ID   ARLY_TREPR              Reviewed;         452 AA.
AC   Q8KTQ9;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 79.
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};
OS   Tremblaya princeps.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Candidatus Tremblaya.
OX   NCBI_TaxID=189385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12088995; DOI=10.1128/aem.68.7.3198-3205.2002;
RA   Baumann L., Thao M.L., Hess J.M., Johnson M.W., Baumann P.;
RT   "The genetic properties of the primary endosymbionts of mealybugs differ
RT   from those of other endosymbionts of plant sap-sucking insects.";
RL   Appl. Environ. Microbiol. 68:3198-3205(2002).
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; AF481102; AAM75989.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KTQ9; -.
DR   SMR; Q8KTQ9; -.
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..452
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000137755"
FT   REGION          431..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   452 AA;  48814 MW;  4364C3EBA945DE00 CRC64;
     MWSGRFSSPV CAPVQSFTAS VGFDRAMCHC DAAVLAAHCR SLYLRRVMSI ADLADVERGL
     SEVAMGARAG AISWRPELED VHRNVEHVLT ELVGKAGRMA HTGKSRNDQV STTARVWLRH
     MAGAAICRVE ELERALAARS RACLNTMMPG LTHMQVAQPV TAAHYLTAYR CMLSRDRSRL
     VRCTRGACVL TLGSGALAGT NHGGDRYTTA DMLGLHCVSP NSLDAVSDRD FVMEYALCCA
     VLMVHMSRLA EDMIAWSSSI VGFAVLGDAL CTGSSIMPQK KNPDILELVR AKAAVLIGGA
     MGIMAVMKAQ GLAYNRDNQE DKAVLLGASR AVTRSLSVMA LAVRSLRLNK SRLRRRLESS
     FAIATDLADS LVWHGMTFRD SHEAVARAVG VAIRAGHAGL RALPLCSRGV VPPLLAARLA
     RIAQPDARVS AFRKDSTGST SPKWSFRAMR RA