ID   ARLY_CLAMS              Reviewed;         493 AA.
AC   B0RHD6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=CMS1237;
OS   Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS   / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=31964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1;
RX   PubMed=18192393; DOI=10.1128/jb.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(2008).
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; AM849034; CAQ01353.1; -; Genomic_DNA.
DR   RefSeq; WP_012298631.1; NZ_MZMN01000003.1.
DR   AlphaFoldDB; B0RHD6; -.
DR   SMR; B0RHD6; -.
DR   STRING; 31964.CMS1237; -.
DR   EnsemblBacteria; CAQ01353; CAQ01353; CMS1237.
DR   KEGG; cms:CMS1237; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_2_11; -.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001318; 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;
KW   Reference proteome.
FT   CHAIN           1..493
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000073841"
SQ   SEQUENCE   493 AA;  52529 MW;  8825D1F88C5D85A5 CRC64;
     MTESTDPSSR AGEAGALWGG RFAGGPSPEL VALSRSTHFD WQLAPYDIAG SRAHARALAA
     AGYLSDAERQ AMLQALDTLE DRVRSGALVA SEADEDVHGA LERGLMDIAG PDLGGKLRAG
     RSRNDQIATL VRMYLRDHAA VIHAMLVQLV DALAAQAEAA GGAIMPGRTH LQHAQPVLLA
     HHLLAHCWPL VRDLERLADW DARADVSPYG SGALAGSTLG LDASAVARDL GFARSSENSI
     DGTAARDVVA EFAFVLAQVG IDLSRLSEEI ILWNTREFGF VTLSDSFSTG SSIMPQKKNP
     DIAELARGKS GRLIGNLSGL LATLKGLPLA YNRDLQEDKE PVFDSVQTLE VLLPAFTGMI
     ATLRFDVDRM AELAPQGFSL ATDVAEWLVK HRVAFRDAHE ITGELVKLAE SRGVGLEDLS
     DDDLRAVSPH LVPEVREVLS IDGSVASRDG VGGTARVRVD EQRAELVRRV AELRARADAA
     AERRAAASAA ASA