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Database: UniProt
Entry: C7R8W1_KANKD
LinkDB: C7R8W1_KANKD
Original site: C7R8W1_KANKD 
ID   C7R8W1_KANKD            Unreviewed;       487 AA.
AC   C7R8W1;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 98.
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   OrderedLocusNames=Kkor_0554 {ECO:0000313|EMBL:ACV25974.1};
OS   Kangiella koreensis (strain DSM 16069 / KCTC 12182 / SW-125).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC   Kangiella.
OX   NCBI_TaxID=523791 {ECO:0000313|EMBL:ACV25974.1, ECO:0000313|Proteomes:UP000001231};
RN   [1] {ECO:0000313|EMBL:ACV25974.1, ECO:0000313|Proteomes:UP000001231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16069 / KCTC 12182 / SW-125
RC   {ECO:0000313|Proteomes:UP000001231};
RX   PubMed=21304661; DOI=10.4056/sigs.36635;
RA   Han C., Sikorski J., Lapidus A., Nolan M., Glavina Del Rio T., Tice H.,
RA   Cheng J.F., Lucas S., Chen F., Copeland A., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Bruce D., Goodwin L., Pitluck S., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Saunders E., Brettin T., Goker M., Tindall B.J., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT   "Complete genome sequence of Kangiella koreensis type strain (SW-125).";
RL   Stand. Genomic Sci. 1:226-233(2009).
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}.
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DR   EMBL; CP001707; ACV25974.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7R8W1; -.
DR   STRING; 523791.Kkor_0554; -.
DR   KEGG; kko:Kkor_0554; -.
DR   eggNOG; COG0615; Bacteria.
DR   eggNOG; COG2870; Bacteria.
DR   HOGENOM; CLU_021150_2_1_6; -.
DR   InParanoid; C7R8W1; -.
DR   OrthoDB; 9802794at2; -.
DR   UniPathway; UPA00356; UER00437.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000001231; 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; 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.
DR   PROSITE; PS00584; PFKB_KINASES_2; 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:UP000001231};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01603}.
FT   DOMAIN          26..317
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
FT   DOMAIN          358..483
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   REGION          1..333
FT                   /note="Ribokinase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT   REGION          358..487
FT                   /note="Cytidylyltransferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT   BINDING         209..212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
SQ   SEQUENCE   487 AA;  52276 MW;  392CC8F9CD3539F7 CRC64;
     MGIITATTSN DWVCPLKVTL PDFSNAKILV IGDIMLDRYW HGGTSRISPE APVPVVNVLE
     AEDRAGGAGN VALNISALGS KVTLCGITGQ DEAADSLTKL LNNHKIQCSF DQRSHQNTIT
     KLRIISRHQQ LIRLDFEKDF SLQSGVNLDL VSELIEQHDL VVLSDYGKGT LQDPQSIIQA
     ARKAGKLVVV DPKGSDFSKY QNATVITPNQ SEFDIVAGKS ANEEEFLNKG QQQRKSLNLD
     ALLVTRSEKG MALFEQGLEP FLQPTQAREV FDVTGAGDTV VAALATCLAS GFDHKSATQI
     ANLAAGIVVA KLGTATATRQ ELLNVMLQHQ PLSQGVVTEA ELIELIQHSK ASGETLVMTN
     GCFDILHAGH VAYLKQAAAL GDRLIVAVNG DDSVRRLKGE GRPVNPVDQR MEVLAGLASV
     DWVVEFSEDT PARLIGECLP DLLVKGGDYK PDQIAGGDAV MKNGGQVIIL DFVDGVSTTK
     IIEKARG
//
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