ID   ARLY_AGRVS              Reviewed;         467 AA.
AC   B9JTJ2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=Avi_4017;
OS   Agrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis (strain
OS   S4)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=311402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4 / ATCC BAA-846;
RX   PubMed=19251847; DOI=10.1128/jb.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA   Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA   Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA   Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA   Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
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; CP000633; ACM37900.1; -; Genomic_DNA.
DR   RefSeq; WP_015917312.1; NC_011989.1.
DR   AlphaFoldDB; B9JTJ2; -.
DR   SMR; B9JTJ2; -.
DR   STRING; 311402.Avi_4017; -.
DR   EnsemblBacteria; ACM37900; ACM37900; Avi_4017.
DR   KEGG; avi:Avi_4017; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_5; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001596; Chromosome 1.
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..467
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000116302"
SQ   SEQUENCE   467 AA;  51148 MW;  062313176B862CC0 CRC64;
     MAEDTKDTTS SNQMWGGRFA SGPAAIMEEI NASIGFDKKL YAQDIRGSIA HATMLAHQGI
     ISGEDKDKIV TGLNTILSEI EAGQFTFSRK LEDIHMNIEA RLADLIGPAA GRLHTARSRN
     DQVALDFRLW VKEELQKAES LLTDLIAAFL DRAEEHAETV MPGFTHLQTA QPVTFGHHCM
     AYVEMFGRDR QRVRHAIEHL DESPIGAAAL AGTGYAIDRH MTAKALGFRE PTRNSIDTVS
     DRDFALEFLS IAAISAVHLS RLAEEIVIWS TPQFGFIRLS DAFSTGSSIM PQKKNPDAAE
     LVRAKTGRIN GSLIALLTIM KGLPLAYSKD MQEDKEQVFD AAESLELALA AMTGMIRDMT
     VRADRMKAAA GSGFSTATDL ADWLVREAGL PFRDAHHVTG RVVALAEEKG CDLADLPLED
     LQAIHTAITA DIYSVLTVEA SVASRKSYGG TAPDEVRKQI KWWRGRN