HLDE_HAEIN
ID HLDE_HAEIN Reviewed; 476 AA.
AC O05074; Q48046;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
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, waaE;
GN OrderedLocusNames=HI_1526;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-427, AND ROLE IN LOS BIOSYNTHESIS.
RC STRAIN=NTHi 2019;
RX PubMed=7868252; DOI=10.1128/iai.63.3.818-824.1995;
RA Lee N.-G., Sunshine M.G., Apicella M.A.;
RT "Molecular cloning and characterization of the nontypeable Haemophilus
RT influenzae 2019 rfaE gene required for lipopolysaccharide biosynthesis.";
RL Infect. Immun. 63:818-824(1995).
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:7868252}.
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:7868252}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_01603};
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01603};
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. {ECO:0000255|HAMAP-
CC Rule:MF_01603}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_01603}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LOS core 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC43516.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC23172.1; -; Genomic_DNA.
DR EMBL; U17642; AAC43516.1; ALT_FRAME; Genomic_DNA.
DR PIR; C64127; C64127.
DR RefSeq; NP_439675.1; NC_000907.1.
DR RefSeq; WP_005693548.1; NC_000907.1.
DR AlphaFoldDB; O05074; -.
DR SMR; O05074; -.
DR STRING; 71421.HI_1526; -.
DR DNASU; 949890; -.
DR EnsemblBacteria; AAC23172; AAC23172; HI_1526.
DR KEGG; hin:HI_1526; -.
DR PATRIC; fig|71421.8.peg.1597; -.
DR eggNOG; COG0615; Bacteria.
DR eggNOG; COG2870; Bacteria.
DR HOGENOM; CLU_021150_2_1_6; -.
DR OMA; CEFANAA; -.
DR PhylomeDB; O05074; -.
DR BioCyc; HINF71421:G1GJ1-1548-MON; -.
DR UniPathway; UPA00356; UER00437.
DR UniPathway; UPA00356; UER00439.
DR UniPathway; UPA00976; -.
DR Proteomes; UP000000579; 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 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; 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.
PE 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; Kinase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..476
FT /note="Bifunctional protein HldE"
FT /id="PRO_0000080112"
FT REGION 1..318
FT /note="Ribokinase"
FT REGION 344..476
FT /note="Cytidylyltransferase"
FT ACT_SITE 264
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01603"
FT BINDING 195..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01603"
FT CONFLICT 36
FT /note="A -> R (in Ref. 2; AAC43516)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="L -> H (in Ref. 2; AAC43516)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="A -> G (in Ref. 2; AAC43516)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="E -> K (in Ref. 2; AAC43516)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="A -> T (in Ref. 2; AAC43516)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="R -> C (in Ref. 2; AAC43516)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 51946 MW; 4F241C08D2C6951E CRC64;
MAQYSAEFKQ AKVLVLGDVM LDRYWFGATN RISPEAPVPV VRVQENEERA GGAANVAMNI
ASLNVPVQLM GLIGQDETGS ALSLLLEKQK IDCNFVALET HPTITKLRIL SRHQQLLRLD
FEEDFNNVDC KDLLAKLESA VKNYGALILS DYGKGTLKDV QKMIQIARKA NVPVLIDPKG
TDFERYRGAT LLTPNMSEFE AVVGKCNTEE EIIEKGLKLI SDIELTALLV TRSEKGMTLL
RPNQEPYHLP TVAKEVFDVT GAGDTVISVL ATALADGRSF EESCYLANVA AGIVVGKLGT
STVSTVELEN AIHARPETGF GIMSEAELKD AVAQAKARGE KIVMTNGCFD ILHPGHISYL
ENARKLGDRL IVAVNSDDSV KRLKGESRPI NNLENRMAVL AGLASVDWLV PFTEDTPQRL
IGEILPDLLV KGGDYKPEEI AGSKEVWANG GDVKVLNFEN GCSTTNVIEK IKLLKD
