ID   ARLY_MYCA1              Reviewed;         472 AA.
AC   A0QHA7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-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}; OrderedLocusNames=MAV_3111;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) 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; CP000479; ABK64487.1; -; Genomic_DNA.
DR   RefSeq; WP_011725264.1; NC_008595.1.
DR   AlphaFoldDB; A0QHA7; -.
DR   SMR; A0QHA7; -.
DR   EnsemblBacteria; ABK64487; ABK64487; MAV_3111.
DR   KEGG; mav:MAV_3111; -.
DR   HOGENOM; CLU_027272_2_2_11; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001574; 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..472
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000000504"
SQ   SEQUENCE   472 AA;  49739 MW;  E3508731CC432B73 CRC64;
     MSTREGSLWG GRFADGPSDA LAALSKSTHF DWVLAPYDIV ASRAHTVILY RAGLLSEEQR
     DGLLAGLDSL AEDVADGSFT PLVTDEDVHA ALERGLIDRV GPDLGGRLRA GRSRNDQVAT
     LFRMWLRDAV RRVAAGALDV VGALVAQAAA HPEAIMPGKT HLQSAQPVLL AHHLLAHAHP
     LLRDVDRIVD FDKRAAVSPY GSGALAGSSL GLDPDAIAAE LGFASAADNS IDATASRDFA
     AEAAFVFAMI GVDLSRLAED VILWSSTEFG YVKLHDAWST GSSIMPQKKN PDIAELARGK
     SGRLIGNLAG LLATLKAQPL AYNRDLQEDK EPVFDAVAQL ELVLPAMAGL VGSLTFDVQR
     MAALAPAGYT LATDIAEWLV RQGVPFRSAH EAAGAAVRAA EQRAVGLDEL TDDELAAISP
     ALTPQVREVL TIEGSVSSRD ARGGTAPARV VEQIDTVAAT AARLRERLGG PA