ID   ARLY_PYRAR              Reviewed;         429 AA.
AC   A4WJI4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=Pars_0971;
OS   Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=340102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL   Submitted (APR-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; CP000660; ABP50551.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WJI4; -.
DR   SMR; A4WJI4; -.
DR   STRING; 340102.Pars_0971; -.
DR   EnsemblBacteria; ABP50551; ABP50551; Pars_0971.
DR   KEGG; pas:Pars_0971; -.
DR   HOGENOM; CLU_027272_2_0_2; -.
DR   OMA; KKNPDVF; -.
DR   PhylomeDB; A4WJI4; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000001567; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase.
FT   CHAIN           1..429
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000089104"
SQ   SEQUENCE   429 AA;  47299 MW;  6605B6CB087660CF CRC64;
     MSFYRSWIGG RGDLVQRYTS SIRDDAEIAE EVVKVMKAHV THLAEIGALR KEVADKIVAA
     LEEVDPTELL RGEFEDIHEA LEKWLIDKLG EDVGGWVGLA RSRNDHVAAA IRLAALKKVG
     ALREAAMRLR CALAARALEY ADCPMPSFTH FQPAQVVTFG HYLLAVDELV AEFLHVLAAA
     EDLAKRSPLG AGPAGGVRTP VDRRRLAELA GFKDVVENTL YASGGRFFAL ALASAVTSFL
     VELSRAVDDF IRWNNPLLGY VEAPPEHVST SSIMPHKRNL VTLEVLRARS EEAVGHYAAL
     SGVVAKVGLG YSLDLQEATR HLWDILNIAI EGVEVLADFV EKIKFNCEKG RRDAELYYAT
     SSDTAEERAL RGVPFRKAYF ELASEIREGK ARLLTVDEAL KRPVLGSANP EEVRKSASRR
     LALCRPKSF