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Database: UniProt
Entry: A0A166GEP7_9GAMM
LinkDB: A0A166GEP7_9GAMM
Original site: A0A166GEP7_9GAMM 
ID   A0A166GEP7_9GAMM        Unreviewed;       478 AA.
AC   A0A166GEP7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   05-JUN-2019, entry version 28.
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=A3759_10895 {ECO:0000313|EMBL:KZZ44697.1};
OS   Thalassolituus sp. HI0120.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Thalassolituus.
OX   NCBI_TaxID=1822263 {ECO:0000313|EMBL:KZZ44697.1, ECO:0000313|Proteomes:UP000077137};
RN   [1] {ECO:0000313|EMBL:KZZ44697.1, ECO:0000313|Proteomes:UP000077137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI0120 {ECO:0000313|EMBL:KZZ44697.1,
RC   ECO:0000313|Proteomes:UP000077137};
RA   Sosa O.A.;
RT   "Microbial cycling of marine high molecular weight dissolved organic
RT   matter.";
RL   Submitted (MAR-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KZZ44697.1}.
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DR   EMBL; LWGC01001430; KZZ44697.1; -; Genomic_DNA.
DR   EnsemblBacteria; KZZ44697; KZZ44697; A3759_10895.
DR   UniPathway; UPA00356; UER00437.
DR   Proteomes; UP000077137; 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:UP000077137};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00446051, ECO:0000313|EMBL:KZZ44697.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077137};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00061368, ECO:0000313|EMBL:KZZ44697.1}.
FT   DOMAIN       11    302       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   DOMAIN      345    436       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
FT   NP_BIND     195    198       ATP. {ECO:0000256|HAMAP-Rule:MF_01603}.
FT   REGION        1    320       Ribokinase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01603}.
FT   REGION      344    478       Cytidylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01603}.
FT   ACT_SITE    264    264       {ECO:0000256|HAMAP-Rule:MF_01603}.
SQ   SEQUENCE   478 AA;  51965 MW;  EC74AD5CDC519BEE CRC64;
     MDVTIPDFHQ ARVLVFGDVM LDRYWQGPTS RISPEAPVPV VKIQDIENRA GGAGNVALNI
     STLGAGVDLM GLIGNDDNGT ALERLLNEAR IDCDFLKHPL HPTITKLRIM SRNQQLIRLD
     FEEAFDATDL TNIYQSFDEK VAQAGVVILS DYGKGALSNP QRLIESARRH KVPVLIDPKG
     TDFERYRGAT LITPNLSEFE AVVGTAKDDE TLVAKARTLI QDYDLQAVLV TRSEKGMTLI
     ERDQEPFHLP TKAREVYDVT GAGDTVISVL AASLAAKQNL QQATALANTA AGVVVGKLGT
     ATVSTEELRQ EIRSESHQGA GIFDESSLLL LVEEARARGE TLVMTNGCFD IIHPGHVQYL
     KEAKALGDRL LVAVNSDESV SRLKGPSRPI NPLDHRMAVL AGLESVDWVV PFGEDTPEHL
     ICRILPDILV KGGDYTIEEI AGGSCVQNNG GEVIILSFKD NCSTTAIVKR IQAEEATD
//
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