ID   ARLY_STRMU              Reviewed;         460 AA.
AC   Q8DVX5;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=SMU_335;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58094.1; -; Genomic_DNA.
DR   RefSeq; NP_720788.1; NC_004350.2.
DR   RefSeq; WP_002262512.1; NC_004350.2.
DR   AlphaFoldDB; Q8DVX5; -.
DR   SMR; Q8DVX5; -.
DR   STRING; 210007.SMU_335; -.
DR   PRIDE; Q8DVX5; -.
DR   EnsemblBacteria; AAN58094; AAN58094; SMU_335.
DR   KEGG; smu:SMU_335; -.
DR   PATRIC; fig|210007.7.peg.290; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_9; -.
DR   OMA; KKNPDVF; -.
DR   PhylomeDB; Q8DVX5; -.
DR   BRENDA; 4.3.2.1; 5941.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000002512; 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..460
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000137834"
SQ   SEQUENCE   460 AA;  51500 MW;  E2FF4C0A3FDBB30A CRC64;
     MTTKNHKLWG GRFEAGLAQW VEEFGASISF DQKLAEFDLK GSIAHVTMLG EKGIISQEDA
     ATIKAGLEDL LEEYKAGQLK FDVSNEDIHM NMESLLTAKI GPVAGKLHTA RSRNDQVATD
     MHLYLKAKLD EVIEKLANLR TVLVDLADKH VHTIMPGYTH LQHAQPISFG HHLMAYYNMF
     TRDSERFIFN VKHTDLSPLG AAALAGTTFP IDREMTAQLM GFAEPYSNSL DAVSDRDFIL
     EFLSNASILM MHMSRMCEEV ISWCSHEYQF VTLSDTFSTG SSIMPQKKNP DMAELIRGKS
     GRVYANLFGL LTVMKALPLA YNKDLQEDKE GMFDTAETIT VALDILAGML SSMIVNDKHM
     AESTQKDFSN ATELADYLAS KGMPFRQAHE IVGKLILECS KNGHYLQDVP LERYQTISDL
     IEEDVYETLK SHTAVERRHS LGGTGFEQVK WQIAEAKKAL