ID A0A367RLH8_9NOSO Unreviewed; 835 AA.
AC A0A367RLH8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Phosphoenolpyruvate--protein phosphotransferase {ECO:0000313|EMBL:RCJ37325.1};
GN ORFNames=A6770_14425 {ECO:0000313|EMBL:RCJ37325.1};
OS Nostoc minutum NIES-26.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=1844469 {ECO:0000313|EMBL:RCJ37325.1, ECO:0000313|Proteomes:UP000252107};
RN [1] {ECO:0000313|Proteomes:UP000252107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tabuchi Yagui T.R.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:RCJ37325.1}.
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DR EMBL; LXQD01000120; RCJ37325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367RLH8; -.
DR Proteomes; UP000252107; 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; IPR023151; PEP_util_CS.
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; PS00742; PEP_ENZYMES_2; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Pyruvate {ECO:0000313|EMBL:RCJ37325.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000252107};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RCJ37325.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..136
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
FT DOMAIN 154..246
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
SQ SEQUENCE 835 AA; 88976 MW; 096C7B131FDEAF52 CRC64;
MVGIVIVSHS KQLALGVQEL AAQMVQGNVR LAVAAGIEDA DNPLGTDPIQ VYEAIASVFS
GDGVLVLMDL GSALMSAEMA LEFLSEAQRQ QVHLCEAPLV EGAIAAVVAA AAGRNIQQVI
AEARGALVAK AIQLGVVSSQ LSVGSSETTT HTEYPTREIR LTVSNRLGLH ARPAAQFVAT
VTRFQSQIRV RNLTRNTEAI RGDSINQVAI LGVLQGHELV ITAAGADADE ALAALQALFT
TNFGEDNTSY EPLQAVDHKV TPAIGGELLG IAASPGVAIA PVVHYQPPII TITEYHVDDP
ELEWQRLHRA ICTAKQEIQT LFSQASIQIG DAEAAIFDAH LLFLEDPVLL EAAHQRILDC
HLNAEAAWQA VVNEVAASYH TLEDSYLQER VDDVVDVGQR VLRLLVGNTH SELHLSEPAI
VVANDLTPSD TAGLDPKKVL GICTTSGSAT SHSAIIARTL GIPAVLGVDA EVLHLEDGTL
MALDGESGKA WVQPEPDILD LLEAKREAWQ TAQQEARATA HQPAITRDGR QVSIFANIGS
IADVQVAVAN GAEGVGLLRT EFLYFERATA PTEEEQFTVY QAIAQVLARR PLIIRTLDIG
GDKPLPYLKL GIPEANPFLG WRGIRLCLDR PELFKTQLRA ILRASAGHNI KVMLPMIATV
AEVRAAKEIL SEVKAELRQA AIPFDRAIAV GIMIEVPSAV AIADRLAAEV DFFSIGTNDL
SQYVMAGDRT NPRVATLVDA LHPAVLRMVQ QTVQAARTAG IWVGLCGELA ADPLATPILV
GLGLNELSVN PQAIPLLKQA IAQLSLAEAE AIAASVLQQD SATDVRALVQ NLISS
//
