ARLY_METMA
ID ARLY_METMA Reviewed; 491 AA.
AC Q8PUM6;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 133.
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=MM_2307;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(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; AE008384; AAM32003.1; -; Genomic_DNA.
DR RefSeq; WP_011034231.1; NC_003901.1.
DR AlphaFoldDB; Q8PUM6; -.
DR SMR; Q8PUM6; -.
DR STRING; 192952.MM_2307; -.
DR EnsemblBacteria; AAM32003; AAM32003; MM_2307.
DR GeneID; 24840130; -.
DR KEGG; mma:MM_2307; -.
DR PATRIC; fig|192952.21.peg.2643; -.
DR eggNOG; arCOG01748; Archaea.
DR HOGENOM; CLU_027272_2_3_2; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000000595; 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 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;
KW Reference proteome.
FT CHAIN 1..491
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137864"
SQ SEQUENCE 491 AA; 54946 MW; D2FCAFDD2B6EB569 CRC64;
MSNILRRGRL EAAQDEEILR YTSSMEADRW IFNADIVVDL AHTVMLREQG IIKEEDCSKI
LSGLLKIREE GMEKLDFSYE DIHISLESRL IDMVGEDVGG RMHSGRSRND EVATCIRLTL
REELLGLLEE IFALRKTLVS LAEKHSETLM PGFTHLQHAQ PTTLAHHLCA HESALGRDFD
RVQDAFSRVN LCPLGAAAFA STGFNLNRKR TQELLGFEGL LENSMDAVSS RDFLIECASV
FSNLMINLSR IAEELVIWSS SEFNFIELDD MYASTSSIMP QKKNPDTAEL MRGKTGVSVG
ALMSLLTICK GLPLSYNRDL QEATPNIWRS VETVRASVRV MEGMVKTMKV HPDVLAAESI
TGFTTATELA DTFVRETGIP FRTAHQIVGM LAKEREKPTM EKIDSASEVV LGESLSSKGL
TENMVKEALN PESNIKRRKI PGGPAPEEMK NYLSKRKTEL ELNAQEIATL KDIIDSAFEN
LLSVVEEYRK I