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Database: UniProt
Entry: B4TQH6
LinkDB: B4TQH6
Original site: B4TQH6 
ID   ARLY_SALSV              Reviewed;         458 AA.
AC   B4TQH6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   29-OCT-2014, entry version 40.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006};
DE            Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE   AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006};
GN   Name=argH {ECO:0000255|HAMAP-Rule:MF_00006};
GN   OrderedLocusNames=SeSA_A4333;
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633;
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- CATALYTIC ACTIVITY: 2-(N(omega)-L-arginino)succinate = fumarate +
CC       L-arginine. {ECO:0000255|HAMAP-Rule:MF_00006}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 3/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00006}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}.
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DR   EMBL; CP001127; ACF89760.1; -; Genomic_DNA.
DR   RefSeq; YP_002117037.1; NC_011094.1.
DR   ProteinModelPortal; B4TQH6; -.
DR   STRING; 439843.SeSA_A4333; -.
DR   EnsemblBacteria; ACF89760; ACF89760; SeSA_A4333.
DR   PATRIC; 32377229; VBISalEnt87589_4306.
DR   eggNOG; COG0165; -.
DR   HOGENOM; HOG000242744; -.
DR   OMA; KEGIFDA; -.
DR   OrthoDB; EOG6P5ZF8; -.
DR   BioCyc; SENT439843:GHHR-1176-MONOMER; -.
DR   UniPathway; UPA00068; UER00114.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; Arginine biosynthesis; Complete proteome;
KW   Cytoplasm; Lyase.
FT   CHAIN         1    458       Argininosuccinate lyase.
FT                                /FTId=PRO_1000089116.
SQ   SEQUENCE   458 AA;  50542 MW;  32076311A8BB5701 CRC64;
     MALWGGRFTQ AADQRFKQFN DSLRFDYRLA EQDIVGSVAW SKALVTVGVL TADEQRQLEE
     ALNVLLEEVR ANPQQILQSD AEDIHSWVEG KLIDKVGQLG KKLHTGRSRN DQVATDLKLW
     CKETVRELLT ANRQLQSALV ETAQANQDAV MPGYTHLQRA QPVTFAHWCL AYVEMLARDE
     SRLQDTLKRL DVSPLGCGAL AGTAYEIDRE QLAGWLGFTS ATRNSLDSVS DRDHVLELLS
     DAAIGMVHLS RFAEDLIFFN SGEAGFVELS DRVTSGSSLM PQKKNPDALE LIRGKCGRVQ
     GALTGMMMTL KGLPLAYNKD MQEDKEGLFD ALDTWLDCLH MAALVLDGIQ VKRLRCQDAA
     QQGYANATEL ADYLVAKGVP FREAHHIVGE AVVEAIRQGK PLEALPLADL QKFSRVIGDD
     VYPILSLQSC LDKRAAKGGV SPQQVAQAID DARARLAL
//
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