ARLY_PSEAB
ID ARLY_PSEAB Reviewed; 464 AA.
AC Q02EA0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=PA14_69500;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ14647.1; -; Genomic_DNA.
DR RefSeq; WP_003141964.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02EA0; -.
DR SMR; Q02EA0; -.
DR PRIDE; Q02EA0; -.
DR EnsemblBacteria; ABJ14647; ABJ14647; PA14_69500.
DR KEGG; pau:PA14_69500; -.
DR HOGENOM; CLU_027272_2_3_6; -.
DR OMA; KKNPDVF; -.
DR BioCyc; PAER208963:G1G74-5854-MON; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000000653; 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.
FT CHAIN 1..464
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000000525"
SQ SEQUENCE 464 AA; 51641 MW; BE16C2C3CFF1C3E9 CRC64;
MSVEKTNQSW GGRFSEPVDA FVARFTASVD FDKRLYRHDI MGSIAHATML AKVGVLSDAE
RDAIVDGLQQ IQAEIEAGSF DWRVDLEDVH MNIEARLTDR IGVTGKKLHT GRSRNDQVAT
DIRLWLRDEI DTILAEITRL QEGLLGLAEA EADTIMPGFT HLQTAQPVTF GHHLLAWFEM
LGRDYERLVD CRKRVNRMPL GSAALAGTTY PIQREITCQL LGFDAVGGNS LDGVSDRDFA
IEFCAAASLA MMHLSRFSEE LVLWTSAQFQ FIDLPDRFCT GSSIMPQKKN PDVPELVRGK
SGRVFGALTG LLTLMKGQPL AYNKDNQEDK EPLFDAADTL RDSLRAFADM VPAIRPRREI
MREAARRGFS TATDLADYLV RKGLPFRDCH EIVGHAVKYG VDSGKDLAEM SLDELRRFSE
QIDADVFDVL TLEGSVNARD HIGGTAPNQV RAAVARGRQL LAQR
