLDGV SDRDFAIEFL NAASLIMVHL SRLSEEMILW ASQEFSFISL TDSCATGSSI MPQKKNPDVP ELIRGKAGRV MGHLQGMLVL MKGLPLAYNK DLQEDKEALF DAVKTVQVSL EAMTILLDEG IVFRQERLAE AVAEDFSNAT DVADYLAAKG VPFREAYNLV GKVVKTSLAA GKLLKDLTLA EWQALHPAFE EDIYQAITPQ QVVAARNSYG GTGFEQVKMA IANAKAELSQ T //