ARLY_CAMJD
ID ARLY_CAMJD Reviewed; 460 AA.
AC A7H3C0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=JJD26997_0883;
OS Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS 269.97).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT isolated from human blood.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000768; ABS43921.1; -; Genomic_DNA.
DR AlphaFoldDB; A7H3C0; -.
DR SMR; A7H3C0; -.
DR EnsemblBacteria; ABS43921; ABS43921; JJD26997_0883.
DR KEGG; cjd:JJD26997_0883; -.
DR HOGENOM; CLU_027272_2_3_7; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000002302; 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..460
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000000464"
SQ SEQUENCE 460 AA; 51787 MW; 150C95D7766DFA28 CRC64;
MKNEMWSGRF SGASDELLKE FNASLNVDKT LFNEDIQGSI AHATMLESCG ILKKEELDAI
VKGLEQVRSE IEQGKFIFDI KDEDIHMAIE KRLSEIIGSE IGGRLHTARS RNDQVATDFK
LFVKKSHIEL IKLLKELIQT MLEHAKVHKK TIMPSFTHLQ HAQPVSFSFY ILAYAFMLMR
DVKRLQNSLE LAGFSPLGSC ACAGTSYATN RELSAKILGF KDIMPNAMDG VSDRDFVLDL
LYDIAVIFTH TSRLCEEMIL FSSSEFSFIT ISDSFSTGSS IMPQKKNPDV CELIRGKTGR
VYGNLISLLT IMKALPLAYN KDMQEDKEGL FDSVKTAKDS LIILNVMLKE IRINKENMLN
ACKKGHLLAT DLADYLVREK NIPFRKAHFI VGNVVAQAEV QGIDISEIKD LSKIDPIFDE
KAMELLNFEF SLNSKQSEGS SSIASVEKQI QILQEFIKKL
