ARLY_PYRFU
ID ARLY_PYRFU Reviewed; 459 AA.
AC Q8U483;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
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=PF0208;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL80332.1; -; Genomic_DNA.
DR RefSeq; WP_011011321.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U483; -.
DR SMR; Q8U483; -.
DR STRING; 186497.PF0208; -.
DR EnsemblBacteria; AAL80332; AAL80332; PF0208.
DR GeneID; 41711999; -.
DR KEGG; pfu:PF0208; -.
DR PATRIC; fig|186497.12.peg.216; -.
DR eggNOG; arCOG01748; Archaea.
DR HOGENOM; CLU_027272_2_0_2; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 51806at2157; -.
DR PhylomeDB; Q8U483; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001013; 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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase;
KW Reference proteome.
FT CHAIN 1..459
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137868"
FT REGION 440..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 51348 MW; 733C8CA5F847694D CRC64;
MYRKALLGST RLDILSYISS MEEDREIVEE VIECLIAHVK GLIHSKLIPE EEGEKILKAL
EELRASKEAL FSIEAEDIHE AIEIYLKEKL GKTGGYLPLG RSRNDHVVCA LRLKAKKALV
EEIGLILELR KALIKKAEEN VYTLMPLFTH LQPAQPSTFA HYLSAIIEEL EDITKILFSG
LGIVDKSSLG AGAIGGTSVL LDRGYMGGIL FSDIITNSLY ATSSRTFLLY SCFLSVLISI
ALSRIAEDFV IFSTPNFGYI KLPNEHLSTS SMMPQKKNPV TMEVARAWAG EAIGHLVAMM
SILKALPSGY NLDMQEVNKH AFALFSGTIK TLKIFVDAMK RVEVNKENMK KDCDIFPILA
TDYAEKIAMN TGRPYREVYM EVASIIGEHE STEKIYSELS SKYGISISLE EGIKKPVVGS
PNPEDVLEFL EKAKKNVEKD EKKLEELRQN ENRDNVYNP
