ARLY_SULAC
ID ARLY_SULAC Reviewed; 447 AA.
AC Q4J8F0;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=Saci_1618;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY80930.1; -; Genomic_DNA.
DR RefSeq; WP_011278432.1; NC_007181.1.
DR AlphaFoldDB; Q4J8F0; -.
DR SMR; Q4J8F0; -.
DR STRING; 330779.Saci_1618; -.
DR EnsemblBacteria; AAY80930; AAY80930; Saci_1618.
DR GeneID; 3474174; -.
DR KEGG; sai:Saci_1618; -.
DR PATRIC; fig|330779.12.peg.1557; -.
DR eggNOG; arCOG01748; Archaea.
DR HOGENOM; CLU_027272_2_3_2; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001018; 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..447
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137869"
SQ SEQUENCE 447 AA; 50950 MW; 625CB2F3BA19CE4C CRC64;
MLYRRWGSDK DFVISYTSSN ESDKEIVEEV KLTLKAHVIE LYLSNYISKD TAKKIIRAIN
SFKDYPSSGY EDVHEALEDY IIKNIGEEGG WVGLGRSRND HVATALRLRT REYIFDIMEE
LYLLRKSLIE QAKKNLNTIM PSYTHFQPAQ PTTLAHYFMY LEEELNTPWE ALFNSLKLIN
RSPLGSGAIV GSNVKIDRKR EAELLGFDDV LYNTISSTSS RIDFINAISS LTLLMLVLSR
FAEDMILLSS MFVNIIKLPD SHVSTSSLMP QKRNSVTMEI LRTKVGECYG DLSSLMMIYK
GLPSGYNLDL QEMNKHYWNC IKHVIPSIHI TRDIIQNIQI KNFGEIQGLT ATDLAEEMAI
SGIPYRKAYI DVANKIKAGT FVAGISYTKS IENKKVIGSP NPSLLTQEIE IKEKRLNNQH
EKFKQYKESV IEKMGQLGVI EDGLLQQ
