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
//