GenomeNet

Database: UniProt/TrEMBL
Entry: D0K3M8_STAAD
LinkDB: D0K3M8_STAAD
Original site: D0K3M8_STAAD 
ID   D0K3M8_STAAD            Unreviewed;       459 AA.
AC   D0K3M8;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   11-JUN-2014, entry version 33.
DE   RecName: Full=Argininosuccinate lyase;
DE            Short=ASAL;
DE            EC=4.3.2.1;
DE   AltName: Full=Arginosuccinase;
GN   Name=argH; OrderedLocusNames=SAAV_0921;
OS   Staphylococcus aureus (strain ED98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=681288;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED98;
RX   PubMed=19884497; DOI=10.1073/pnas.0909285106;
RA   Lowder B.V., Guinane C.M., Ben Zakour N.L., Weinert L.A.,
RA   Conway-Morris A., Cartwright R.A., Simpson A.J., Rambaut A., Nubel U.,
RA   Fitzgerald J.R.;
RT   "Recent human-to-poultry host jump, adaptation, and pandemic spread of
RT   Staphylococcus aureus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:19545-19550(2009).
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.
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; CP001781; ACY10838.1; -; Genomic_DNA.
DR   RefSeq; YP_003281844.1; NC_013450.1.
DR   ProteinModelPortal; D0K3M8; -.
DR   SMR; D0K3M8; 6-457.
DR   STRING; 681288.SAAV_0921; -.
DR   EnsemblBacteria; ACY10838; ACY10838; SAAV_0921.
DR   GeneID; 8613679; -.
DR   KEGG; sad:SAAV_0921; -.
DR   PATRIC; 32445894; VBIStaAur139507_0925.
DR   eggNOG; COG0165; -.
DR   HOGENOM; HOG000242744; -.
DR   KO; K01755; -.
DR   OMA; IRPRREI; -.
DR   OrthoDB; EOG6P5ZF8; -.
DR   BioCyc; SAUR681288:GJ8Z-912-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.
SQ   SEQUENCE   459 AA;  52017 MW;  6C6A89026336228C CRC64;
     MSNKAWGGRF EVQPEEWVDD FNASITFDQT LIDQDIEGSI AHATMLANQG IISQQDSEQI
     IQGLKSIQHD YHQDQIQFSA SLEDIHLNIE HELIKRIGDA GGKLHTGRSR NDQVATDMHL
     YTKKQVQDII ALIKSLQSVI VDIASNNVDT IMPGYTHLQR AQPISFAHHI MTYFWMLQRD
     QQRFEDSLKR IDINPLGAAA LSGTTYPIDR HETTALLNFG SLYENSLDAV SDRDYIIETL
     HNISLTMVHL SRFAEEIIFW STDEAKFITL SDAFSTGSSI MPQKKNPDMA ELIRGKVGRT
     TGHLMSMLMT LKGLPLAYNK DMQEDKEGLF DAVHTIKGSL RIFEGMIQTM TINKERLNQT
     VKEDFSNATE LADYLVTKNI PFRTAHEIVG KIVLECIQQG HYLLDVPLAT YQQHHSSIDA
     DIYDYLQPEN CLKRRQSYGS TGQSSVKQQL DVAKQLLSQ
//
DBGET integrated database retrieval system