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Database: UniProt
Entry: A0A286DNG3_9ACTN
LinkDB: A0A286DNG3_9ACTN
Original site: A0A286DNG3_9ACTN 
ID   A0A286DNG3_9ACTN        Unreviewed;       493 AA.
AC   A0A286DNG3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338};
DE            EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338};
GN   ORFNames=SAMN06297387_1025 {ECO:0000313|EMBL:SOD60074.1};
OS   Streptomyces zhaozhouensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1300267 {ECO:0000313|EMBL:SOD60074.1, ECO:0000313|Proteomes:UP000219072};
RN   [1] {ECO:0000313|EMBL:SOD60074.1, ECO:0000313|Proteomes:UP000219072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7095 {ECO:0000313|EMBL:SOD60074.1,
RC   ECO:0000313|Proteomes:UP000219072};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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};
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}.
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DR   EMBL; OCNE01000002; SOD60074.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286DNG3; -.
DR   OrthoDB; 4899737at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000219072; Unassembled WGS sequence.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
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   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   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Lyase {ECO:0000313|EMBL:SOD60074.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219072}.
FT   DOMAIN          108..312
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          376..413
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   493 AA;  52372 MW;  17D33A9F3ECA7CBC CRC64;
     MTGGGAREPD QADTGRLAAT LGARTRSMVF GTAEPSAIDG ELELLTTIDL AHVVMLAERR
     LVPGRDAAEL LRHVGRLRAD GFRELHHRPM PRGLYLMYEA HLVSALGPET GGKLHTGRSR
     NDIKATATAM RLRAELAELL GQTLRLQAVL LCRARAYREV VMPVYTHYQP AMPVTYGYYL
     AGVATALERD IAALRHTLGE LDRCPLGAGA VSGTDLPIDP ARTAALLGFE APVAHAMDAV
     ASRDTALRAV AGAAGVGLTL SRLATDLQLW STQEFGFVTF PERLVGGSSA MPQKRNAFLL
     EHVKGRAGAA VGVWTGAASS MKSTPFTNSI EVGTEAVSEV WGALAGTVES VLLAQVLVSG
     GRPVAARMAA RAEEGFVTAT VVANRLVRQG VPFRTAHHTV GAAVRRAVES GSTRLTGADL
     PAGSVPPLDE VTAEHRYGGG PGMFDTSFDE VRRRLVDHAG WLRGRRESWA VARQRLDGAV
     AELTARPEGN EAP
//
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