ID   ARLY_RHOFA              Reviewed;         505 AA.
AC   Q93JQ9;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, 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}; Synonyms=attA;
OS   Rhodococcus fascians.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1828;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D188;
RX   PubMed=11679063; DOI=10.1046/j.1365-2958.2001.02615.x;
RA   Maes T., Vereecke D., Ritsema T., Cornelis K., Thu H.N., Van Montagu M.,
RA   Holsters M., Goethals K.;
RT   "The att locus of Rhodococcus fascians strain D188 is essential for full
RT   virulence on tobacco through the production of an autoregulatory
RT   compound.";
RL   Mol. Microbiol. 42:13-28(2001).
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; AJ311775; CAC43335.1; -; Genomic_DNA.
DR   RefSeq; YP_007878693.1; NC_021080.1.
DR   AlphaFoldDB; Q93JQ9; -.
DR   SMR; Q93JQ9; -.
DR   STRING; 1443905.GCA_000761075_00051; -.
DR   eggNOG; COG0165; Bacteria.
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..505
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000137815"
SQ   SEQUENCE   505 AA;  55561 MW;  97DF7B41E357A922 CRC64;
     MSEKLWGGRF STDITDDVLR YTETASVDSR MLEHDLWQNI AHVLMLGRAG INTEPDTKAL
     LAGLLDMESS RADGGLQLDV RQEDVHLNTE FMLIERIGPV GGRMHTARSR NDQVQTDARM
     VTREWLLDAS EELLMFVQDL LGCPESEREA VLPGYTHSQA AQPISVAFWK AAHAQALLRD
     ASRLMDAWKR ININPLGACA LAGTTFALDR DYTSRLLGFD APMVNALDAT STRDWTVEVA
     GAAASGAVNL SRMQEEIVTW SSNEYALAEV HDSFATGSSI MPQKKNPVVA ELARGKSGRA
     VGALVQLLVM EKSVGLGYSC DLQEDKPVYW GALDTYLDTI RLCRRQNLHT AFDGARGRAL
     CWDNFSTATE IANILVSRFD VPFRTAHRIT GDLVNAALGG GHTLRNVAFT TTFLREEHDI
     DISEVDMKQI CDPLHTLRSY ISAGSTGPTR VSEQQEQGLA DVTDRLAEIR QARTRLWEAK
     AECLRAARSV VGGVSVPELA MEVGV