GenomeNet

Database: UniProt/TrEMBL
Entry: B3R616_CUPTR
LinkDB: B3R616_CUPTR
Original site: B3R616_CUPTR 
ID   B3R616_CUPTR            Unreviewed;       470 AA.
AC   B3R616;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   26-NOV-2014, entry version 47.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|SAAS:SAAS00067294};
DE            Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|SAAS:SAAS00067347};
DE   AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN   Name=argH {ECO:0000256|HAMAP-Rule:MF_00006,
GN   ECO:0000313|EMBL:CAQ70341.1};
GN   OrderedLocusNames=RALTA_A2407 {ECO:0000313|EMBL:CAQ70341.1};
OS   Cupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis
OS   (strain LMG 19424)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=164546 {ECO:0000313|EMBL:CAQ70341.1, ECO:0000313|Proteomes:UP000001692};
RN   [1] {ECO:0000313|EMBL:CAQ70341.1, ECO:0000313|Proteomes:UP000001692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R1 / LMG 19424 {ECO:0000313|Proteomes:UP000001692};
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M.,
RA   Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V.,
RA   Batut J., Medigue C., Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
CC   -!- CATALYTIC ACTIVITY: 2-(N(omega)-L-arginino)succinate = fumarate +
CC       L-arginine. {ECO:0000256|HAMAP-Rule:MF_00006,
CC       ECO:0000256|SAAS:SAAS00067374}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 3/3.
CC       {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|SAAS:SAAS00067273}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006,
CC       ECO:0000256|SAAS:SAAS00067213}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CU633749; CAQ70341.1; -; Genomic_DNA.
DR   RefSeq; YP_002006402.1; NC_010528.1.
DR   ProteinModelPortal; B3R616; -.
DR   STRING; 164546.RALTA_A2407; -.
DR   EnsemblBacteria; CAQ70341; CAQ70341; RALTA_A2407.
DR   GeneID; 6453732; -.
DR   KEGG; cti:RALTA_A2407; -.
DR   PATRIC; 21531450; VBICupTai42494_2365.
DR   eggNOG; COG0165; -.
DR   HOGENOM; HOG000242744; -.
DR   KO; K01755; -.
DR   OMA; KGCDLPD; -.
DR   OrthoDB; EOG6P5ZF8; -.
DR   BioCyc; CTAI164546:GJNE-2401-MONOMER; -.
DR   BioCyc; CTAI977880:GLC7-2401-MONOMER; -.
DR   UniPathway; UPA00068; UER00114.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 1.10.275.10; -; 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   PANTHER; PTHR11444; PTHR11444; 1.
DR   PANTHER; PTHR11444:SF3; PTHR11444:SF3; 1.
DR   Pfam; PF14698; ASL_C2; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00838; argH; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006,
KW   ECO:0000256|SAAS:SAAS00067315};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006,
KW   ECO:0000256|SAAS:SAAS00067228};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001692};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006,
KW   ECO:0000256|SAAS:SAAS00067394};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00006,
KW   ECO:0000256|SAAS:SAAS00067331}.
SQ   SEQUENCE   470 AA;  51113 MW;  CB29BA81D230489E CRC64;
     MSTSQLAKKG EAWSARFSEP MSDLVKRYTA SVFFDKRLAL FDIQGSLAHA AMLAKQGIIA
     EADRAEIERG MAQIRGEIEA GSFEWKLDLE DVHLNIEARL TALVGDAGKR LHTGRSRNDQ
     VATDIRLWLR SEIDNIIALL GALRTSLLDL AEQNADTILP GFTHLQVAQP VTFGHHLLAY
     NEMFTRDAER MADCRKRVNR LPLGAAALAG TSYPIDREFV AQQLGFDGVC RNSLDAVSDR
     DFAIEFCAAA ALVMTHVSRF SEELVLWMSP RVGFIDIADR FCTGSSIMPQ KKNPDVPELA
     RGKTGRVNGH LIGLLTLMKG QPLAYNKDNQ EDKEPLFDTV DTVVDTLRIF ADMVPGISVK
     PEAMRAAALQ GYATATDLAD YLVKKGLPFR DAHEAVAHAV RACDGRQCDL ADLTVAELRE
     VSGLGDKAAL IGDDVHAVLT LEGSVAARNH VGGTAPDQVR AAIAAARAAL
//
DBGET integrated database retrieval system