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Database: UniProt
Entry: A0A0K8MED4_9PROT
LinkDB: A0A0K8MED4_9PROT
Original site: A0A0K8MED4_9PROT 
ID   A0A0K8MED4_9PROT        Unreviewed;       478 AA.
AC   A0A0K8MED4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 46.
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   ECO:0000313|EMBL:GAO98234.1};
GN   ORFNames=Cva_00882 {ECO:0000313|EMBL:GAO98234.1};
OS   Caedimonas varicaedens.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Holosporales;
OC   Caedimonadaceae; Caedimonas.
OX   NCBI_TaxID=1629334 {ECO:0000313|EMBL:GAO98234.1, ECO:0000313|Proteomes:UP000036771};
RN   [1] {ECO:0000313|EMBL:GAO98234.1, ECO:0000313|Proteomes:UP000036771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Suzuki H., Dapper A.L., Gibson A.K., Jackson C., Lee H., Pejaver V.R.,
RA   Doak T., Lynch M.;
RT   "Caedibacter varicaedens, whole genome shotgun sequence.";
RL   Submitted (MAR-2015) 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: 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:GAO98234.1}.
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DR   EMBL; BBVC01000036; GAO98234.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K8MED4; -.
DR   STRING; 1629334.Cva_00882; -.
DR   UniPathway; UPA00356; UER00437.
DR   Proteomes; UP000036771; 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   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; 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.
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:UP000036771};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01603}.
FT   DOMAIN          9..307
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
FT   DOMAIN          350..444
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   REGION          1..322
FT                   /note="Ribokinase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT   REGION          350..478
FT                   /note="Cytidylyltransferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT   BINDING         198..201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
SQ   SEQUENCE   478 AA;  52523 MW;  9D696F4B2949E900 CRC64;
     MLFQRIPHTT ILCVGDVMLD YFVYGNVDRI SPEAPVPVFH KAQQTRVLGG AGNVVRNLSG
     FSAKTIFLSV VGHDRESEMV EQLLSELPQT QFFLIKDVSR ATTVKTRYIA HNQQLLRADH
     ETTHHLSHEI KEDLKKTFEN YLDEVDVVIF SDYGKGLFDR DLLTSLIQSA RKRGKSVIVD
     PKGHDYTLYC GATVLTPNLK ELSQASQKSL KTDDDIVKAA RSLLEKCQVE TMLVTRGERG
     MTLVDLQGMS EHIPTQALEV FDVSGAGDTV IAMFSAACAA KTPALQAAQF ANVAAGIVVG
     KVGTAITTLE EMREKLLSTT KRASSAKILT LPNALEQIIA WKRRGLKIGF TNGCFDLLHP
     GHIALLAQSK AECDRLIVGL NSDASVKRLK GEERPVQNQE ARSTVLSSLE SVDMVVIFEE
     DTPSSLIQQL RPDVLIKGAD YTLENVVGAR EVASWGGHVV LANLIPNQST TSTIQRMK
//
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