ID   ARLY_BACAC              Reviewed;         462 AA.
AC   C3L913;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=BAMEG_4911;
OS   Bacillus anthracis (strain CDC 684 / NRRL 3495).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=568206;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 684 / NRRL 3495;
RA   Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C.,
RA   Sutton G., Sims D.;
RT   "Genome sequence of Bacillus anthracis str. CDC 684.";
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; CP001215; ACP16168.1; -; Genomic_DNA.
DR   RefSeq; WP_000041275.1; NC_012581.1.
DR   AlphaFoldDB; C3L913; -.
DR   SMR; C3L913; -.
DR   GeneID; 45024502; -.
DR   KEGG; bah:BAMEG_4911; -.
DR   HOGENOM; CLU_027272_2_3_9; -.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
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_1000116306"
SQ   SEQUENCE   462 AA;  52165 MW;  2BBACFDA26EBB4DA CRC64;
     MSKLWGGRFT EEAEAWVEEF GASISFDQQL VNQDINGSIA HVTMLAKQGI VTKEEAEKIK
     IGLQYLLEEA KQNKLHFSVE AEDIHLNIEK MLMEKIGEVG GKLHTGRSRN DQVATDMHLY
     LKEKVEHIIK AIKQLQTVLV 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 LVLHCTQKGI YLIDVPLATY KEMSALFEED
     LYEVLSPYAA VKRRNSAGGT GFEQIEKALE KAKGLTKEAI KN