位置:首页 > 蛋白库 > HLDE_TRIL1
HLDE_TRIL1
ID   HLDE_TRIL1              Reviewed;         491 AA.
AC   B3E5M9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Glov_0977;
OS   Trichlorobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) (Geobacter
OS   lovleyi).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Trichlorobacter.
OX   NCBI_TaxID=398767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1151 / DSM 17278 / SZ;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E.,
RA   Ritalahti K.M., Loeffler F.E., Richardson P.;
RT   "Complete sequence of chromosome of Geobacter lovleyi SZ.";
RL   Submitted (MAY-2008) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001089; ACD94700.1; -; Genomic_DNA.
DR   RefSeq; WP_012469050.1; NC_010814.1.
DR   AlphaFoldDB; B3E5M9; -.
DR   SMR; B3E5M9; -.
DR   STRING; 398767.Glov_0977; -.
DR   EnsemblBacteria; ACD94700; ACD94700; Glov_0977.
DR   KEGG; glo:Glov_0977; -.
DR   eggNOG; COG0615; Bacteria.
DR   eggNOG; COG2870; Bacteria.
DR   HOGENOM; CLU_021150_2_1_7; -.
DR   OMA; CEFANAA; -.
DR   OrthoDB; 1030724at2; -.
DR   UniPathway; UPA00356; UER00437.
DR   UniPathway; UPA00356; UER00439.
DR   Proteomes; UP000002420; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..491
FT                   /note="Bifunctional protein HldE"
FT                   /id="PRO_1000148126"
FT   REGION          1..330
FT                   /note="Ribokinase"
FT   REGION          356..491
FT                   /note="Cytidylyltransferase"
FT   ACT_SITE        275
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01603"
FT   BINDING         205..208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01603"
SQ   SEQUENCE   491 AA;  53022 MW;  2DB15DB12403A12A CRC64;
     MDRKMVESLF QRASTLKCLV VGDLMLDEYL WGRTDRISPE APVQVVDVLR EDLRLGGAGN
     VANNLLALGC QVTVASVIGE DENGWALLKA FSRQGVDTAP IYQEPGRRTG RKTRVIAANQ
     QIVRIDRESR EPLSGQIEQQ LINWLQQHIT GFDVVLVSDY LKGVLTPSVL ASVTSTASRR
     NIPVLVDPKG SDYSKYRGAT CLTPNRKEAE AASGVPIQDG ASLQQAADTI MSTVGLDNLL
     ITRSEEGMSL FCGNGETVHI PTVAREVFDV TGAGDTVLAL LACGLAGGLP LAESARLANV
     AAGIAVAKLG TSTVTPAEII AAVSLEHRDS DSKIKNREVL SEIIAAERAK GRQVVFTNGC
     FDLLHAGHVK YLQAARRLGD LLILGLNSDA SVRRLKGPKR PLIDEDERGH LMAALDCIDY
     VCLFEEDTPL ELITALKPQI LVKGGDYTPE GVVGKDLVES YGGRVELIPF VDGKSTTNII
     EKVLERYTDE Q
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025