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Entry: A0A0S1XXD6_9BORD
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ID   A0A0S1XXD6_9BORD        Unreviewed;       477 AA.
AC   A0A0S1XXD6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=ASB57_05715 {ECO:0000313|EMBL:ALM82525.1};
OS   Bordetella sp. N.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM82525.1, ECO:0000313|Proteomes:UP000064621};
RN   [1] {ECO:0000313|EMBL:ALM82525.1, ECO:0000313|Proteomes:UP000064621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N {ECO:0000313|EMBL:ALM82525.1,
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, 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}.
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DR   EMBL; CP013111; ALM82525.1; -; Genomic_DNA.
DR   RefSeq; WP_057651312.1; NZ_CP013111.1.
DR   AlphaFoldDB; A0A0S1XXD6; -.
DR   STRING; 1746199.ASB57_05715; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000064621; 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; 1.10.40.30; 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|HAMAP-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:ALM82525.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064621}.
FT   DOMAIN          26..319
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          382..450
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   477 AA;  52358 MW;  AD45888C371E2A8B CRC64;
     MANTPANTPS SAQDQFANKA QAWSARFSEP VSDLVKRYTA SVDFDKRLAR QDIQGSLAHA
     DMLAAQGIIT AQDLADIQRG MTQILSEIDA GSFQWLLDLE DVHLNIEKRL VELVGDAGKR
     LHTGRSRNDQ VATDIRLWLR GEIDILLDLL RQLRHALAGV ALENAATIMP GFTHLQVAQP
     VTFGHHLLAY AEMFGRDAER LADCRRRVNR LPLGAAALAG TSYPIDRERV ARTLGFDGVC
     RNSLDAVSDR DFAIEFCAAA ALVMTHVSRF SEELVLWMSP RVGFIDLADR FCTGSSIMPQ
     KKNPDVPELA RGKTGRVNGH LVALLTLMKG QPLAYNKDNQ EDKEGLFDTA DTLRDTLTIF
     ADMAGGIKVK ADNMRAAALQ GFATATDLAD YLVKRGLPFR DAHEVVAHAV RDCEQRGCDL
     ADLTLAELQA YNASIGEDIH QVLTLEGSVA ARNHIGGTAP ERVRDEAQRV LDETKRA
//
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