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Database: UniProt
Entry: A0A1G5PQT3_9GAMM
LinkDB: A0A1G5PQT3_9GAMM
Original site: A0A1G5PQT3_9GAMM 
ID   A0A1G5PQT3_9GAMM        Unreviewed;       477 AA.
AC   A0A1G5PQT3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-JUN-2019, entry version 15.
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=SAMN03097708_00629 {ECO:0000313|EMBL:SCZ51944.1};
OS   Thiohalomonas denitrificans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thiohalomonas.
OX   NCBI_TaxID=415747 {ECO:0000313|EMBL:SCZ51944.1, ECO:0000313|Proteomes:UP000199648};
RN   [1] {ECO:0000313|EMBL:SCZ51944.1, ECO:0000313|Proteomes:UP000199648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLD2 {ECO:0000313|EMBL:SCZ51944.1,
RC   ECO:0000313|Proteomes:UP000199648};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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-
CC       heptose. {ECO:0000256|HAMAP-Rule:MF_01603,
CC       ECO:0000256|SAAS:SAAS00015127}.
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-glycero-D-manno-
CC       heptose 7-phosphate at the C-1 position to selectively form D-
CC       glycero-beta-D-manno-heptose-1,7-bisphosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_01603, ECO:0000256|SAAS:SAAS00015116}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H(+) =
CC         ADP-D-glycero-beta-D-manno-heptose + diphosphate;
CC         Xref=Rhea:RHEA:27465, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:59967, ChEBI:CHEBI:61593;
CC         EC=2.7.7.70; Evidence={ECO:0000256|HAMAP-Rule:MF_01603,
CC         ECO:0000256|SAAS:SAAS01118290};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP +
CC         D-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         ECO:0000256|SAAS:SAAS01118289};
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       {ECO:0000256|HAMAP-Rule:MF_01603, ECO:0000256|SAAS:SAAS00015131}.
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       {ECO:0000256|HAMAP-Rule:MF_01603, ECO:0000256|SAAS:SAAS00015137}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01603,
CC       ECO:0000256|SAAS:SAAS00015115}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       cytidylyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01603,
CC       ECO:0000256|SAAS:SAAS00540903}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
CC       kinase PfkB family. {ECO:0000256|HAMAP-Rule:MF_01603,
CC       ECO:0000256|SAAS:SAAS00540902}.
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DR   EMBL; FMWD01000002; SCZ51944.1; -; Genomic_DNA.
DR   BioCyc; GCF_900102855:BLP65_RS03130-MONOMER; -.
DR   UniPathway; UPA00356; UER00437.
DR   Proteomes; UP000199648; 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; -; 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 {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00015142};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00232977};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199648};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00446051, ECO:0000313|EMBL:SCZ51944.1};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00423489};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00015119};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00015117, ECO:0000313|EMBL:SCZ51944.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199648};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00061368, ECO:0000313|EMBL:SCZ51944.1}.
FT   DOMAIN       12    303       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   DOMAIN      345    435       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
FT   NP_BIND     195    198       ATP. {ECO:0000256|HAMAP-Rule:MF_01603}.
FT   REGION        1    319       Ribokinase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01603}.
FT   REGION      344    477       Cytidylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01603}.
FT   ACT_SITE    264    264       {ECO:0000256|HAMAP-Rule:MF_01603}.
SQ   SEQUENCE   477 AA;  51757 MW;  B4F976FED8CFAF63 CRC64;
     MKLELPDFSR ARVLIVGDLM LDRYWHGDTS RISPEAPVPV VRVGDVEERP GGAGNVALNI
     VALGGSATVI GLTGNDEAAD SLQLHLETQG VTCRFERQGQ FPTVTKLRVI SRHQQLIRLD
     FEDGFPGYSA EGLFDHYQDR LADTDVIVLS DYGKGTLRSA RALISAGRAA GKPVLIDPKG
     TDFERYRGAT LITPNLGEFE AVVGICRDEH ELELRAEQLR RELEIQALLV TRSERGVSLF
     IKDEPPLHLP THAREVFDVT GAGDTVISTL AGALAAGASF EMATSLANLA AGVVVGKLGT
     ATATVPELRQ AMRQQEPLSR GVMDEEALVG IVRDARAHGE RIVMTNGCFD ILHAGHVAYL
     QQAAALGDRL IVAVNNDTSV RKLKGEGRPI NPVEQRMVVL NALESVDWVI PFSEETPERL
     ICKLLPDTLV KGGDYRPEEI AGGPCVQKAG GKIVILDFVD GCSTTRIVEN IREQNRD
//
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