ID   ARLY_BACC4              Reviewed;         462 AA.
AC   B7H6Y4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=BCB4264_A4737;
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus B4264.";
RL   Submitted (OCT-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};
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; CP001176; ACK64015.1; -; Genomic_DNA.
DR   RefSeq; WP_000041293.1; NC_011725.1.
DR   AlphaFoldDB; B7H6Y4; -.
DR   SMR; B7H6Y4; -.
DR   EnsemblBacteria; ACK64015; ACK64015; BCB4264_A4737.
DR   KEGG; bcb:BCB4264_A4737; -.
DR   HOGENOM; CLU_027272_2_3_9; -.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000007096; 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..462
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000116198"
SQ   SEQUENCE   462 AA;  52190 MW;  6813F7B0AE03D4E2 CRC64;
     MSKLWGGRFT EEAEAWVEEF GASISFDQQL VNQDINGSMA HVTMLAKQGI VTQEEAEKIK
     IGLQYLLKEA KENKLQFSVE AEDIHLNIEK MLIEQIGEVG GKLHTGRSRN DQVATDMHLY
     LKEKVEHIIK ATKQLQTVLV HQAENNIETI MPGYTHLQRA QPISFAHHIL AYFWMLERDV
     NRYEDSLKRI NISPLGAGAL AGTTFPIDRE YSAELLGFNG IYENSLDAVS DRDFILEFLS
     NSSMLMMHLS RFCEELILWS SQEFQFIEMS DQYATGSSIM PQKKNPDMAE LIRGKTGRVY
     GNLFSLLTVM KGLPLAYNKD LQEDKEGMFD TVKTVEGCLH IMAGMLETMT VNKEKMGQAV
     TQDFSNATEI ADYLANKGLP FRQAHEIVGK LVLYCTQKGI YLLDVSLETY KEMSSLFEED
     LYEVLSPYAA VKRRNSAGGT GFEQIKNALE KAKGLTKEVI KG