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Database: UniProt
Entry: HLDE_SHIFL
LinkDB: HLDE_SHIFL
Original site: HLDE_SHIFL 
ID   HLDE_SHIFL              Reviewed;         477 AA.
AC   Q7UBI8; Q83Q47;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   08-MAY-2019, entry version 94.
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}; Synonyms=rfaE;
GN   OrderedLocusNames=SF3093, S3298;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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:
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:0000255|HAMAP-Rule:MF_01603};
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: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   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core
CC       biosynthesis.
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; AE005674; AAN44569.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18381.1; -; Genomic_DNA.
DR   RefSeq; NP_708862.1; NC_004337.2.
DR   SMR; Q7UBI8; -.
DR   PRIDE; Q7UBI8; -.
DR   EnsemblBacteria; AAN44569; AAN44569; SF3093.
DR   EnsemblBacteria; AAP18381; AAP18381; S3298.
DR   GeneID; 1026686; -.
DR   KEGG; sfl:SF3093; -.
DR   KEGG; sfx:S3298; -.
DR   PATRIC; fig|198214.7.peg.3670; -.
DR   eggNOG; ENOG4105DW0; Bacteria.
DR   eggNOG; COG2870; LUCA.
DR   HOGENOM; HOG000237584; -.
DR   KO; K03272; -.
DR   UniPathway; UPA00356; UER00437.
DR   UniPathway; UPA00356; UER00439.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
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   GO; GO:0009244; P:lipopolysaccharide core region 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   Acetylation; ATP-binding; Carbohydrate metabolism; Complete proteome;
KW   Kinase; Lipopolysaccharide biosynthesis; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN         1    477       Bifunctional protein HldE.
FT                                /FTId=PRO_0000080127.
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}.
FT   MOD_RES     179    179       N6-acetyllysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01603}.
FT   CONFLICT    133    133       M -> L (in Ref. 2; AAP18381).
FT                                {ECO:0000305}.
SQ   SEQUENCE   477 AA;  51129 MW;  E0F224053402A228 CRC64;
     MKVTLPEFER AGVMVVGDVM LDRYWYGPTS RISPEAPVPV VKVNTIEERP GGAANVAMNI
     ASLGANARLV GLTGIDDAAR ALSKSLADVN VKCDFVSVPT HPTITKLRVL SRNQQLIRLD
     FEEGFEGVDP QPMHERINQA LSSIGALVLS DYAKGALASV QQMIQLARKA GVPVLIDPKG
     TDFERYRGAT LLTPNLSEFE AVVGKCKTEE EIVERGMKLI ADYELSALLV TRSEQGMSLL
     QPGKAPLHMP TQAQEVYDVT GAGDTVIGVL AATLAAGNSL EEACFFANAA AGVVVGKLGT
     STVSPIELEN AVRGRADTGF GVMTEEELKL AVAAARKRGE KVVMTNGVFD ILHAGHVFYL
     ANARKLGDRL IVAVNSDAST KRLKGDSRPV NPLEQRMIVL GALEAVDWVV SFEEDTPQRL
     IAGILPDLLV KGGDYKPEEI AGSKEVWANG GEVLVLNFED GCSTTNIIKK IQQDKKG
//
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