ID   ARLY_METPE              Reviewed;         494 AA.
AC   B8GH19;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   04-NOV-2026, entry version 77.
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};
GN   OrderedLocusNames=Mpal_1078;
OS   Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Methanomicrobia; Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX   NCBI_TaxID=521011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX   PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA   Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA   Yavitt J.B., Zinder S.H.;
RT   "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT   Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL   Genome Announc. 3:0-0(2015).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001338; ACL16424.1; -; Genomic_DNA.
DR   RefSeq; WP_012617743.1; NC_011832.1.
DR   AlphaFoldDB; B8GH19; -.
DR   SMR; B8GH19; -.
DR   STRING; 521011.Mpal_1078; -.
DR   GeneID; 7270994; -.
DR   KEGG; mpl:Mpal_1078; -.
DR   eggNOG; arCOG01748; Archaea.
DR   HOGENOM; CLU_027272_2_3_2; -.
DR   OMA; AAAWQVM; -.
DR   OrthoDB; 27337at2157; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000002457; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01359; Argininosuccinate_lyase; 1.
DR   FunFam; 1.20.200.10:FF:000015; argininosuccinate lyase isoform X2; 1.
DR   Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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; IPR022761; Fumarate-Lyase-like_N.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   NCBIfam; TIGR00838; argH; 1.
DR   PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR   Pfam; PF14698; ASL_C2; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase;
KW   Reference proteome.
FT   CHAIN           1..494
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000116333"
SQ   SEQUENCE   494 AA;  53416 MW;  9A5DC8E09AC638B0 CRC64;
     MIHDVVREGR LSGVRSGEVA AFLSSRNADH WIAEADVLVD IAHLLMLYRQ GIIEPEPAAA
     VMDVLLRFSA DGVPEEAFDE QFEDIHAGIE SLLIAEVGIE QGGRLHIGRS RNDEVATCLR
     LRLCEELLVI GDAVNGLCEV LVSLAGEHTH SVMPGFTHLQ HAQPTTLAHH LLSYAQAFSR
     DLERLLSTYQ RVNRSPLGAA AFASTGYPID REFTATMLGF SGVLENSMDA VSTRDFALEA
     LADCAILMVN ASRCCEELIL WSSSLVRFVQ LDDAYCSTSS IMPQKKNPDT LEIMRARAGS
     VIGASTAALS IVKALPMSYN RDLQQLTPHL WEGIGDAGAS IRILAGALST ATFNTERMET
     EAGRGFSTAT ELADMMVREC GLPFRTAHHI VGRAVRSGSL TLVSLKKAAT GESIDLTALG
     LTEEKVQAAL DPVHGIEARS VLGGPAVASV STAIETLQES VKAGRTAIAE ERYRRTTAIT
     TLIKEARRLK TFHQ
//