ID A0A0V7ZZ41_9CYAN Unreviewed; 850 AA.
AC A0A0V7ZZ41;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Phosphoenolpyruvate-protein phosphotransferase {ECO:0000313|EMBL:KST69845.1};
GN ORFNames=BC008_36425 {ECO:0000313|EMBL:KST69845.1};
OS Mastigocoleus testarum BC008.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Mastigocoleus.
OX NCBI_TaxID=371196 {ECO:0000313|EMBL:KST69845.1, ECO:0000313|Proteomes:UP000053372};
RN [1] {ECO:0000313|EMBL:KST69845.1, ECO:0000313|Proteomes:UP000053372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC008 {ECO:0000313|EMBL:KST69845.1,
RC ECO:0000313|Proteomes:UP000053372};
RA Guida B.S., Garcia-Pichel F.;
RT "Draft Genome of the Euendolithic (true boring) Cyanobacterium
RT Mastigocoleus testarum strain BC008.";
RL Genome Announc. 0:0-0(2015).
CC -!- FUNCTION: Component of the dihydroxyacetone kinase complex, which is
CC responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation
CC of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is
CC phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent
CC reaction, and a phosphorelay system on histidine residues finally leads
CC to phosphoryl transfer to DhaL and dihydroxyacetone.
CC {ECO:0000256|ARBA:ARBA00002788}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone
CC phosphate + pyruvate; Xref=Rhea:RHEA:18381, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:16016, ChEBI:CHEBI:57642, ChEBI:CHEBI:58702;
CC EC=2.7.1.121; Evidence={ECO:0000256|ARBA:ARBA00001113};
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KST69845.1}.
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DR EMBL; LMTZ01000013; KST69845.1; -; Genomic_DNA.
DR RefSeq; WP_027844768.1; NZ_LMTZ01000013.1.
DR AlphaFoldDB; A0A0V7ZZ41; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000053372; 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:0047324; F:phosphoenolpyruvate-glycerone phosphotransferase activity; IEA:UniProtKB-EC.
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 CDD; cd00367; PTS-HPr_like; 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; 3.40.50.510; Phosphotransferase system, mannose-type IIA component; 1.
DR Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1.
DR InterPro; IPR012844; DhaM_N.
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; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR006318; PTS_EI-like.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR001020; PTS_HPr_His_P_site.
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; TIGR02364; dha_pts; 1.
DR NCBIfam; TIGR01003; PTS_HPr_family; 1.
DR NCBIfam; TIGR01417; PTS_I_fam; 1.
DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR Pfam; PF03610; EIIA-man; 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 PRINTS; PR00107; PHOSPHOCPHPR.
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; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR SUPFAM; SSF53062; PTS system fructose IIA component-like; 1.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Pyruvate {ECO:0000313|EMBL:KST69845.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053372};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KST69845.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..134
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
FT DOMAIN 158..248
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
FT REGION 249..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 92013 MW; 7FA7F76380DF110D CRC64;
MVGIIIVSHS KQLAQGVREL ATQMVQGTVP LAIAAGIDDP ENPLGTDVME VHAAIESVYS
DDGVVILMDL GSALMSAEMA LEFLPSEQQE KVHLCAAPLV EGAIAAVVAA ASGANIDQVI
AEAKGALAAK SAQLGEDIEF TTSASQSHLI DSEEEQHADR IQVKISNRMG LHARPAAKFV
ATANQFQSQI RVQNLTKGGV PVRGESINEV AMLGARCGDD LAIFATGTDA HEALMTLQKL
IESNFGEPEI VDESPSTTSP SSTEIPNGPN NSFLRGIPAS PGVVIAPTVR YQPTFLAVEE
RYVDDVEGEW ERLQVVLITA YQEIQTLLSH ASTQIGDSEA AIFDAHLLFL SDPALLDAVR
HRIYEHNLNA EAAWQFTVEE IANGYRQMDD PYMRERAADM IDVGQRVQQL LGGSVTSPPK
LSQPAILVAK DLTPSDTAQL DSSLVLGICI TQGSATSHSA ILARSLGIPA VVGAPKQVLQ
VTDKTTIALD GETGQIWIDP DQSVKAELQV KQQEWENTQN QALESVRELA RTRDGRRIKV
LANISGIKDA RVALKMGAEG FGLLRTEFLY LDRAKAPTEA EQFSIYQEIA QSLDNQSLEH
KSLVNQPLEN QPLIIRTLDV GGDKPLAYLQ KPLESNPFLG WRGIRFCLDN VELFKTQLRA
ILRVSSSHRI KIMFPMIATL AELQRTKAIL NQVKTKLRQE NIPFDENMEV GMMIEIPSAV
AIADRLATEV DFFSIGSNDL SQYTTAADRT NPRVAKLADG LHPGVLKMIN QSIQAAHQAG
IWVGLCGELA SDPQAISILV GLGIDEISLN PHAIPKIKKA IAQLSFPEAE AIAQAALKLD
SSECVRMLIS
//