HLDE_SHEPA
ID HLDE_SHEPA Reviewed; 476 AA.
AC A8H086;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 75.
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}; OrderedLocusNames=Spea_0646;
OS Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=398579;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700345 / ANG-SQ1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT "Complete sequence of Shewanella pealeana ATCC 700345.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-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-heptose.
CC {ECO:0000255|HAMAP-Rule:MF_01603}.
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 -!- 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=ABV85973.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000851; ABV85973.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041410824.1; NC_009901.1.
DR AlphaFoldDB; A8H086; -.
DR SMR; A8H086; -.
DR STRING; 398579.Spea_0646; -.
DR EnsemblBacteria; ABV85973; ABV85973; Spea_0646.
DR KEGG; spl:Spea_0646; -.
DR eggNOG; COG0615; Bacteria.
DR eggNOG; COG2870; Bacteria.
DR HOGENOM; CLU_021150_2_1_6; -.
DR UniPathway; UPA00356; UER00437.
DR UniPathway; UPA00356; UER00439.
DR Proteomes; UP000002608; 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 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.
DR PROSITE; PS00584; PFKB_KINASES_2; 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_0000335559"
FT REGION 1..319
FT /note="Ribokinase"
FT REGION 345..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"
SQ SEQUENCE 476 AA; 50318 MW; 1985CD182646EAF2 CRC64;
MKISLPAFEK AKVLVVGDVM LDRYWAGPTA RISPEAPVPV VKVEQLEDRP GGAANVAINI
ATLGGSASLA GIVGVDETAD ALTVGVRALG VEPNWHKVAD KPTITKLRVM SRNQQLLRLD
FEESYSQAES DALLAQSLSE LDKVDVAVLS DYAKGALISP QSFIEAANAK GVKVLVDPKG
SDFSKYRGAY LLTPNMSEFE VVVGKVESEA DLVAKAQGLL QAFDLTAMLV TRSEKGMTLI
TKDQPELHIP TVAREVYDVT GAGDTVISAL ATAIAAGSDL PQACAIANTA AGIVVAKLGT
STVTRLELIE ALSLSHGESG FGAVSEDQLA YALEQAKLRG ERVVMTNGCF DILHAGHVSY
LQQARALGDR LIVAVNTDAS VKRLKGEGRP VNSEDRRMTV LAALASVDWV VPFSEDTPQR
IISRLLPDLL VKGGDYKVED IAGGSEVMAA GGQVKVLGFE DGISTTAIIQ NIMANQ
