ID   ARLY_YERPB              Reviewed;         457 AA.
AC   B2JZE4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-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=YPTS_0118;
OS   Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB1/+;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL   Submitted (APR-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; CP001048; ACC87117.1; -; Genomic_DNA.
DR   RefSeq; WP_011191469.1; NZ_CP009780.1.
DR   AlphaFoldDB; B2JZE4; -.
DR   SMR; B2JZE4; -.
DR   GeneID; 66843495; -.
DR   KEGG; ypb:YPTS_0118; -.
DR   PATRIC; fig|502801.10.peg.3795; -.
DR   OMA; KKNPDVF; -.
DR   BioCyc; YPSE502801:YPTS_RS00590-MON; -.
DR   UniPathway; UPA00068; UER00114.
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..457
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000089133"
SQ   SEQUENCE   457 AA;  50099 MW;  939A81896A427A09 CRC64;
     MALWGGRFSQ AADQRFKQFN DSLRFDYRLA EQDIIGSVAW SKALVTVGVL NADEQQQLEQ
     ALSVLLEEVQ ANPHAILASD AEDIHSWVET KLIDKVGDLG KKLHTGRSRN DQVATDLKLW
     CKFQITELQT AVQQLQQALV MTAEANQDAV MPGYTHLQRA QPVTFAHWCL AYVEMLSRDE
     SRLQDTLKRL DVSPLGCGAL AGTAYAIDRE QLAGWLGFAS ATRNSLDSVS DRDHVLELLS
     DASIGMVHLS RFAEDLIFFN SGEAAFVDLS DRVTSGSSLM PQKKNPDALE LIRGKCGRVQ
     GALTGMTMTL KGLPLAYNKD MQEDKEGLFD ALNTWLDCLH MAALVLDGIQ VKRPRCKEAA
     EQGYANATEL ADYLVAKGVP FREAHHIVGE AVVEAIRQGK ALEALALSDL QQFSSVIGDD
     VYPILALQSC LDKRVAKGGV SPQQVASAIA EAKARLF