ID   ARLY_XANC5              Reviewed;         432 AA.
AC   Q3BSI8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=XCV2544;
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10;
RX   PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   genome sequence.";
RL   J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ24221.1; -; Genomic_DNA.
DR   RefSeq; WP_011347702.1; NZ_CP017190.1.
DR   AlphaFoldDB; Q3BSI8; -.
DR   SMR; Q3BSI8; -.
DR   STRING; 456327.BJD11_10180; -.
DR   EnsemblBacteria; CAJ24221; CAJ24221; XCV2544.
DR   GeneID; 63991573; -.
DR   KEGG; xcv:XCV2544; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_0_6; -.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000007069; 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   Gene3D; 1.10.275.10; -; 1.
DR   HAMAP; MF_00006; Arg_succ_lyase; 1.
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; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase.
FT   CHAIN           1..432
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000089127"
SQ   SEQUENCE   432 AA;  46367 MW;  D41BBB452E9D105E CRC64;
     MTNLLWQKPG VAVDAKIQSF LAGDDVILDR EFFLYDIAAS KAHAQGLQHI GILSLQELGG
     LSEQLDLLAA DFRSGAFVLD AQYEDCHSAI EARLTERLGD AGRKIHTGRS RNDQILVATR
     LWLKDKLQRV ATLSAEIAKV ALDRAQAEAG LPVPGYTHIQ RAVVSSAGMW WAGWAEAFID
     NAVRADDTVR LVDSNPLGTA AGYGVNLPLD RAHTTAELGF ARLLVSPIYA QLSRGKYELA
     ALEALGSATL DLRRIAWDLS LFTSGEFAFV ALPAQYTTGS SIMPNKRNPD VIELMRATHA
     SVAAARTEIE QLLSLPSGYH RDLQSSKGAI VHGFGRGLAA LELLPALLAN LEWRPDKLRA
     AIDSGMYATD VAVEAAVAGV PFREAYKAAA QAAETAGQGR TPEGSLAARV SPGAAADLQL
     DVLQARWQAL RA