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Database: UniProt
Entry: G2H0S9_9ENTR
LinkDB: G2H0S9_9ENTR
Original site: G2H0S9_9ENTR 
ID   G2H0S9_9ENTR            Unreviewed;       480 AA.
AC   G2H0S9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   05-JUN-2019, entry version 62.
DE   RecName: Full=Bifunctional protein HldE {ECO:0000256|HAMAP-Rule:MF_01603};
DE   Includes:
DE     RecName: Full=D-beta-D-heptose 7-phosphate kinase {ECO:0000256|HAMAP-Rule:MF_01603};
DE              EC=2.7.1.167 {ECO:0000256|HAMAP-Rule:MF_01603};
DE     AltName: Full=D-beta-D-heptose 7-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01603};
DE     AltName: Full=D-glycero-beta-D-manno-heptose-7-phosphate kinase {ECO:0000256|HAMAP-Rule:MF_01603};
DE   Includes:
DE     RecName: Full=D-beta-D-heptose 1-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_01603};
DE              EC=2.7.7.70 {ECO:0000256|HAMAP-Rule:MF_01603};
DE     AltName: Full=D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_01603};
GN   Name=hldE {ECO:0000256|HAMAP-Rule:MF_01603};
GN   ORFNames=Rin_00016620 {ECO:0000313|EMBL:EGY28401.1};
OS   Candidatus Regiella insecticola 5.15.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Candidatus Regiella.
OX   NCBI_TaxID=1005043 {ECO:0000313|EMBL:EGY28401.1};
RN   [1] {ECO:0000313|EMBL:EGY28401.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5.15 {ECO:0000313|EMBL:EGY28401.1};
RX   PubMed=21948522; DOI=10.1101/gr.125351.111;
RA   Hansen A.K., Vorburger C., Moran N.A.;
RT   "Genomic basis of endosymbiont-conferred protection against an insect
RT   parasitoid.";
RL   Genome Res. 22:106-114(2012).
CC   -!- FUNCTION: Catalyzes the ADP transfer from ATP to D-glycero-beta-D-
CC       manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-
CC       heptose. {ECO:0000256|HAMAP-Rule:MF_01603,
CC       ECO:0000256|SAAS:SAAS00015127}.
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-glycero-D-manno-
CC       heptose 7-phosphate at the C-1 position to selectively form D-
CC       glycero-beta-D-manno-heptose-1,7-bisphosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_01603, ECO:0000256|SAAS:SAAS00015116}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H(+) =
CC         ADP-D-glycero-beta-D-manno-heptose + diphosphate;
CC         Xref=Rhea:RHEA:27465, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:59967, ChEBI:CHEBI:61593;
CC         EC=2.7.7.70; Evidence={ECO:0000256|HAMAP-Rule:MF_01603,
CC         ECO:0000256|SAAS:SAAS01118290};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP +
CC         D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+);
CC         Xref=Rhea:RHEA:27473, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:60204, ChEBI:CHEBI:60208, ChEBI:CHEBI:456216;
CC         EC=2.7.1.167; Evidence={ECO:0000256|HAMAP-Rule:MF_01603,
CC         ECO:0000256|SAAS:SAAS01118289};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-
CC       manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose
CC       from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
CC       {ECO:0000256|HAMAP-Rule:MF_01603, ECO:0000256|SAAS:SAAS00015131}.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-
CC       manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose
CC       from D-glycero-beta-D-manno-heptose 7-phosphate: step 3/4.
CC       {ECO:0000256|HAMAP-Rule:MF_01603, ECO:0000256|SAAS:SAAS00015137}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01603,
CC       ECO:0000256|SAAS:SAAS00015115}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       cytidylyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01603,
CC       ECO:0000256|SAAS:SAAS00540903}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
CC       kinase PfkB family. {ECO:0000256|HAMAP-Rule:MF_01603,
CC       ECO:0000256|SAAS:SAAS00540902}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EGY28401.1}.
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DR   EMBL; AGCA01000393; EGY28401.1; -; Genomic_DNA.
DR   RefSeq; WP_006707311.1; NZ_AGCA01000393.1.
DR   EnsemblBacteria; EGY28401; EGY28401; Rin_00016620.
DR   PATRIC; fig|1005043.3.peg.1533; -.
DR   UniPathway; UPA00356; UER00437.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0033785; F:heptose 7-phosphate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0033786; F:heptose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01172; RfaE_like; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01603; HldE; 1.
DR   InterPro; IPR023030; Bifunc_HldE.
DR   InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR011913; RfaE_dom_I.
DR   InterPro; IPR011914; RfaE_dom_II.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   Pfam; PF00294; PfkB; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR   TIGRFAMs; TIGR02198; rfaE_dom_I; 1.
DR   TIGRFAMs; TIGR02199; rfaE_dom_II; 1.
DR   PROSITE; PS00583; PFKB_KINASES_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00015142};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00232977};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00446051};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00423489};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00015119};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00015117};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00061368}.
FT   DOMAIN       12    309       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   DOMAIN      349    460       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
FT   NP_BIND     199    202       ATP. {ECO:0000256|HAMAP-Rule:MF_01603}.
FT   REGION        1    322       Ribokinase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01603}.
FT   REGION      348    480       Cytidylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01603}.
FT   ACT_SITE    268    268       {ECO:0000256|HAMAP-Rule:MF_01603}.
SQ   SEQUENCE   480 AA;  52071 MW;  217D6E12C0FAB331 CRC64;
     MKMTLPFFEG AKVLVVGDLM LDRYWYGSTN RISPEAPVPI VKVDTNSIEE RPGGAANVAM
     NIAALGASCY VIGLTGVDLA ANILKEKLKE AKVVCQCIEL PHHPTNTKLR VISRHQQLIR
     LDFEEGDSFT EFDPQPLLIC VKERLPEISV LVLSDYAKGA LNNVQELIQL ARMNNIPVLV
     DPKGRDFERY RGATLLTPNL SEFETLVGHC SNEDELVTRG MQLMASFELT ALLVTRSEKG
     MTLLQCNKQP LHFPTQAKDV FDVTGAGDTV IGVLAAALAA GDTLEESCFL ANAAAGVVVG
     KLGTSTVSPI ELERVIHGES NTGYGVVTEQ QLQLAIQAAR RGGEKIVMTN GCFDILHAGH
     VSYLANARKL GDRLIVAVND DASVGRLKGK NRPINPLNQR MQVLAALEAV DWVVPFSEDT
     PARLIAKILP DVLVKGGDYQ LQDVAGRKEI QAAGGEVKIL NFEEGLSTSK LISKIQNSLE
//
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