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Database: UniProt
Entry: B7I338
LinkDB: B7I338
Original site: B7I338 
ID   ARLY_ACIB5              Reviewed;         477 AA.
AC   B7I338;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   11-JUN-2014, entry version 34.
DE   RecName: Full=Argininosuccinate lyase;
DE            Short=ASAL;
DE            EC=4.3.2.1;
DE   AltName: Full=Arginosuccinase;
GN   Name=argH; OrderedLocusNames=AB57_0347;
OS   Acinetobacter baumannii (strain AB0057).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=480119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB0057;
RX   PubMed=18931120; DOI=10.1128/JB.00834-08;
RA   Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H.,
RA   Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A.,
RA   Hujer A.M., Bonomo R.A., Gill S.R.;
RT   "Comparative genome sequence analysis of multidrug-resistant
RT   Acinetobacter baumannii.";
RL   J. Bacteriol. 190:8053-8064(2008).
CC   -!- CATALYTIC ACTIVITY: 2-(N(omega)-L-arginino)succinate = fumarate +
CC       L-arginine.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily.
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DR   EMBL; CP001182; ACJ39773.1; -; Genomic_DNA.
DR   RefSeq; YP_002317756.1; NC_011586.1.
DR   ProteinModelPortal; B7I338; -.
DR   SMR; B7I338; 29-473.
DR   STRING; 480119.AB57_0347; -.
DR   EnsemblBacteria; ACJ39773; ACJ39773; AB57_0347.
DR   GeneID; 7046005; -.
DR   KEGG; abn:AB57_0347; -.
DR   PATRIC; 20694503; VBIAciBau111166_0345.
DR   eggNOG; COG0165; -.
DR   HOGENOM; HOG000242744; -.
DR   KO; K01755; -.
DR   OMA; IRPRREI; -.
DR   OrthoDB; EOG6P5ZF8; -.
DR   BioCyc; ABAU480119:GHQY-354-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; Arginine biosynthesis; Complete proteome;
KW   Cytoplasm; Lyase.
FT   CHAIN         1    477       Argininosuccinate lyase.
FT                                /FTId=PRO_1000116297.
SQ   SEQUENCE   477 AA;  52721 MW;  5CFC4B64EC2A97E4 CRC64;
     MTTSSNPPNS AAPNQTSGMW GGRFSEATDA FVAEFTASVQ FDQRFYKQDI AGSIAHATML
     AKVGVLTEAE RDDIIEGLST IRAEIEAGTF EWRIDLEDVH MNIESRLTQR IGITGKKLHT
     GRSRNDQVAT DIRLYLRDEI DDILGLLERL QKGLLGLAAK NVNTIMPGFT HLQTAQPVTF
     GHHLLAWFEM LVRDTERLQD CRKRVNRMPL GSAALAGTTY PIDRAYTAEL LGFEAVSENS
     LDAVSDRDFA IEFNAAASLI MMHLSRMSEE LILWTSAQFK FVNIPDRFCT GSSIMPQKKN
     PDVPELIRGK SGRVFGDLVS LLTLMKGQPL AYNKDNQEDK EPLFDAIDTV RGSLMAFADM
     IPALVPNVEI MREAALRGFS TATDLADYLV KKGVAFRDAH EIVGKAVALG VAEEKDLSEL
     TLEQLQQFSD LITADVFDKA LTLEASVNAR DHIGGTSPKQ VEAAIARAHK RLEQLYA
//
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