ID F8EVL7_ZYMMT Unreviewed; 762 AA.
AC F8EVL7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN OrderedLocusNames=Zymop_1464 {ECO:0000313|EMBL:AEI38354.1};
OS Zymomonas mobilis subsp. pomaceae (strain ATCC 29192 / DSM 22645 / JCM
OS 10191 / CCUG 17912 / NBRC 13757 / NCIMB 11200 / NRRL B-4491 / Barker I).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=579138 {ECO:0000313|EMBL:AEI38354.1, ECO:0000313|Proteomes:UP000000491};
RN [1] {ECO:0000313|EMBL:AEI38354.1, ECO:0000313|Proteomes:UP000000491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29192 / DSM 22645 / JCM 10191 / CCUG 17912 / NBRC 13757 /
RC NCIMB 11200 / NRRL B-4491 / Barker I
RC {ECO:0000313|Proteomes:UP000000491};
RX PubMed=21742897; DOI=10.1128/JB.05273-11;
RA Kouvelis V.N., Davenport K.W., Brettin T.S., Bruce D., Detter C., Han C.S.,
RA Nolan M., Tapia R., Damoulaki A., Kyrpides N.C., Typas M.A., Pappas K.M.;
RT "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. pomaceae
RT lectotype strain ATCC 29192.";
RL J. Bacteriol. 193:5049-5050(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-
CC L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880, Rhea:RHEA-
CC COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:58702, ChEBI:CHEBI:64837; EC=2.7.3.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000683};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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; CP002865; AEI38354.1; -; Genomic_DNA.
DR RefSeq; WP_013934742.1; NC_015709.1.
DR AlphaFoldDB; F8EVL7; -.
DR STRING; 579138.Zymop_1464; -.
DR KEGG; zmp:Zymop_1464; -.
DR PATRIC; fig|579138.3.peg.1551; -.
DR eggNOG; COG3605; Bacteria.
DR HOGENOM; CLU_007308_7_1_5; -.
DR Proteomes; UP000000491; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
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 NCBIfam; TIGR01417; PTS_I_fam; 1.
DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 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; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 28..173
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
FT COILED 215..242
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 762 AA; 84877 MW; 707AD8B96D9DBD40 CRC64;
MSPSQQIATI AAREILTRLH DVMASRSNAQ SKLDQVVRII STALCSDVCS IYLLRDGVLE
LFATYGLKQE AVHVTKLALG QGLVGTIARD MAILNLSEAT SHPDFVHNPE TGEDLFHSFA
GVPIVRREQS VGVLAVQTTD PRRFADIEVE ALQTVAMVLA ELIFSAGLID ENSLSSGGVK
DQGSLRYNGL KLVEGMGRGY AVFHQPRITI EFTVAEDVEA ERQRLNAAFS QMREQIERMA
QDVEFFGSSN DHREVLATYR MFAYDEGWRR RIDEAIDSGL TAEAAIERVQ QHNRMRMREI
GDPLLAERLH DLEDLSNRLL RLVSGQLGTA ARLGLHSDAI LIARNMGPAE LLEYDRRRLK
GIVLEEGSLT SHVTIVAKAM GIPVLGRVKE IHQGVREGDL LLVDSNQGAV FIRPTPEIEE
AFATRFALSR KRRAEFAAMR DLPAITRDNH RIELMINAGL RDDVAALDAT GADGIGLFRT
EFEFLVSSTL PQRERQLRLY RDVLDAAGNR PVIFRTVDIG NDKTLPYINN SEDENEENPA
LGWRAIRLAL ERKALLKVQA RALIEGAADR HLYVMFPMIA EPWEYDQAQT LFESQNKWLI
KHNKPRAKVI HYGSMLEVPS LAESLDILLP KLDFLSIGTN DLIQFFFAAD RAHPKLAERY
DWLSPALLRF LARIIDQANA AGCKVGLCGE MGGRSLTAMA LIGLGLKRLS ITPVAIGPIK
AMIRSLDRDA FAPFLRDLLA RGVSNIGEHL EKWADKHGVI IN
//
