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Entry: A0A0V7ZZ41_9CYAN
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Original site: A0A0V7ZZ41_9CYAN 
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
//
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