ARLY_PYRIL
ID ARLY_PYRIL Reviewed; 429 AA.
AC A1RR78;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-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}; OrderedLocusNames=Pisl_0281;
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) 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; CP000504; ABL87460.1; -; Genomic_DNA.
DR RefSeq; WP_011762037.1; NC_008701.1.
DR AlphaFoldDB; A1RR78; -.
DR SMR; A1RR78; -.
DR STRING; 384616.Pisl_0281; -.
DR EnsemblBacteria; ABL87460; ABL87460; Pisl_0281.
DR GeneID; 4616786; -.
DR KEGG; pis:Pisl_0281; -.
DR eggNOG; arCOG01748; Archaea.
DR HOGENOM; CLU_027272_2_0_2; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 51806at2157; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000002595; 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 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.
FT CHAIN 1..429
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000089106"
SQ SEQUENCE 429 AA; 47481 MW; 30644D6F08D9B740 CRC64;
MSFYRSWIGE EGELIKRYTS SIKDDVEIAE EVIKVMEAHV KHLAEVGIMP KEAADAILKT
LKEATPEQLL SSEFEDIHEA LEKWLIDRLG EETAGWVGLG RSRNDHVAAA IRLAALRKAS
ALRKNVEKMR CILAKKALEY ADCAMPSFTH FQPAQAITFG HYLLAVDELA AEFLHVLKAV
EKLLKRSPLG AGPAGGTRTP IDRERLAKLA GFEDVVENAL YASGSRFFAL ALASAVVSFL
TELSRTVDDL IRWNSPLVGY VAAPDSHVST SSIMPHKRNL VTLEVFRARA AEALGHLTAL
NAVVMKIGLG YSLDLQEATR HLWAVLNMAT EGVEIFIDFL EKMSFNCVKA REDAERYHST
SSDTAETIAL SGVPFRKAYF QLAKEIKEGT ARLMSIEEAL QRPTRGSANP EEVKKAASTR
LVFCREKPL
