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Database: UniProt
Entry: A0A0S1XY41_9BORD
LinkDB: A0A0S1XY41_9BORD
Original site: A0A0S1XY41_9BORD 
ID   A0A0S1XY41_9BORD        Unreviewed;       524 AA.
AC   A0A0S1XY41;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338};
DE            EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338};
GN   ORFNames=ASB57_07035 {ECO:0000313|EMBL:ALM82740.1};
OS   Bordetella sp. N.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM82740.1, ECO:0000313|Proteomes:UP000064621};
RN   [1] {ECO:0000313|EMBL:ALM82740.1, ECO:0000313|Proteomes:UP000064621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N {ECO:0000313|EMBL:ALM82740.1,
RC   ECO:0000313|Proteomes:UP000064621};
RA   Hou L.;
RT   "Draft genome of Bordetella sp. N.";
RL   Submitted (NOV-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}.
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DR   EMBL; CP013111; ALM82740.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S1XY41; -.
DR   STRING; 1746199.ASB57_07035; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000064621; Chromosome.
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; 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; 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   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Lyase {ECO:0000313|EMBL:ALM82740.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064621}.
FT   DOMAIN          116..309
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          384..460
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
FT   REGION          15..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  57174 MW;  76F3D51E3489C569 CRC64;
     MALACAPALT AAQIKPVEPA AGNAEKPSAK PAEKPATKAP AKPVRDEFFW LGEINKATAV
     INTDEGLLDK SMAPRLAAAV QKVIDDGNQP GGKRPSTVIT FEPLLIKAGG LDVTLLHAGR
     SSQDMHATYR SAILRDKLLE LADQLHATSK TLVDLAAKHV DTIVPNYTNG VAAQPNSYGH
     YLLGFAAALE RDAQRIQETY ARVDRSPMGT TVLNGTSWPL NRKRMADYLG YAKLVDNAYD
     AAQISSMDEP VEVSSIVTAI GLHTGNFIED IMTQYAQSRP WILLQEGGGN TYVSSAMPQK
     RNPGLLNSTR SDASTALTLA MGPIIQTHNI TPGMPDPKEV DQNSAMVDAA IKALKKWDRV
     LKALVINPDR ALEELNSDWT ASQELADLLM RKYKLPFREG HHFASEVVEY ARQHDIKPLA
     FPYADAKRIY ADVVKGSKYP QELPMSEAEF RASLDPVAIV KARATSGGPQ PAEMERMLKE
     ARDNLAQQDT WIKSHRSHID DALARLNKDF DTLVAQGDKA TPAK
//
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