(data stored in ACNUC15324 zone)

HOGENOM: ACIAD_1_PE405

ID   ACIAD_1_PE405                        STANDARD;      PRT;   764 AA.
AC   ACIAD_1_PE405; Q6FEW8;
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   SubName: Full=Phosphoenolpyruvate-protein phosphotransferase; EC=2.7.3 9;
DE   (ACIAD_1.PE405).
GN   Name=ptsP; OrderedLocusNames=ACIAD0454;
OS   ACINETOBACTER SP. ADP1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIAD_1.PE405.
CC       Acinetobacter sp. ADP1 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:Q6FEW8_ACIAD
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- GENE_FAMILY: HOG000278514 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q6FEW8; -.
DR   EMBL; CR543861; CAG67390.1; -; Genomic_DNA.
DR   RefSeq; YP_045212.1; NC_005966.1.
DR   PDB; 3CI6; X-ray; 1.55 A; A/B=1-168.
DR   PDBsum; 3CI6; -.
DR   ProteinModelPortal; Q6FEW8; -.
DR   SMR; Q6FEW8; 1-168.
DR   STRING; Q6FEW8; -.
DR   GeneID; 2879344; -.
DR   GenomeReviews; CR543861_GR; ACIAD0454.
DR   KEGG; aci:ACIAD0454; -.
DR   NMPDR; fig|62977.3.peg.1111; -.
DR   eggNOG; COG3605; -.
DR   OMA; IINANRG; -.
DR   PhylomeDB; Q6FEW8; -.
DR   ProtClustDB; CLSK706958; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:EC.
DR   GO; GO:0005351; F:sugar:hydrogen symporter activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR008279; PEP-utiliz_enz_mobile_dom.
DR   InterPro; IPR006318; PEP_P_trans.
DR   InterPro; IPR023151; PEP_utiliser_CS.
DR   InterPro; IPR000121; PEP_utilisers.
DR   InterPro; IPR008731; PTS_PEP_utilis_N.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase.
DR   Gene3D; G3DSA:3.50.30.10; PEP_mobile; 1.
DR   Gene3D; G3DSA:1.10.274.10; PTS_PEP_utilis_N; 1.
DR   Gene3D; G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF05524; PEP-utilisers_N; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   PRINTS; PR01736; PHPHTRNFRASE.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF47831; PEP-utilisers_N; 1.
DR   SUPFAM; SSF52009; PEP_mobile; 1.
DR   SUPFAM; SSF51621; Pyrv/PenolPyrv_Kinase_cat; 1.
DR   TIGRFAMs; TIGR01417; PTS_I_fam; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   HOGENOMDNA; ACIAD_1.PE405; -.
KW   3D-structure; Complete proteome; Kinase; Magnesium; Metal-binding;
KW   Pyruvate; Transferase.
SQ   SEQUENCE   764 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSNMQLDTLR RIVQEINSSV SLHDSLDIMV NQVADAMKVD VCSIYLLDER NQRYLLMASK
     GLNPESVGHV SLQLSEGLVG LVGQREEIVN LENASKHERF AYLPETGEEI YNSFLGVPVM
     YRRKVMGVLV VQNKQPQDFS EAAESFLVTL CAQLSGVIAH AHAVGNIDVF RKPSNGATYK
     TFQGVPGSGG IALGRAIVLY PPADLASVPD REAEDISDEL QLLDQAVSSV RTEIQQLDEK
     MQDSLMSEER ALFSVFLRML DENALPAEIK ELIRAGNWAQ GAVRRVIDKH ITLFAQMEDD
     YLRERVSDLK DLGRRILASL QEADSSHREI SPDSIIIGEE ISTAALVELP VDNIAAIVTT
     EGAANSHMVI VARALGIPTV VGVTELPINT LDDAEMIVDA YQGRIFINPP RRMRQRYKEI
     QKEEEQIAKD LKQYETRDAI TPDGVAVRLY VNTGLMIDVV RGVQRGAKGV GLYRSEIPFM
     LRDRFPGEEE QRAMYRQQLS HFANKPVTMR TLDIGADKDL PYFSIEEENS ALGWRGLRFT
     LDHPEIFSTQ VRAMLKASIG LNNLHILLPM VTSVSEVEEV LYLVERDWNA VQEEEQVKIT
     KPKIGIMVEV PSVLLQIDEF SELVDFFSVG SNDLIQYLLA VDRNNPRVSS VYSHFHPSVL
     RALQRLVKDC HKYEKPVSIC GEMAGDPLSA ILLMAMGFNT LSMSSSNILR VRKAICHVAM
     SDAEKLLSEV VKMNNPLMVK SWIEYYFKNH GLGDMVKSNR LVSV
//

If you have problems or comments...

PBIL Back to PBIL home page