ARLY_ECOLI
ID ARLY_ECOLI Reviewed; 457 AA.
AC P11447; Q2M8Q5; Q47060;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 3.
DT 03-AUG-2022, entry version 180.
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};
GN OrderedLocusNames=b3960, JW3932;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
RX PubMed=2851495; DOI=10.1016/0378-1119(88)90030-3;
RA Parsot C., Boyen A., Cohen G.N., Glansdorff N.;
RT "Nucleotide sequence of Escherichia coli argB and argC genes: comparison of
RT N-acetylglutamate kinase and N-acetylglutamate-gamma-semialdehyde
RT dehydrogenase with homologous and analogous enzymes.";
RL Gene 68:275-283(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
RC STRAIN=K12;
RX PubMed=6292860; DOI=10.1093/nar/10.19.5935;
RA Charlier D.R.M., Piette J., Glansdorff N.;
RT "IS3 can function as a mobile promoter in E. coli.";
RL Nucleic Acids Res. 10:5935-5948(1982).
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:0000305}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}.
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DR EMBL; U00006; AAC43066.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76942.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77351.1; -; Genomic_DNA.
DR EMBL; M21446; AAA23479.1; -; Genomic_DNA.
DR EMBL; J01590; AAB59147.1; -; Genomic_DNA.
DR PIR; C65203; C65203.
DR RefSeq; NP_418395.1; NC_000913.3.
DR RefSeq; WP_001230087.1; NZ_SSZK01000065.1.
DR PDB; 1TJ7; X-ray; 2.44 A; A/B=1-457.
DR PDBsum; 1TJ7; -.
DR AlphaFoldDB; P11447; -.
DR SMR; P11447; -.
DR BioGRID; 4263466; 10.
DR DIP; DIP-9142N; -.
DR STRING; 511145.b3960; -.
DR jPOST; P11447; -.
DR PaxDb; P11447; -.
DR PRIDE; P11447; -.
DR EnsemblBacteria; AAC76942; AAC76942; b3960.
DR EnsemblBacteria; BAE77351; BAE77351; BAE77351.
DR GeneID; 948463; -.
DR KEGG; ecj:JW3932; -.
DR KEGG; eco:b3960; -.
DR PATRIC; fig|1411691.4.peg.2745; -.
DR EchoBASE; EB1205; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_6; -.
DR InParanoid; P11447; -.
DR OMA; KKNPDVF; -.
DR PhylomeDB; P11447; -.
DR BioCyc; EcoCyc:ARGSUCCINLYA-MON; -.
DR BioCyc; MetaCyc:ARGSUCCINLYA-MON; -.
DR UniPathway; UPA00068; UER00114.
DR EvolutionaryTrace; P11447; -.
DR PRO; PR:P11447; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IDA:EcoCyc.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Lyase; Reference proteome.
FT CHAIN 1..457
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137768"
FT CONFLICT 28
FT /note="R -> G (in Ref. 5; AAB59147)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="W -> R (in Ref. 5; AAB59147)"
FT /evidence="ECO:0000305"
FT HELIX 14..20
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 30..46
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 52..71
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:1TJ7"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 109..144
FT /evidence="ECO:0007829|PDB:1TJ7"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:1TJ7"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:1TJ7"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 165..190
FT /evidence="ECO:0007829|PDB:1TJ7"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:1TJ7"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 233..259
FT /evidence="ECO:0007829|PDB:1TJ7"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 296..310
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 319..323
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 324..346
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 353..360
FT /evidence="ECO:0007829|PDB:1TJ7"
FT TURN 363..366
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 367..376
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 381..398
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:1TJ7"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 427..432
FT /evidence="ECO:0007829|PDB:1TJ7"
FT HELIX 442..456
FT /evidence="ECO:0007829|PDB:1TJ7"
SQ SEQUENCE 457 AA; 50318 MW; 0109EF31675B9717 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 PLEDLPLSEL QKFSQVIDED
VYPILSLQSC LDKRAAKGGV SPQQVAQAIA FAQARLG
