ID   ARLY_METM7              Reviewed;         481 AA.
AC   A6VI01;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=MmarC7_1010;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-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; CP000745; ABR66077.1; -; Genomic_DNA.
DR   RefSeq; WP_011977390.1; NC_009637.1.
DR   AlphaFoldDB; A6VI01; -.
DR   SMR; A6VI01; -.
DR   STRING; 426368.MmarC7_1010; -.
DR   EnsemblBacteria; ABR66077; ABR66077; MmarC7_1010.
DR   GeneID; 5328479; -.
DR   KEGG; mmz:MmarC7_1010; -.
DR   eggNOG; arCOG01748; Archaea.
DR   HOGENOM; CLU_027272_2_3_2; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 51806at2157; -.
DR   UniPathway; UPA00068; UER00114.
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; IPR029419; Arg_succ_lyase_C.
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; PF14698; ASL_C2; 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..481
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000000501"
SQ   SEQUENCE   481 AA;  54274 MW;  C12B19FA5786D925 CRC64;
     MNILRRGRLG SNVKEDVMKF TTSLEFDKEI FESDILCDIA HTTMLIEQNV ISEENGKKII
     AELKKIAEKG MENLDLDPSL DDIHMVIESE LIKELGEDVA GRMHTGRSRN DEVATDLRLS
     LRKKVLEIIG HLITMEQNML KVSNEHKETL TVGYTHLQQA QPVTFGHHIL SHVSAIERDI
     SRFFDTYNRI NISPLGCSAM ATTGFNLNRK RTQELLGFYD IIENSMDGVS SRDFIVETMA
     NISMLGTNLS KICEELVVFS SAEFNTIEIA NEYTSTSSIM PQKKNPDVAE ITRAKLSTLN
     GELVTVLTIM KALPNTYNRD LQEISPHLWK SVYTLIDCIQ MVDGMISTIK VNKERMKENA
     EKNYSTATEL ADTLVRECGI AFRMAHGIVG ELVKRSIEEK VEIKEIILEV LEKNNLSLSQ
     EKIDTALDPF ENVKLRNVIG GPAPEEVERA ISSFNTKIST HKEKLDEKIA EVNTVNKNLL
     K