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Database: UniProt
Entry: Y0KJ71_9PROT
LinkDB: Y0KJ71_9PROT
Original site: Y0KJ71_9PROT 
ID   Y0KJ71_9PROT            Unreviewed;       485 AA.
AC   Y0KJ71;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Bifunctional protein HldE {ECO:0000256|HAMAP-Rule:MF_01603};
DE   Includes:
DE     RecName: Full=D-beta-D-heptose 7-phosphate kinase {ECO:0000256|HAMAP-Rule:MF_01603};
DE              EC=2.7.1.167 {ECO:0000256|HAMAP-Rule:MF_01603};
DE     AltName: Full=D-beta-D-heptose 7-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01603};
DE     AltName: Full=D-glycero-beta-D-manno-heptose-7-phosphate kinase {ECO:0000256|HAMAP-Rule:MF_01603};
DE   Includes:
DE     RecName: Full=D-beta-D-heptose 1-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_01603};
DE              EC=2.7.7.70 {ECO:0000256|HAMAP-Rule:MF_01603};
DE     AltName: Full=D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_01603};
GN   Name=hldE {ECO:0000256|HAMAP-Rule:MF_01603};
GN   ORFNames=Meth11DRAFT_1921 {ECO:0000313|EMBL:EUJ11085.1};
OS   Methylophilaceae bacterium 11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae.
OX   NCBI_TaxID=1101195 {ECO:0000313|EMBL:EUJ11085.1, ECO:0000313|Proteomes:UP000022668};
RN   [1] {ECO:0000313|EMBL:EUJ11085.1, ECO:0000313|Proteomes:UP000022668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11 {ECO:0000313|EMBL:EUJ11085.1,
RC   ECO:0000313|Proteomes:UP000022668};
RG   DOE Joint Genome Institute;
RA   Chistoserdova L., Huntemann M., Han J., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Palaniappan K., Ivanova N., Schaumberg A.,
RA   Pati A., Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003753, ECO:0000256|HAMAP-Rule:MF_01603}.
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:0000256|ARBA:ARBA00002319,
CC       ECO:0000256|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:0000256|ARBA:ARBA00000534, ECO:0000256|HAMAP-
CC         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:0000256|HAMAP-Rule:MF_01603};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004713}.
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:0000256|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:0000256|HAMAP-
CC       Rule:MF_01603}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01603}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       cytidylyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01603}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
CC       kinase PfkB family. {ECO:0000256|HAMAP-Rule:MF_01603}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EUJ11085.1}.
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DR   EMBL; JCKJ01000001; EUJ11085.1; -; Genomic_DNA.
DR   AlphaFoldDB; Y0KJ71; -.
DR   STRING; 1101195.Meth11DRAFT_1921; -.
DR   PATRIC; fig|1101195.3.peg.1885; -.
DR   eggNOG; COG0615; Bacteria.
DR   eggNOG; COG2870; Bacteria.
DR   UniPathway; UPA00356; UER00437.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000022668; Unassembled WGS sequence.
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; HUPs; 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   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   NCBIfam; TIGR02198; rfaE_dom_I; 1.
DR   NCBIfam; TIGR02199; rfaE_dom_II; 1.
DR   PANTHER; PTHR46969; BIFUNCTIONAL PROTEIN HLDE; 1.
DR   PANTHER; PTHR46969:SF1; BIFUNCTIONAL PROTEIN HLDE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   Pfam; PF00294; PfkB; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   PROSITE; PS00583; PFKB_KINASES_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01603};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_01603};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01603};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01603};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01603};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01603}; Reference proteome {ECO:0000313|Proteomes:UP000022668};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01603}.
FT   DOMAIN          17..311
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
FT   DOMAIN          356..451
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   REGION          1..328
FT                   /note="Ribokinase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT   REGION          356..485
FT                   /note="Cytidylyltransferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT   BINDING         207..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
SQ   SEQUENCE   485 AA;  51820 MW;  7363660EDBB80152 CRC64;
     MQHTLVSRVK QFGQTKQHAL VIGDVMLDRY LIGEVSRISP EAPVPVVLLK KQNERAGGAS
     NVAANLALLG VQTHILGCIG QDTEGKSLMQ LMQASGIDTQ GMVTSSHRPT IAKTRILGGH
     QQMMRLDQEN SGVFNAEETS QILNAFQQAL AKTPSIVVLS DYAKGLLSTT ICQTIIQACQ
     QANIPVLVDP KGVDYSKYQG ATALTPNKKE TAEACHTNVN DVALIEKAQQ LKSSLGLQFL
     AVTRSEEGIT LLDDTTHHLQ AAAQQVFDVS GAGDTVIATL AAGLMHGLSP LDSLELANVA
     AGVVVGKVGT VPITKSDLIH ALEDQRSNEQ AHKICDLPEL LEKVAVWKQA KQAIVFTNGC
     FDLLHAGHVT YLEAAKKRGD KLILGLNTDR SVSALKGPTR PVVNENDRAR VLAALASVDA
     VILFDEDTPL NLIHAIQPNI IAKGSDYTAD QVVGGKEVLS WGGEIALIDL VEGRSTSNLI
     KKMNS
//
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