ARLY_ECOL5
ID ARLY_ECOL5 Reviewed; 457 AA.
AC Q0TAA0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=ECP_4173;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(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; CP000247; ABG72129.1; -; Genomic_DNA.
DR RefSeq; WP_001230079.1; NC_008253.1.
DR AlphaFoldDB; Q0TAA0; -.
DR SMR; Q0TAA0; -.
DR STRING; 362663.ECP_4173; -.
DR PRIDE; Q0TAA0; -.
DR EnsemblBacteria; ABG72129; ABG72129; ECP_4173.
DR KEGG; ecp:ECP_4173; -.
DR HOGENOM; CLU_027272_2_3_6; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000009182; 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..457
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000000478"
SQ SEQUENCE 457 AA; 50234 MW; 83D7D020765B9715 CRC64;
MALWGGRFTQ AADQRFKQFN DSLRFDYRLA EQDIVGSVAW SKALVTVGVL TAEEQAQLEE
ALNVLLEDVR ARPQQILESD AEDIHSWVEG KLIDKVGQLG KKLHTGRSRN DQVATDLKLW
CKDTVSELLT ANRQLQSALV ETAQNNQDAV MPGYTHLQRA QPVTFAHWCL AYVEMLARDE
SRLQDALKRL DVSPLGCGAL AGTAYEIDRE QLAGWLGFAS ATRNSLDSVS DRDHVLELLS
AAAIGMVHLS RFAEDLIFFN TGEAGFVELS DRVTSGSSLM PQKKNPDALE LIRGKCGRVQ
GALTGMMMTL KGLPLAYNKD MQEDKEGLFD ALDTWLDCLH MAALVLDGIQ VKRPRCQEAA
QQGYANATEL ADYLVAKGVP FREAHHIVGE AVVEAIRQGK ALEDLPLSEL QKFSQVIGED
VYPILSLQSC LDKRAAKGGV SPQQVAQAIA FAQARLG
