ID   ARLY_STRM5              Reviewed;         431 AA.
AC   B4SQ92;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Smal_2723;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA   Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) 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; CP001111; ACF52423.1; -; Genomic_DNA.
DR   RefSeq; WP_012511640.1; NC_011071.1.
DR   AlphaFoldDB; B4SQ92; -.
DR   SMR; B4SQ92; -.
DR   STRING; 391008.Smal_2723; -.
DR   EnsemblBacteria; ACF52423; ACF52423; Smal_2723.
DR   KEGG; smt:Smal_2723; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_0_6; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   BioCyc; SMAL391008:SMAL_RS13850-MON; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001867; 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   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..431
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000089120"
SQ   SEQUENCE   431 AA;  46486 MW;  63286E58CEBB20D9 CRC64;
     MADLLWQKPG VAVDAKIQTF LAGDDVILDR EFFLHDIAAS AAHAQGLQHI GILSADELAG
     LLRELDVLAQ DFRAGRFVLD TQYEDGHSAI EARLTERLGD AGRKIHTGRS RNDQILVATR
     LWLKEKLQRV AQLSAEVAKV ALDRAQAEKD LPIPGYTHIQ RAVVSSAGMW WAGWAEAFID
     NAIRARDTHA LVDANPLGTA AGYGVNLPLD REHTTAALGF ARMQISPIYA QLSRGKFELA
     ALEALGAATL DLRRIAWDLS LFTSAEFGFV ALPAQYTTGS SIMPNKRNPD VIELMRATHA
     SVAAARTEIE QLLSLPSGYH RDLQSSKGAI FHGFGRGLAA LELLPSLLAN LEWRDDKLRA
     AIDSGMYATD VAVEAAVAGV PFREAYKAAA AGADSAGQGR TPEGSLAARV SPGSAADLRL
     DELRARWQAL S