ARLY_CAMC5
ID ARLY_CAMC5 Reviewed; 467 AA.
AC A7GXA8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=Ccur92_05460; ORFNames=CCV52592_0522;
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92;
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 "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
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; CP000767; EAU00753.1; -; Genomic_DNA.
DR RefSeq; WP_011992025.1; NC_009715.2.
DR AlphaFoldDB; A7GXA8; -.
DR SMR; A7GXA8; -.
DR STRING; 360105.CCV52592_0522; -.
DR EnsemblBacteria; EAU00753; EAU00753; CCV52592_0522.
DR KEGG; ccv:CCV52592_0522; -.
DR HOGENOM; CLU_027272_2_3_7; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000006380; 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..467
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000321434"
SQ SEQUENCE 467 AA; 51497 MW; 9E9ADEF18CE90415 CRC64;
MQESLKKMWS GRFSGESSEL LEEFNASIGF DKNLYREDIA GSKAHAKMLG ACGILKPEEA
AAIVAGLDAV LAQIEEGKFE FKTADEDIHM AVEKRLSELI GSELGGRLHT ARSRNDQVAL
DFRLYVLRQN EQIARQIREF IATLTSLASA HLDTLMPGYT HLQHAQPVSL AYHLLAYAFM
FKRDFERFIS SHERNNLCPL GSAALAGTPH PIRRELVAQE LNFAGITQNA MDSVSDRDFA
LEILFNISVL MTHASRLCEE LILWSSQEFG FVTISDAYST GSSIMPQKKN PDVAELIRGK
TGRANGNLIA LLTTMKGLPL AYNKDMQEDK EGVFDSVRTA TSSLAILNAM MKEAKFNEQN
MLAATKKGHL SATDLADYLV REKNVPFRTA HFITGKAVAH AENLGVDLSE LDAAQLKSVD
ENLDENAVKF LNLHASKEAR TSAGGTANAS VRKQIEELES WLSKSGD
