ID D0Z406_PHODD Unreviewed; 833 AA.
AC D0Z406;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Phosphoenolpyruvate-protein phosphotransferase of PTS system {ECO:0000313|EMBL:EEZ40137.1};
DE EC=2.7.3.9 {ECO:0000313|EMBL:EEZ40137.1};
GN ORFNames=VDA_001159 {ECO:0000313|EMBL:EEZ40137.1};
OS Photobacterium damselae subsp. damselae CIP 102761.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ40137.1, ECO:0000313|Proteomes:UP000003579};
RN [1] {ECO:0000313|EMBL:EEZ40137.1, ECO:0000313|Proteomes:UP000003579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ40137.1,
RC ECO:0000313|Proteomes:UP000003579};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA Bartels D.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC fructose 1-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:49252, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:37721, ChEBI:CHEBI:58674,
CC ChEBI:CHEBI:64837; EC=2.7.1.202;
CC Evidence={ECO:0000256|ARBA:ARBA00001401};
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}.
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DR EMBL; ADBS01000002; EEZ40137.1; -; Genomic_DNA.
DR RefSeq; WP_005306375.1; NZ_ADBS01000002.1.
DR AlphaFoldDB; D0Z406; -.
DR eggNOG; COG1080; Bacteria.
DR Proteomes; UP000003579; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR CDD; cd00367; PTS-HPr_like; 1.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR Gene3D; 3.30.1340.10; HPr-like; 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; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_sf.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR006318; PTS_EI-like.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR001020; PTS_HPr_His_P_site.
DR InterPro; IPR004715; PTS_IIA_fruc.
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; TIGR00848; fruA; 1.
DR NCBIfam; TIGR01417; PTS_I_fam; 1.
DR PANTHER; PTHR46244:SF4; MULTIPHOSPHORYL TRANSFER PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF00381; PTS-HPr; 1.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR PRINTS; PR01736; PHPHTRNFRASE.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55594; HPr-like; 1.
DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS51350; PTS_HPR_DOM; 1.
DR PROSITE; PS00369; PTS_HPR_HIS; 1.
PE 3: Inferred from homology;
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 Pyruvate {ECO:0000313|EMBL:EEZ40137.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003579};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEZ40137.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 5..97
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
FT DOMAIN 687..830
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000259|PROSITE:PS51094"
SQ SEQUENCE 833 AA; 92113 MW; 27B38F5FF7EFB2FE CRC64;
MSHPIQSFQF QCPLPNGIHA RPATHLEKQC QQFECQIILT NLRTQQSGDA KSVLSLVGTD
TLLNDQCEMR FEGVDSEQAC AALQHYIEQE FPHCDEALET LADESDIILP QSLTRLNPTL
ISGKRLATGI AQGQLSVFSQ IEPEHFATEH KDEQEETRFT TAHQQVCHAL SQKIANATAQ
EKEIIESHLA IVNDSAFVAG IKQHLANHST ANAILAEVER VSAQLRNASS SYLRERVLDI
KDVAIQLLTA AYPEKNLITE FTLNKPSVVI ANDLTPSQFL GLDREHLQGL VLTHAGSTSH
TVILARAFGI PTLSGIELSD CTKALNQTVY LDANLGVLAV DATPQVAQYF HRAIKLAQTQ
QEKQNGFAQQ KATTQDGHCI EVAANIACSI EAEGAFNQGA EGIGLFRTEM LFMDRSQAPD
EEEQFNHYRQ VLEAANGKPV IIRTMDIGGD KPIDYLQLPE EHNPFLGYRA VRIYPQFLTL
FHTQLKAILR AAQYGKAKMM IPMIQSIEEI RWVKQQLEVV KAELSSQGVS YSEHLELGIM
VEIPAVAFIV DQFCQEVDFF SIGSNDMTQY LLAVDRDNAQ VAKLYNSLAP SFLRMLNQVV
TTAHQHNKWV GLCGELGADA KVLPLLVGAG LDEISMGAPK IAATKSTLAT LDFAHCQQLF
ADACQCCTIS DVEQLLNQAS SAQPGKALLS QDCVFKHADF SSKEEVIQAL VGNLGVQGRC
DNAYKLEEDV WAREAVFSTG LGHGFAIPHT KSENIRHSSI SIAHLETPID WQSDSGDVDF
VIMLTLNKDQ GDQHMRIFSS LARKLIHQSF RDMLRDADNE AEVIRILEQE LAL
//
