ID   ARLY_CLOBK              Reviewed;         440 AA.
AC   B1IK07;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006};
DE            Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE   AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006};
GN   Name=argH {ECO:0000255|HAMAP-Rule:MF_00006}; OrderedLocusNames=CLD_1895;
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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};
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   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}.
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DR   EMBL; CP000939; ACA46282.1; -; Genomic_DNA.
DR   RefSeq; WP_003404558.1; NC_010516.1.
DR   AlphaFoldDB; B1IK07; -.
DR   SMR; B1IK07; -.
DR   EnsemblBacteria; ACA46282; ACA46282; CLD_1895.
DR   KEGG; cbb:CLD_1895; -.
DR   HOGENOM; CLU_027272_2_3_9; -.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000008541; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase.
FT   CHAIN           1..440
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000089076"
SQ   SEQUENCE   440 AA;  50293 MW;  9DBA70E1E5E0A255 CRC64;
     MKLWGGRFKE EESKLMEDFN SSLSFDKKLY YEDIRGSIAH VKMLANQNII KEEEKEKILL
     GLEEILKEID EGILKIEGDY EDIHSFVEIN LINKIGNVGK KLHTGRSRND QVALDMKLYA
     KKSTEEVIEC LKELMDSLIK VGNENNYIMP GYTHLQRAQV VTFRYHLLAY FEMFKRDEKR
     LKNALEILNE SPLGSGALAG STYSIDREYT AKLLGFRKPV DNFLDGVSDR DYIIELISKF
     SIIMMHLSRL SEELILWSSS EFRFIQIGDA YSTGSSIMPQ KKNPDGAELI RGKTGRVYGD
     LIGILTVMKS LPLAYNKDMQ EDKEPFFDAK DTVISCLKVM EGIISTLKVN KENLMKSVKK
     GFLNATEAAD YLVNKGMAFR DAHKVIGEIV IYCEDKNSAI EDLSLEELKQ FSDLFCEDIY
     GFIDYKSSIN KGIKKEMGYS