ARLY_THENN
ID ARLY_THENN Reviewed; 398 AA.
AC Q9Z4S3; B9K8S6;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 109.
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=CTN_1183;
OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=309803;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA Kim J.J., Park K.J., Lee S.Y.;
RT "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 115-398.
RX PubMed=10732680; DOI=10.1007/pl00008670;
RA Dimova D., Weigel P., Takahashi M., Marc F., Van Duyne G.D., Sakanyan V.;
RT "Thermostability, oligomerization and DNA-binding properties of the
RT regulatory protein ArgR from the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Mol. Gen. Genet. 263:119-130(2000).
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; CP000916; ACM23359.1; -; Genomic_DNA.
DR EMBL; AJ009897; CAB38108.1; -; Genomic_DNA.
DR RefSeq; WP_015919674.1; NC_011978.1.
DR AlphaFoldDB; Q9Z4S3; -.
DR SMR; Q9Z4S3; -.
DR STRING; 309803.CTN_1183; -.
DR EnsemblBacteria; ACM23359; ACM23359; CTN_1183.
DR KEGG; tna:CTN_1183; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_0_0; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000000445; 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; 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; 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..398
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137842"
FT CONFLICT 171
FT /note="G -> S (in Ref. 2; CAB38108)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 46000 MW; 381B0C7F5F4C0823 CRC64;
MSEKLWEKGY TVDEEVEKFT VGDDYIVDMR IIKYDIKASI VHSKMLQRTG LLTQEEQKKI
EEALNELLHL VEEGKFQIKP EDEDCHTAIE NFLVKKLGET GKKIHTARSR NDQVLTALRL
MYKDELKKIK DLVVELQKSL DGFIERFGQI KFAGFTHTRK AMPTDFATWA GALRDALQDD
LKLLETVYDI IDQSPLGTGA GYGVPIEVDR EFTAKELGFS RVQWNPIYTQ NSRGKFEYLL
LHVLSQISYD LNRFASDIIF FSLPEIGFLK LPKELCTGSS IMPHKINPDP LELVRAYHHF
VVSRMVMAVS LPSNLILGYH RDLQLLKKPV IESIDVVKNI LRIMKIIFDR IEVDREKSED
SITEEVLATH RVYELVKKGI PFRDAYRMVA EKYGREKD