ID   ARLY_PYRAE              Reviewed;         429 AA.
AC   Q8ZU95;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 110.
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=PAE2887;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64513.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZU95; -.
DR   SMR; Q8ZU95; -.
DR   STRING; 178306.PAE2887; -.
DR   EnsemblBacteria; AAL64513; AAL64513; PAE2887.
DR   KEGG; pai:PAE2887; -.
DR   PATRIC; fig|178306.9.peg.2158; -.
DR   eggNOG; arCOG01748; Archaea.
DR   HOGENOM; CLU_027272_2_0_2; -.
DR   InParanoid; Q8ZU95; -.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IBA:GO_Central.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
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;
KW   Reference proteome.
FT   CHAIN           1..429
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000137867"
SQ   SEQUENCE   429 AA;  47472 MW;  294D51EFB2BCA578 CRC64;
     MSFYRSWIGG TGDLVKKYTS SIKDDVELAE EVVRVMKGHV AHLVEIGSIP KEAGERIIKA
     LEEVDASELL KEEFEDVHEA LEKWLIDKLG EEIGGWVGLG RSRNDHVAAA IRLAALRKTE
     RLKEEACRLR CALAKRALEY ADCPMPSFTH FQPAQVITFG HYLLAIDELL AEFLHILRGV
     EDLLNRSPLG AGPAGGVRTP LDRRRLAELV GFKEVVENAL YASGSRFFAL ALASAVVSFL
     AELSRAVDDF IRWNSPVVGY VNSPDSHVST SSIMPHKRNL VTLEVLRARI AEALGHFAAM
     SALVMKVGMG YSLDLQEATR HLWAVLNIAT EGMAVFRDFI ENMAFNCEKS RKDAEAYFTT
     SSDTAEDEAL KGVPFRKAYF QLASAIKAGT ARLLTINEAL KRPVYGSANT EEVKRAASRR
     LALCRPKPL