(data stored in ACNUC7421 zone)

SWISSPROT: Q2IM99_ANADE

ID   Q2IM99_ANADE            Unreviewed;       599 AA.
AC   Q2IM99;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 99.
DE   RecName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000256|PIRNR:PIRNR000732};
DE            EC=2.7.3.9 {ECO:0000256|PIRNR:PIRNR000732};
DE   AltName: Full=Phosphotransferase system, enzyme I {ECO:0000256|PIRNR:PIRNR000732};
GN   OrderedLocusNames=Adeh_0153 {ECO:0000313|EMBL:ABC79930.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79930.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|EMBL:ABC79930.1, ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|EMBL:ABC79930.1,
RC   ECO:0000313|Proteomes:UP000001935};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: General (non sugar-specific) component of the
CC       phosphoenolpyruvate-dependent sugar phosphotransferase system
CC       (sugar PTS). This major carbohydrate active-transport system
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane.
CC       Enzyme I transfers the phosphoryl group from phosphoenolpyruvate
CC       (PEP) to the phosphoryl carrier protein (HPr).
CC       {ECO:0000256|PIRNR:PIRNR000732}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-
CC         phospho-L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880,
CC         Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:29979, ChEBI:CHEBI:58702, ChEBI:CHEBI:64837;
CC         EC=2.7.3.9; Evidence={ECO:0000256|PIRNR:PIRNR000732};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000732,
CC         ECO:0000256|PIRSR:PIRSR000732-3};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000732}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|PIRNR:PIRNR000732, ECO:0000256|SAAS:SAAS00563041}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000251; ABC79930.1; -; Genomic_DNA.
DR   RefSeq; WP_011419213.1; NC_007760.1.
DR   STRING; 290397.Adeh_0153; -.
DR   EnsemblBacteria; ABC79930; ABC79930; Adeh_0153.
DR   KEGG; ade:Adeh_0153; -.
DR   eggNOG; ENOG4105BZ3; Bacteria.
DR   eggNOG; COG1080; LUCA.
DR   HOGENOM; HOG000278513; -.
DR   KO; K08483; -.
DR   OMA; CNAEWAL; -.
DR   BioCyc; ADEH290397:G1G5W-157-MONOMER; -.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-EC.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.274.10; -; 1.
DR   Gene3D; 3.20.20.60; -; 1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR018274; PEP_util_AS.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR023151; PEP_util_CS.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR024692; PTS_EI.
DR   InterPro; IPR006318; PTS_EI-like.
DR   InterPro; IPR008731; PTS_EIN.
DR   InterPro; IPR036618; PtsI_HPr-bd_sf.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   Pfam; PF05524; PEP-utilisers_N; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   PIRSF; PIRSF000732; PTS_enzyme_I; 1.
DR   SUPFAM; SSF47831; SSF47831; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   SUPFAM; SSF52009; SSF52009; 1.
DR   TIGRFAMs; TIGR01417; PTS_I_fam; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2IM99.
DR   SWISS-2DPAGE; Q2IM99.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR000732};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000732};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR000732,
KW   ECO:0000256|PIRSR:PIRSR000732-3};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000732,
KW   ECO:0000256|PIRSR:PIRSR000732-3};
KW   Phosphotransferase system {ECO:0000256|PIRNR:PIRNR000732};
KW   Pyruvate {ECO:0000313|EMBL:ABC79930.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   Sugar transport {ECO:0000256|PIRNR:PIRNR000732};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000732,
KW   ECO:0000256|SAAS:SAAS00451307, ECO:0000313|EMBL:ABC79930.1};
KW   Transport {ECO:0000256|PIRNR:PIRNR000732}.
FT   DOMAIN       11    136       PEP-utilisers_N. {ECO:0000259|Pfam:
FT                                PF05524}.
FT   DOMAIN      163    236       PEP-utilizers. {ECO:0000259|Pfam:
FT                                PF00391}.
FT   DOMAIN      267    549       PEP-utilizers_C. {ECO:0000259|Pfam:
FT                                PF02896}.
FT   REGION      463    464       PEP binding. {ECO:0000256|PIRSR:
FT                                PIRSR000732-2}.
FT   COILED      406    426       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    200    200       Tele-phosphohistidine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR000732-1}.
FT   ACT_SITE    511    511       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000732-1}.
FT   METAL       440    440       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000732-3}.
FT   METAL       464    464       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000732-3}.
FT   BINDING     307    307       PEP. {ECO:0000256|PIRSR:PIRSR000732-2}.
FT   BINDING     343    343       PEP. {ECO:0000256|PIRSR:PIRSR000732-2}.
FT   BINDING     474    474       PEP. {ECO:0000256|PIRSR:PIRSR000732-2}.
SQ   SEQUENCE   599 AA;  65382 MW;  B3FC26E1E618D5CA CRC64;
     MSRSSATTLV GIGASPGIAI GRCWTIERRR VRTPKRRLTP EEVEGELARL RTSLEISDVQ
     LAEVRGKVEE AQVPGSAEHT AIIDMHRMML KDEMLVLEAQ RQIREERLNA EWAVKRATRK
     IKNAFHEQAD DYFKERRADV DFVGERIIKN LLGQAPDVED VPPEGVIVVA HDLSPADTAL
     LLHEHKVAAF VTDAGAKTSH TAIVARALEV PAVVGVGRVT AVAERGDWIV VDGARGLVVI
     NPSPGERAGY EAAREKQLAG EQALLATRDL PARTLDDLTV RLAGNIEFAE EVPSLLAHGG
     EAVGLYRTEF LFMGRSDLPG EEEHYQNYRR ILEALAPRPV TIRTFDLGGD KLPAGMRVTA
     ENPALGLRAI RYCLRQPDMF RAQLRALLRA SVHGNLRVMF PMISGVAELR AAKHALRQAA
     DELRAEGVPF RQVPVGIMVE LPSAAMIADR LAAECDFFSI GTNDLIQYTI GIDRQDKDVA
     YLYKPLHLAV LRLLKLICDA GRAAGVPVSM CGEMAGEPVN ALVLLGLGVS ELSMNGPSIP
     LVKRVVRAAR AEEGRALVDR LLALTTADDI EHEVQAEMAR RFPGLLDGDD EGPEPAGQG
//

If you have problems or comments...

PBIL Back to PBIL home page