ID ARLY_PSEAE Reviewed; 464 AA.
AC P50987; Q9HTT6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 27-MAR-2024, entry version 148.
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=PA5263;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-243.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Whitchurch C.B., Alm R.A., Mattick J.S.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-241.
RX PubMed=2121708; DOI=10.1128/jb.172.11.6252-6260.1990;
RA Mohr C.D., Deretic V.;
RT "Gene-scrambling mutagenesis: generation and analysis of insertional
RT mutations in the alginate regulatory region of Pseudomonas aeruginosa.";
RL J. Bacteriol. 172:6252-6260(1990).
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; AE004091; AAG08648.1; -; Genomic_DNA.
DR EMBL; L48729; AAA88425.1; -; Genomic_DNA.
DR EMBL; M61001; AAA25721.1; -; Genomic_DNA.
DR PIR; A37143; A37143.
DR PIR; E82989; E82989.
DR RefSeq; NP_253950.1; NC_002516.2.
DR RefSeq; WP_003114030.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; P50987; -.
DR SMR; P50987; -.
DR STRING; 208964.PA5263; -.
DR PaxDb; 208964-PA5263; -.
DR GeneID; 879636; -.
DR KEGG; pae:PA5263; -.
DR PATRIC; fig|208964.12.peg.5516; -.
DR PseudoCAP; PA5263; -.
DR HOGENOM; CLU_027272_2_3_6; -.
DR InParanoid; P50987; -.
DR OrthoDB; 9769623at2; -.
DR PhylomeDB; P50987; -.
DR BioCyc; PAER208964:G1FZ6-5384-MONOMER; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IBA:GO_Central.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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 NCBIfam; TIGR00838; argH; 1.
DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 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..464
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137806"
FT CONFLICT 6..7
FT /note="TN -> PY (in Ref. 2; AAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 11..37
FT /note="GGRFSEPVDAFVARFTASVDFDKRLYR -> VDPLQASPSTPSSRRVRRQPS
FT TSTSVLYH (in Ref. 2; AAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="D -> E (in Ref. 2; AAA88425)"
FT /evidence="ECO:0000305"
FT CONFLICT 189..220
FT /note="VDCRKRVNRMPLGSAALAGTTYPIQREITCQL -> RRLPQAGQPHAARLGG
FT PGRHHLPDPARRSPASC (in Ref. 2; AAA88425 and 3; AAA25721)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 51641 MW; BE16C2C3CFE423E9 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 RAAVARGRKL LAQR
//
