ID HLDE_GEOLS Reviewed; 491 AA.
AC B3E5M9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 29-MAY-2013, entry version 41.
DE RecName: Full=Bifunctional protein HldE;
DE Includes:
DE RecName: Full=D-beta-D-heptose 7-phosphate kinase;
DE EC=2.7.1.-;
DE AltName: Full=D-beta-D-heptose 7-phosphotransferase;
DE Includes:
DE RecName: Full=D-beta-D-heptose 1-phosphate adenosyltransferase;
DE EC=2.7.7.-;
GN Name=hldE; OrderedLocusNames=Glov_0977;
OS Geobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
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.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L.,
RA Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y.,
RA Fletcher K.E., 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-
CC heptose 7-phosphate at the C-1 position to form D,D-heptose-1,7-
CC bisphosphate (By similarity).
CC -!- FUNCTION: Catalyzes the ADP transfer to D-glycero-D-manno-heptose
CC 1-phosphate, yielding ADP-D,D-heptose (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + D-glycero-beta-D-manno-heptose 7-
CC phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate.
CC -!- CATALYTIC ACTIVITY: ATP + D-glycero-beta-D-manno-heptose 1-
CC phosphate = diphosphate + ADP-D-glycero-beta-D-manno-heptose.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-
CC manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose
CC from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-
CC manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose
CC from D-glycero-beta-D-manno-heptose 7-phosphate: step 3/4.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
CC kinase PfkB family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC cytidylyltransferase family.
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DR EMBL; CP001089; ACD94700.1; -; Genomic_DNA.
DR RefSeq; YP_001951220.1; NC_010814.1.
DR ProteinModelPortal; B3E5M9; -.
DR STRING; 398767.Glov_0977; -.
DR EnsemblBacteria; ACD94700; ACD94700; Glov_0977.
DR GeneID; 6366825; -.
DR KEGG; glo:Glov_0977; -.
DR PATRIC; 21993643; VBIGeoLov31523_0944.
DR eggNOG; COG2870; -.
DR HOGENOM; HOG000237584; -.
DR KO; K03272; -.
DR OMA; TKLRVMS; -.
DR ProtClustDB; CLSK828725; -.
DR BioCyc; GLOV398767:GH32-986-MONOMER; -.
DR UniPathway; UPA00356; UER00437.
DR UniPathway; UPA00356; UER00439.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0019200; F:carbohydrate kinase activity; IEA:HAMAP.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:HAMAP.
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:0046835; P:carbohydrate phosphorylation; IEA:GOC.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_2; 1.
DR Pfam; PF00294; PfkB; 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; FALSE_NEG.
PE 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase;
KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW Transferase.
FT CHAIN 1 491 Bifunctional protein HldE.
FT /FTId=PRO_1000148126.
FT NP_BIND 205 208 ATP (Potential).
FT REGION 1 330 Ribokinase.
FT REGION 356 491 Cytidylyltransferase.
FT ACT_SITE 275 275 Potential.
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
//
