ID   ARLY_GLUOX              Reviewed;         481 AA.
AC   Q5FPK5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=GOX1955;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(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; CP000009; AAW61691.1; -; Genomic_DNA.
DR   RefSeq; WP_011253468.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FPK5; -.
DR   SMR; Q5FPK5; -.
DR   STRING; 290633.GOX1955; -.
DR   EnsemblBacteria; AAW61691; AAW61691; GOX1955.
DR   KEGG; gox:GOX1955; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_5; -.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000006375; 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..481
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000240733"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   481 AA;  52162 MW;  A9D8778EFEE0F05F CRC64;
     MKNAPVDTQS DAATSFEGTA ANPQWGGRFA SGPAAIMGEI NASIGFDKIL WRQDIRGSLA
     HAAMLQKVGL LTETELAEIR QGLGDIAQEI GEGRFEFSPA LEDIHMNIEA RLSERIGEAG
     KRLHTARSRN DQVATDFRLW VRDAIDGLQE QTASLMRSLA TRALEHAATP MPGFTHLQVA
     QPVTFGHHLL AYVEMLSRDR GRLRDARARL NECPLGSAAL AGTSFPIDRR MTAAALDFDR
     PTANSLDAVS DRDFALEFLS ALSLQAMHLS RLAEEIVMWA SAPFGFITLS DAFTTGSSIM
     PQKRNPDAAE LVRAKIGRIM GDFVGLLTVM KGLPLAYAKD TQEDKEPVFD ATEAMTLSLA
     AMDGMIRDLK ANTTRMRAVA GMGFSTATDL ADWLVRELRV PFRTAHHVTG RLVGMAEQKG
     CDLADLSLEE MQSVEPQINA GVFDVLTVEA SLASRTSEGG TAPANVKHQA ESWLAKLGET
     A