(data stored in ACNUC7421 zone)

SWISSPROT: HLDE_EDWI9

ID   HLDE_EDWI9              Reviewed;         477 AA.
AC   C5BHH2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 54.
DE   RecName: Full=Bifunctional protein HldE {ECO:0000255|HAMAP-Rule:MF_01603};
DE   Includes:
DE     RecName: Full=D-beta-D-heptose 7-phosphate kinase {ECO:0000255|HAMAP-Rule:MF_01603};
DE              EC=2.7.1.167 {ECO:0000255|HAMAP-Rule:MF_01603};
DE     AltName: Full=D-beta-D-heptose 7-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01603};
DE     AltName: Full=D-glycero-beta-D-manno-heptose-7-phosphate kinase {ECO:0000255|HAMAP-Rule:MF_01603};
DE   Includes:
DE     RecName: Full=D-beta-D-heptose 1-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_01603};
DE              EC=2.7.7.70 {ECO:0000255|HAMAP-Rule:MF_01603};
DE     AltName: Full=D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_01603};
GN   Name=hldE {ECO:0000255|HAMAP-Rule:MF_01603};
GN   OrderedLocusNames=NT01EI_0538;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-
CC       Rule:MF_01603}.
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:0000255|HAMAP-Rule:MF_01603}.
CC   -!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 7-phosphate +
CC       ATP = D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP.
CC       {ECO:0000255|HAMAP-Rule:MF_01603}.
CC   -!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 1-phosphate +
CC       ATP = ADP-D-glycero-beta-D-manno-heptose + diphosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01603}.
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:0000255|HAMAP-Rule:MF_01603}.
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:0000255|HAMAP-Rule:MF_01603}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01603}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
CC       kinase PfkB family. {ECO:0000255|HAMAP-Rule:MF_01603}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       cytidylyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01603}.
DR   EMBL; CP001600; ACR67771.1; -; Genomic_DNA.
DR   RefSeq; WP_015869971.1; NC_012779.2.
DR   ProteinModelPortal; C5BHH2; -.
DR   SMR; C5BHH2; -.
DR   STRING; 634503.NT01EI_0538; -.
DR   PRIDE; C5BHH2; -.
DR   EnsemblBacteria; ACR67771; ACR67771; NT01EI_0538.
DR   GeneID; 7961563; -.
DR   KEGG; eic:NT01EI_0538; -.
DR   PATRIC; fig|634503.3.peg.488; -.
DR   eggNOG; ENOG4105DW0; Bacteria.
DR   eggNOG; COG2870; LUCA.
DR   HOGENOM; HOG000237584; -.
DR   KO; K03272; -.
DR   OMA; CDPKGKD; -.
DR   OrthoDB; POG091H01Y4; -.
DR   UniPathway; UPA00356; UER00437.
DR   UniPathway; UPA00356; UER00439.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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;
DR   PRODOM; C5BHH2.
DR   SWISS-2DPAGE; C5BHH2.
KW   ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase;
KW   Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN         1    477       Bifunctional protein HldE.
FT                                /FTId=PRO_1000215693.
FT   NP_BIND     195    198       ATP. {ECO:0000255|HAMAP-Rule:MF_01603}.
FT   REGION        1    318       Ribokinase.
FT   REGION      344    477       Cytidylyltransferase.
FT   ACT_SITE    264    264       {ECO:0000255|HAMAP-Rule:MF_01603}.
SQ   SEQUENCE   477 AA;  51011 MW;  FDA0CA8623BF5A98 CRC64;
     MKVTLPDFRR AQVLVVGDVM LDRYWYGPTS RISPEAPVPV VKVETIEERP GGAANVAMNI
     ASLGASARLV GLTGVDDAAR ALSTRLDEVH VECDFVAIPA QPTITKLRVL SRNQQLIRLD
     FEEGFGGVDP GPILARIRQA LPQVGAVILS DYAKGALASV QAMICLARDA GVPVLIDPKG
     TDFERYRGAT LLTPNLSEFE AVVGRCHSEQ EIVDRGLALM ERFDLTALLV TRSEQGMTLL
     QRGIAPLHMP TQAQEVYDVT GAGDTVIGML AASIAAGASL DEACFLANAA AGVVVGKLGT
     STVSPIELEN AIRGRADTGF GVMTQEELKT AVLQARQRGE KVVMTNGVFD ILHAGHVSYL
     ANARRLGDRL IVAVNSDAST SRLKGPERPV NPLVQRMLVL AALEAVDWVI PFEEDTPQRI
     IAEILPDLLV KGGDYKPEEI AGGKEVIAAG GEVRVLNFED GCSTSNIINI IRQGQND
//

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