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Database: UniProt
Entry: A0A0P9ET10_9CHLR
LinkDB: A0A0P9ET10_9CHLR
Original site: A0A0P9ET10_9CHLR 
ID   A0A0P9ET10_9CHLR        Unreviewed;       161 AA.
AC   A0A0P9ET10;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   28-JUN-2023, entry version 18.
DE   RecName: Full=argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338};
DE            EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338};
DE   Flags: Fragment;
GN   ORFNames=SE17_44555 {ECO:0000313|EMBL:KPV41855.1};
OS   Kouleothrix aurantiaca.
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Kouleothrix.
OX   NCBI_TaxID=186479 {ECO:0000313|EMBL:KPV41855.1, ECO:0000313|Proteomes:UP000050509};
RN   [1] {ECO:0000313|EMBL:KPV41855.1, ECO:0000313|Proteomes:UP000050509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COM-B {ECO:0000313|EMBL:KPV41855.1,
RC   ECO:0000313|Proteomes:UP000050509};
RA   Hemp J.;
RT   "Draft genome sequence of Kouleothrix aurantiaca JCM 19913.";
RL   Submitted (SEP-2015) 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}.
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:KPV41855.1}.
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DR   EMBL; LJCR01003819; KPV41855.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P9ET10; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000050509; 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   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   InterPro; IPR009049; Argininosuccinate_lyase.
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   PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 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:ARBA00022571};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Lyase {ECO:0000313|EMBL:KPV41855.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050509}.
FT   DOMAIN          2..145
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KPV41855.1"
FT   NON_TER         161
FT                   /evidence="ECO:0000313|EMBL:KPV41855.1"
SQ   SEQUENCE   161 AA;  17464 MW;  CB5C450C1E3C5706 CRC64;
     MQRAQPILLA HWLLSHFWPL ERDRARLADC AARTAVLPLG SGALAGTPLR IDRAALAAEL
     GMREPSPNSL DAVSDRDFVA EFLFCAAMIG THLSRLAEDI IIYSTSEFGF VTLDDAYSTG
     SSLMPQKKNP DSFELLRGKS GRLIGHLVGL LTVLKGLPAA Y
//
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