ID   ARLY_CAMJJ              Reviewed;         460 AA.
AC   A1VZR4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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};
GN   OrderedLocusNames=CJJ81176_0938;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-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; CP000538; EAQ71890.1; -; Genomic_DNA.
DR   RefSeq; WP_002869160.1; NC_008787.1.
DR   AlphaFoldDB; A1VZR4; -.
DR   SMR; A1VZR4; -.
DR   STRING; 354242.CJJ81176_0938; -.
DR   EnsemblBacteria; EAQ71890; EAQ71890; CJJ81176_0938.
DR   KEGG; cjj:CJJ81176_0938; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_7; -.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000000646; 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..460
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000000465"
SQ   SEQUENCE   460 AA;  51734 MW;  1DC37C0A8918D618 CRC64;
     MKNEMWSGRF SSASDELLKE FNASLNVDKT LFNEDIQGSI AHATMLESCG ILKKEELDAI
     IKGLEQVKSE IEQGKFVFDI KDEDIHMAIE KRLSEIIGSE IGGRLHTARS RNDQVATDFK
     LFVKKSHIEL IKLLKELIQT MLEYAKVHKK TIMPSFTHLQ HAQPVSFSFY ILAYAFMLMR
     DVKRLQNSLE LADFLPLGSC ACAGTSYATN RELSAKILGF KDIMPNAMDG VSDRDFALDL
     LYDIAVIFTH TSRLCEEMIL FSSSEFSFIT ISDSFSTGSS IMPQKKNPDV CELIRGKTGR
     VYGNLISLLT IMKALPLAYN KDMQEDKEGI FDSVKTAKDS LIILNAMLKE IQINKENMLN
     ACKKGHMLAT DLADYLVREK NIPFRKAHFI VGNVVAQAEV QGIDISEIKD LSKIDPVFDE
     KAMELLNFEF SLNSKQSEGS SSIASVEKQI QILEGFIQNL