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Database: UniProt
Entry: W9G7E8_9MICO
LinkDB: W9G7E8_9MICO
Original site: W9G7E8_9MICO 
ID   W9G7E8_9MICO            Unreviewed;       479 AA.
AC   W9G7E8;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE            Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE   AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN   Name=argH {ECO:0000256|HAMAP-Rule:MF_00006};
GN   ORFNames=N865_11245 {ECO:0000313|EMBL:EWT01207.1};
OS   Intrasporangium oryzae NRRL B-24470.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=1386089 {ECO:0000313|EMBL:EWT01207.1, ECO:0000313|Proteomes:UP000019489};
RN   [1] {ECO:0000313|EMBL:EWT01207.1, ECO:0000313|Proteomes:UP000019489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-24470 {ECO:0000313|EMBL:EWT01207.1,
RC   ECO:0000313|Proteomes:UP000019489};
RA   Liu H., Wang G.;
RT   "Intrasporangium oryzae NRRL B-24470.";
RL   Submitted (AUG-2013) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000985, ECO:0000256|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.
CC       {ECO:0000256|ARBA:ARBA00004941, ECO:0000256|HAMAP-Rule:MF_00006}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EWT01207.1}.
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DR   EMBL; AWSA01000026; EWT01207.1; -; Genomic_DNA.
DR   RefSeq; WP_034806621.1; NZ_AWSA01000026.1.
DR   AlphaFoldDB; W9G7E8; -.
DR   STRING; 1386089.N865_11245; -.
DR   PATRIC; fig|1386089.3.peg.2588; -.
DR   eggNOG; COG0165; Bacteria.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000019489; Unassembled WGS sequence.
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; 1.10.40.30; 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; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
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.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00006};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW   Rule:MF_00006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:EWT01207.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019489}.
FT   DOMAIN          18..313
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          376..443
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   479 AA;  51480 MW;  1947B3C87B616678 CRC64;
     MSTEEPQAPA ERVSLWGGRF AGGPDQALAA LSKSTHFDWR LAPQDIAGSR AHARVLYAAG
     LLSDEHLAGM LAGLDRLEAD VLSGAFGPAE DDEDVHTALE RGLIERVGAD LGGRLRAGRS
     RNDQVATLFR MYLREHARTV GGLVLDVVDA LVAQADRHLG VAMPGRTHLQ HAQPVLLSHH
     LLAHAWALLR DVDRLRDWDA RADASPYGSG ALAGSSLGLD PEAVAHDLGF ARAVENSIDG
     TASRDFVAEF SFVSAMTAVD ISRIAEEVIL WATKEFSFVT LHDSYSTGSS IMPQKKNPDV
     AELARGKAGR LVGDLAGLLT TLKALPLAYN RDLQEDKEPV FDAVDTLEVL LPAFSGMVDT
     LTFNTERLES LAPQGFALAT DIAEWLVRQG VPFRVAHEVA GACVRECETR GIELWDLSDE
     DFARISEHLT PEVRSVLSVQ GSLASRDAVG GTAPARVTEQ LAAARARLAA ARAWTGRSD
//
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