ID   ARLY_NOSP7              Reviewed;         461 AA.
AC   Q9LAE5; B2JA54;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006, ECO:0000303|PubMed:11683360};
DE            Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006};
DE            Short=ASL {ECO:0000303|PubMed:11683360};
DE            EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006, ECO:0000269|PubMed:11683360};
DE   AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006};
GN   Name=argH {ECO:0000255|HAMAP-Rule:MF_00006, ECO:0000303|PubMed:11683360};
GN   OrderedLocusNames=Npun_F5831;
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, PATHWAY, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 29133 / PCC 73102;
RX   PubMed=11683360; DOI=10.1007/s002840010298;
RA   Troshina O., Hansel A., Lindblad P.;
RT   "Cloning, characterization, and functional expression in Escherichia coli
RT   of argH encoding argininosuccinate lyase in the cyanobacterium Nostoc sp.
RT   strain PCC 73102.";
RL   Curr. Microbiol. 43:260-264(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA   Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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:11683360};
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, ECO:0000269|PubMed:11683360}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11683360}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}.
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DR   EMBL; AF143209; AAF66620.1; -; Genomic_DNA.
DR   EMBL; CP001037; ACC84129.1; -; Genomic_DNA.
DR   RefSeq; WP_012412072.1; NC_010628.1.
DR   AlphaFoldDB; Q9LAE5; -.
DR   SMR; Q9LAE5; -.
DR   STRING; 63737.Npun_F5831; -.
DR   EnsemblBacteria; ACC84129; ACC84129; Npun_F5831.
DR   KEGG; npu:Npun_F5831; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_3; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   PhylomeDB; Q9LAE5; -.
DR   BRENDA; 4.3.2.1; 4371.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001191; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
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; Cytoplasm; Lyase;
KW   Reference proteome.
FT   CHAIN           1..461
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000137798"
FT   CONFLICT        92
FT                   /note="K -> R (in Ref. 1; AAF66620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        366
FT                   /note="D -> N (in Ref. 1; AAF66620)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   461 AA;  51415 MW;  6B69F49E9A26CCC3 CRC64;
     MTKEQTWSQR FESALHPAIA RFNASIGFDI ELIEYDLTGS QAHAKMLAHT GIISSEEGEQ
     LVAGLEQIRQ EHRQGKFHPG VDAEDVHFAV EKRLTEIVGD VGKKLHTARS RNDQVGTDTR
     LYLRDQIQQI KSELREFQGV LLDIAEKHVE TLIPGYTHLQ RAQPVSLAHH LLAYFQMAQR
     DWERLGDVSR RVNISPLGCG ALAGTTFPID RHYTAKLLDF DNIYANSLDG VSDRDFAIEF
     LCAASLIMVH LSRLAEEVIL WSSEEFRFVI LKDSCATGSS IMPQKKNPDV PELVRGKTGR
     VFGHLQAMLV IMKGLPLAYN KDLQEDKEGL FDSVNTVKAS LEAMTILLRE GLEFRTQRLA
     QAVTEDFSNA TDVADYLAAR GVPFREAYNL VGKVVKTSIA AGKLLKDLEL EEWQQLHPAF
     AADIYEAISP RQVVAARNSH GGTGFVQVSK ALIAARAQID Q