(data stored in ACNUC7421 zone)

HOGENOM: STAAM_1_PE1000

ID   STAAM_1_PE1000                       STANDARD;      PRT;   269 AA.
AC   STAAM_1_PE1000; P65776; Q99V84;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Probable inorganic polyphosphate/ATP-NAD kinase;
DE   Short=Poly(P)/ATP NAD kinase; EC=2.7.1 23; (STAAM_1.PE1000).
GN   Name=ppnK; OrderedLocusNames=SAV1007;
OS   STAPHYLOCOCCUS AUREUS SUBSP. AUREUS MU50.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STAAM_1.PE1000.
CC       Staphylococcus aureus subsp. aureus Mu50, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:PPNK_STAAM
CC   -!- FUNCTION: Catalyzes the phosphorylation of NAD to NADP. Utilizes
CC       ATP and other nucleoside triphosphates as well as inorganic
CC       polyphosphate as a source of phosphorus (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + NAD(+) = ADP + NADP(+).
CC   -!- COFACTOR: Divalent metal ions (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the NAD kinase family.
CC   -!- GENE_FAMILY: HOG000275803 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P65776; Q99V84; -.
DR   EMBL; BA000017; BAB57169.1; -; Genomic_DNA.
DR   RefSeq; NP_371531.1; NC_002758.2.
DR   ProteinModelPortal; P65776; -.
DR   SMR; P65776; 1-263.
DR   STRING; P65776; -.
DR   World-2DPAGE; 0002:P65776; -.
DR   EnsemblBacteria; EBSTAT00000007565; EBSTAP00000007383; EBSTAG00000007564.
DR   GeneID; 1120982; -.
DR   GenomeReviews; BA000017_GR; SAV1007.
DR   KEGG; sav:SAV1007; -.
DR   eggNOG; COG0061; -.
DR   GeneTree; EBGT00050000025514; -.
DR   OMA; TISFANC; -.
DR   ProtClustDB; PRK04885; -.
DR   BioCyc; SAUR158878:SAV1007-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:EC.
DR   HAMAP; MF_00361; NAD_kinase; 1; -.
DR   InterPro; IPR016064; ATP-NAD_kinase_PpnK-typ.
DR   InterPro; IPR017438; ATP-NAD_kinase_PpnK-typ_a/b.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_all-b.
DR   InterPro; IPR002504; polyP/ATP_NADK_prd.
DR   Gene3D; G3DSA:2.60.200.30; ATP-NAD_kinase_PpnK-typ; 1.
DR   Gene3D; G3DSA:3.40.50.10330; ATP-NAD_kinase_PpnK-typ_a/b; 1.
DR   PANTHER; PTHR20275; ATP_NADK; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   SUPFAM; SSF111331; ATP-NAD_kinase_PpnK-typ; 1.
DR   HOGENOMDNA; STAAM_1.PE1000; -.
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; NAD; NADP;
KW   Nucleotide-binding; Transferase.
SQ   SEQUENCE   269 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRYTILTKGD SKSNALKHKM MNYMKDFRMI EDSENPEIVI SVGGDGTLLQ AFHQYSHMLS
     KVAFVGVHTG HLGFYADWLP HEVEKLIIEI NNSEFQVIEY PLLEIIMRYN DNGYETRYLA
     LNEATMKTEN GSTLVVDVNL RGKHFERFRG DGLCVSTPSG STAYNKALGG ALIHPSLEAM
     QITEIASINN RVFRTVGSPL VLPKHHTCLI SPVNHDTIRM TIDHVSIKHK NVNSIQYRVA
     NEKVRFARFR PFPFWKRVHD SFISSDEER
//

If you have problems or comments...

PBIL Back to PBIL home page