HLDE_SALTY
ID HLDE_SALTY Reviewed; 477 AA.
AC Q7CPR9; Q9AJ74; Q9RFY7; Q9RFY8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Bifunctional protein HldE;
DE Includes:
DE RecName: Full=D-beta-D-heptose 7-phosphate kinase;
DE EC=2.7.1.167;
DE AltName: Full=D-beta-D-heptose 7-phosphotransferase;
DE AltName: Full=D-glycero-beta-D-manno-heptose-7-phosphate kinase;
DE Includes:
DE RecName: Full=D-beta-D-heptose 1-phosphate adenylyltransferase;
DE EC=2.7.7.70;
DE AltName: Full=D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase;
GN Name=hldE; Synonyms=rfaE, waaE; OrderedLocusNames=STM3200;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ROLE IN LPS BIOSYNTHESIS.
RX PubMed=12441667; DOI=10.1023/a:1021103501626;
RA Jin U.-H., Chung T.-W., Lee Y.-C., Ha S.-D., Kim C.-H.;
RT "Molecular cloning and functional expression of the rfaE gene required for
RT lipopolysaccharide biosynthesis in Salmonella typhimurium.";
RL Glycoconj. J. 18:779-787(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (MUTANTS SL1027 AND SL1102).
RX PubMed=10629197; DOI=10.1128/jb.182.2.488-497.2000;
RA Valvano M.A., Marolda C.L., Bittner M., Glaskin-Clay M., Simon T.L.,
RA Klena J.D.;
RT "The rfaE gene from Escherichia coli encodes a bifunctional protein
RT involved in the biosynthesis of the lipopolysaccharide core precursor ADP-
RT L-glycero-D-manno-heptose.";
RL J. Bacteriol. 182:488-497(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-
CC phosphate at the C-1 position to selectively form D-glycero-beta-D-
CC manno-heptose-1,7-bisphosphate. {ECO:0000305|PubMed:12441667}.
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-heptose.
CC {ECO:0000305|PubMed:12441667}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-
CC 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;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H(+) = ADP-
CC D-glycero-beta-D-manno-heptose + diphosphate; Xref=Rhea:RHEA:27465,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:59967, ChEBI:CHEBI:61593; EC=2.7.7.70;
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-
CC heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-
CC glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-
CC heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-
CC glycero-beta-D-manno-heptose 7-phosphate: step 3/4.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
CC kinase PfkB family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC cytidylyltransferase family. {ECO:0000305}.
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DR EMBL; AF155126; AAK20933.1; -; Genomic_DNA.
DR EMBL; AF163661; AAD49846.1; -; Genomic_DNA.
DR EMBL; AF163662; AAD49847.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22074.1; -; Genomic_DNA.
DR RefSeq; NP_462115.1; NC_003197.2.
DR RefSeq; WP_000867682.1; NC_003197.2.
DR AlphaFoldDB; Q7CPR9; -.
DR SMR; Q7CPR9; -.
DR STRING; 99287.STM3200; -.
DR PaxDb; Q7CPR9; -.
DR DNASU; 1254723; -.
DR EnsemblBacteria; AAL22074; AAL22074; STM3200.
DR GeneID; 1254723; -.
DR KEGG; stm:STM3200; -.
DR PATRIC; fig|99287.12.peg.3395; -.
DR HOGENOM; CLU_021150_2_1_6; -.
DR OMA; CEFANAA; -.
DR PhylomeDB; Q7CPR9; -.
DR BioCyc; SENT99287:STM3200-MON; -.
DR BRENDA; 2.7.1.167; 5542.
DR BRENDA; 2.7.7.70; 5542.
DR UniPathway; UPA00356; UER00437.
DR UniPathway; UPA00356; UER00439.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0033785; F:heptose 7-phosphate kinase activity; IBA:GO_Central.
DR GO; GO:0033786; F:heptose-1-phosphate adenylyltransferase activity; IBA:GO_Central.
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 ATP-binding; Carbohydrate metabolism; Kinase;
KW Lipopolysaccharide biosynthesis; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..477
FT /note="Bifunctional protein HldE"
FT /id="PRO_0000080125"
FT REGION 1..318
FT /note="Ribokinase"
FT REGION 344..477
FT /note="Cytidylyltransferase"
FT ACT_SITE 264
FT /evidence="ECO:0000255"
FT BINDING 195..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VARIANT 2
FT /note="K -> R (in mutants SL1102 and SL1027; heptoseless
FT LPS)"
FT VARIANT 236
FT /note="G -> E (in mutant SL1102; heptoseless LPS)"
FT VARIANT 273..276
FT /note="Missing (in mutant SL1102; heptoseless LPS)"
FT VARIANT 315..316
FT /note="RA -> PP (in mutant SL1027; heptoseless LPS)"
FT CONFLICT 4
FT /note="N -> T (in Ref. 1; AAK20933)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="A -> E (in Ref. 1; AAK20933)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 51124 MW; E4FF6B1DEE80568C CRC64;
MKVNLPAFER AGVMVVGDVM LDRYWYGPTC RISPEAPVPV VKVNTVEERP GGAANVAMNI
ASLGANARLV GLTGIDDAAR ALSKTLAEVN VKCDFVSVPT HPTITKLRVL SRNQQLIRLD
FEEGFEGVDP QPLHERINQA LGSIGALVLS DYAKGALTSV QTMISLARQA GVPVLIDPKG
TDFERYRGAT LLTPNLSEFE AVAGKCKSED ELVERGMKLI ADYDLSALLV TRSEQGMTLL
QPNKAPLHMP TQAQEVYDVT GAGDTVIGVL AATLAAGNTL EEACYFANAA AGVVVGKLGT
STVSPIELEN AVRGRADTGF GVMTEEELRQ AVASARKRGE KVVMTNGVFD ILHAGHVSYL
ANARKLGDRL IVAVNSDAST KRLKGESRPV NPLEQRMIVL GALESVDWVV SFEEDTPQRL
IAGILPDLLV KGGDYKPEEI AGSEEVWANG GEVMVLNFED GCSTTNIIKK IQTESEK
