ID   ARLY_CLOBH              Reviewed;         440 AA.
AC   A5I5A3; A7G6G6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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};
GN   OrderedLocusNames=CBO2669, CLC_2543;
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA   Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA   Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT   Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
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; CP000727; ABS38692.1; -; Genomic_DNA.
DR   EMBL; AM412317; CAL84230.1; -; Genomic_DNA.
DR   RefSeq; WP_011986965.1; NC_009698.1.
DR   RefSeq; YP_001255168.1; NC_009495.1.
DR   RefSeq; YP_001388381.1; NC_009698.1.
DR   AlphaFoldDB; A5I5A3; -.
DR   SMR; A5I5A3; -.
DR   GeneID; 5186924; -.
DR   KEGG; cbh:CLC_2543; -.
DR   KEGG; cbo:CBO2669; -.
DR   PATRIC; fig|413999.7.peg.2652; -.
DR   HOGENOM; CLU_027272_2_3_9; -.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
DR   PRO; PR:A5I5A3; -.
DR   Proteomes; UP000001986; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IBA:GO_Central.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
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;
KW   Reference proteome.
FT   CHAIN           1..440
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000000468"
SQ   SEQUENCE   440 AA;  50482 MW;  10C3B618D629C920 CRC64;
     MKLWGGRFKE EESKLMEDFN SSLSFDKKLY YEDIKGSIAH VKMLTNQNII KEEEKEKILL
     GLEEILKEID EGILKIEGDY EDIHSFVEIN LINKIGNVGK KLHTGRSRND QVALDMKLYA
     KKSTEEVIEC LKELMDSLIK VGNENNYIMP GYTHLQRAQV VTFRYHLLAY FEMFKRDEKR
     LENALEILNE SPLGSGALAG STYNIDKEYT AKLLGFRKPV DNFLDGVSDR DYIIELISKF
     SIIMMHLSRL SEELILWSSS EFRFIQIGDA YSTGSSIMPQ KKNPDGAELI RGKIGRVYGD
     LISILTVMKS LPLAYNKDMQ EDKEPFFDAK DTVISCLKVM EGIISTLKVN KENLMKSVKK
     GFLNATEAAD YLVNKGMAFR DAHKVIGEVV IYCEDKNSAI EDLSLEELKQ FSDLFCEDIY
     EFIDYKNSIN KGIKKEMGYF