ID   ARLY_MYCTA              Reviewed;         470 AA.
AC   A5U316;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=MRA_1670;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ73416.1; -; Genomic_DNA.
DR   RefSeq; WP_003408180.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U316; -.
DR   SMR; A5U316; -.
DR   STRING; 419947.MRA_1670; -.
DR   EnsemblBacteria; ABQ73416; ABQ73416; MRA_1670.
DR   KEGG; mra:MRA_1670; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_2_11; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001988; 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..470
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000000510"
SQ   SEQUENCE   470 AA;  49774 MW;  1844ED923D797ECE CRC64;
     MSTNEGSLWG GRFAGGPSDA LAALSKSTHF DWVLAPYDLT ASRAHTMVLF RAGLLTEEQR
     DGLLAGLDSL AQDVADGSFG PLVTDEDVHA ALERGLIDRV GPDLGGRLRA GRSRNDQVAA
     LFRMWLRDAV RRVATGVLDV VGALAEQAAA HPSAIMPGKT HLQSAQPILL AHHLLAHAHP
     LLRDLDRIVD FDKRAAVSPY GSGALAGSSL GLDPDAIAAD LGFSAAADNS VDATAARDFA
     AEAAFVFAMI AVDLSRLAED IIVWSSTEFG YVTLHDSWST GSSIMPQKKN PDIAELARGK
     SGRLIGNLAG LLATLKAQPL AYNRDLQEDK EPVFDSVAQL ELLLPAMAGL VASLTFNVQR
     MAELAPAGYT LATDLAEWLV RQGVPFRSAH EAAGAAVRAA EQRGVGLQEL TDDELAAISP
     ELTPQVREVL TIEGSVSARD CRGGTAPGRV AEQLNAIGEA AERLRRQLVR