ARLY_CAMJE
ID ARLY_CAMJE Reviewed; 460 AA.
AC Q46104; Q0P9W8; Q9PP02;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 132.
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=Cj0931c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43431 / TGH 9011 / Serotype O:3;
RX PubMed=8144452; DOI=10.1128/jb.176.7.1865-1871.1994;
RA Hani E.K., Chan V.L.;
RT "Cloning, characterization, and nucleotide sequence analysis of the argH
RT gene from Campylobacter jejuni TGH9011 encoding argininosuccinate lyase.";
RL J. Bacteriol. 176:1865-1871(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M77188; AAA93048.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL35051.1; -; Genomic_DNA.
DR PIR; B81367; B81367.
DR RefSeq; WP_010891895.1; NC_002163.1.
DR RefSeq; YP_002344329.1; NC_002163.1.
DR AlphaFoldDB; Q46104; -.
DR SMR; Q46104; -.
DR IntAct; Q46104; 24.
DR STRING; 192222.Cj0931c; -.
DR PaxDb; Q46104; -.
DR PRIDE; Q46104; -.
DR EnsemblBacteria; CAL35051; CAL35051; Cj0931c.
DR GeneID; 905111; -.
DR KEGG; cje:Cj0931c; -.
DR PATRIC; fig|192222.6.peg.915; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_7; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000000799; 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;
KW Reference proteome.
FT CHAIN 1..460
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137753"
FT CONFLICT 12
FT /note="G -> D (in Ref. 1; AAA93048)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="E -> Q (in Ref. 1; AAA93048)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="L -> F (in Ref. 1; AAA93048)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..209
FT /note="AI -> RT (in Ref. 1; AAA93048)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="K -> E (in Ref. 1; AAA93048)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="P -> L (in Ref. 1; AAA93048)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="P -> F (in Ref. 1; AAA93048)"
FT /evidence="ECO:0000305"
FT CONFLICT 387..391
FT /note="AHFIV -> HIYS (in Ref. 1; AAA93048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 51660 MW; 66DA10A252B54249 CRC64;
MKNEMWSGRF SGASDELLKE FNASLNVDKT LFNEDIQGSI AHATMLESCG ILKKEELDAI
IKGLEQVRSE IEQGKFIFDI KDEDIHMAVE KRLSEIIGSE IGGRLHTARS RNDQVATDFK
LFVKKSHIEL IKLLKELIQT MLEHAKVHKK TIMPSFTHLQ HAQPVSFSFY ILAYAFMLMR
DIKRLQNSLE LADFSPLGSC ACAGTSYAIN RELSAKILGF KDIMPNAMDG VSDRDFALDL
LYDIAVIFTH TSRLCEEMIL FSSSEFSFIT ISDSFSTGSS IMPQKKNPDV CELIRGKTGR
VYGNLISLLT IMKALPLAYN KDMQEDKEGI FDSVKTAKDS LIILNAMLKE IQINKENMLN
ACKKGHLLAT DLADYLVREK NIPFRKAHFI VGNVVAQAEA QGIDISEIKD LSKIDPVFDE
KAMELLNFEF SLNSKQSEGS SSIASVEKQI QILEGFIQNL
