ID   ARLY2_ALKCK             Reviewed;         462 AA.
AC   Q5WED9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Argininosuccinate lyase 2 {ECO:0000255|HAMAP-Rule:MF_00006};
DE            Short=ASAL 2 {ECO:0000255|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE   AltName: Full=Arginosuccinase 2 {ECO:0000255|HAMAP-Rule:MF_00006};
GN   Name=argH2 {ECO:0000255|HAMAP-Rule:MF_00006}; OrderedLocusNames=ABC2736;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) 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; AP006627; BAD65271.1; -; Genomic_DNA.
DR   RefSeq; WP_011247579.1; NC_006582.1.
DR   AlphaFoldDB; Q5WED9; -.
DR   SMR; Q5WED9; -.
DR   STRING; 66692.ABC2736; -.
DR   EnsemblBacteria; BAD65271; BAD65271; ABC2736.
DR   KEGG; bcl:ABC2736; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_9; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001168; 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;
KW   Reference proteome.
FT   CHAIN           1..462
FT                   /note="Argininosuccinate lyase 2"
FT                   /id="PRO_0000240713"
SQ   SEQUENCE   462 AA;  51026 MW;  477E236E219BC471 CRC64;
     MSKLWGGRFT KTAEQWVDEF GASIGFDQQL VEEDITGSIA HVTMLAKQHI LSEEEAAQIK
     NGLKTLQKKA AAGELVFSAA QEDIHLNLEK LLIDEIGPVG GKLHTGRSRN DQVATDMHLY
     LRTQTEEIME AIRTLQAALV KQAEGHVETL IPGYTHLQRA QPVSFAHHLL AYFWMLERDY
     GRLQDSLKRV NISPLGAGAL AGTTFPIDRA YTAELLHFEG IYENSLDAVS DRDFIVEFLA
     ASATLMMHLS RLCEELILWS AQEFQFIEID DAFATGSSIM PQKKNPDMAE LIRGKTGRVY
     GSLFSLLTTL KGLPLAYNKD MQEDKEGMFD TVKTVKGSLR IFAGMIETIT VNTDAMAKAV
     TSDFSNATEL ADYLATKGMP FREAHEVVGK LVLTAIEKGV YLLDLPIEVY KEASSLFADD
     IYEVLQPKTV VGRRNSAGGT GFEQVKLALG KANDLLSQSI KG