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Bifunctional protein HldE [Includes: D-beta-D-heptose 1-phosphate adenylyltransferase (EC 2.7.7.70) (D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase); D-beta-D-heptose 7-phosphate kinase (EC 2.7.1.167) (D-glycero-beta-D-manno-heptose-7-phosphate kinase) (D-beta-D-heptose 7-phosphotransferase)]

 A0A1D2QSJ5_9GAMM        Unreviewed;       471 AA.
A0A1D2QSJ5;
30-NOV-2016, integrated into UniProtKB/TrEMBL.
30-NOV-2016, sequence version 1.
27-SEP-2017, entry version 9.
RecName: Full=Bifunctional protein HldE {ECO:0000256|HAMAP-Rule:MF_01603};
Includes:
RecName: Full=D-beta-D-heptose 1-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_01603};
EC=2.7.7.70 {ECO:0000256|HAMAP-Rule:MF_01603};
AltName: Full=D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_01603};
Includes:
RecName: Full=D-beta-D-heptose 7-phosphate kinase {ECO:0000256|HAMAP-Rule:MF_01603};
EC=2.7.1.167 {ECO:0000256|HAMAP-Rule:MF_01603};
AltName: Full=D-beta-D-heptose 7-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01603};
AltName: Full=D-glycero-beta-D-manno-heptose-7-phosphate kinase {ECO:0000256|HAMAP-Rule:MF_01603};
Name=hldE {ECO:0000256|HAMAP-Rule:MF_01603};
ORFNames=AB835_02795 {ECO:0000313|EMBL:ODS24534.1};
Candidatus Endobugula sertula (Bugula neritina bacterial symbiont).
Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
Cellvibrionaceae; Candidatus Endobugula.
NCBI_TaxID=62101 {ECO:0000313|EMBL:ODS24534.1};
[1] {ECO:0000313|EMBL:ODS24534.1}
NUCLEOTIDE SEQUENCE.
STRAIN=AB1-4 {ECO:0000313|EMBL:ODS24534.1};
PubMed=27590822;
Miller I.J., Vanee N., Fong S.S., Lim-Fong G.E., Kwan J.C.;
"Lack of overt genome reduction in the bryostatin-producing bryozoan
symbiont, 'Candidatus Endobugula sertula'.";
Appl. Environ. Microbiol. 0:0-0(2016).
-!- FUNCTION: Catalyzes the ADP transfer from ATP to D-glycero-beta-D-
manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-
heptose. {ECO:0000256|HAMAP-Rule:MF_01603,
ECO:0000256|SAAS:SAAS00558028}.
-!- FUNCTION: Catalyzes the phosphorylation of D-glycero-D-manno-
heptose 7-phosphate at the C-1 position to selectively form D-
glycero-beta-D-manno-heptose-1,7-bisphosphate. {ECO:0000256|HAMAP-
Rule:MF_01603, ECO:0000256|SAAS:SAAS00634129}.
-!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 1-phosphate +
ATP = ADP-D-glycero-beta-D-manno-heptose + diphosphate.
{ECO:0000256|HAMAP-Rule:MF_01603, ECO:0000256|SAAS:SAAS00366614}.
-!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 7-phosphate +
ATP = D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP.
{ECO:0000256|HAMAP-Rule:MF_01603, ECO:0000256|SAAS:SAAS00634104}.
-!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-
manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose
from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
{ECO:0000256|HAMAP-Rule:MF_01603, ECO:0000256|SAAS:SAAS00634108}.
-!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-
manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose
from D-glycero-beta-D-manno-heptose 7-phosphate: step 3/4.
{ECO:0000256|HAMAP-Rule:MF_01603, ECO:0000256|SAAS:SAAS00054951}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01603,
ECO:0000256|SAAS:SAAS00634121}.
-!- SIMILARITY: In the C-terminal section; belongs to the
cytidylyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01603,
ECO:0000256|SAAS:SAAS00634114}.
-!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
kinase PfkB family. {ECO:0000256|HAMAP-Rule:MF_01603,
ECO:0000256|SAAS:SAAS00634109}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:ODS24534.1}.
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EMBL; MDLC01000007; ODS24534.1; -; Genomic_DNA.
UniPathway; UPA00356; UER00437.
UniPathway; UPA00356; UER00439.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0033785; F:heptose 7-phosphate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0033786; F:heptose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd01172; RfaE_like; 1.
Gene3D; 3.40.1190.20; -; 1.
Gene3D; 3.40.50.620; -; 1.
HAMAP; MF_01603; HldE; 1.
InterPro; IPR023030; Bifunc_HldE.
InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
InterPro; IPR004821; Cyt_trans-like.
InterPro; IPR011611; PfkB_dom.
InterPro; IPR011913; RfaE_dom_I.
InterPro; IPR011914; RfaE_dom_II.
InterPro; IPR029056; Ribokinase-like.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF01467; CTP_transf_like; 1.
Pfam; PF00294; PfkB; 1.
SUPFAM; SSF53613; SSF53613; 1.
TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
TIGRFAMs; TIGR02198; rfaE_dom_I; 1.
TIGRFAMs; TIGR02199; rfaE_dom_II; 1.
PROSITE; PS00583; PFKB_KINASES_1; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01603,
ECO:0000256|SAAS:SAAS00054912};
Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01603,
ECO:0000256|SAAS:SAAS00054907};
Kinase {ECO:0000256|HAMAP-Rule:MF_01603,
ECO:0000256|SAAS:SAAS00644883, ECO:0000313|EMBL:ODS24534.1};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01603,
ECO:0000256|SAAS:SAAS00634118};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01603,
ECO:0000256|SAAS:SAAS00054912};
Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01603,
ECO:0000256|SAAS:SAAS00444162};
Transferase {ECO:0000256|HAMAP-Rule:MF_01603,
ECO:0000256|SAAS:SAAS00444162, ECO:0000256|SAAS:SAAS00644883,
ECO:0000313|EMBL:ODS24534.1}.
DOMAIN 11 301 PfkB. {ECO:0000259|Pfam:PF00294}.
DOMAIN 343 445 CTP_transf_like.
{ECO:0000259|Pfam:PF01467}.
NP_BIND 194 197 ATP. {ECO:0000256|HAMAP-Rule:MF_01603}.
REGION 1 317 Ribokinase. {ECO:0000256|HAMAP-
Rule:MF_01603}.
REGION 342 471 Cytidylyltransferase. {ECO:0000256|HAMAP-
Rule:MF_01603}.
ACT_SITE 263 263 {ECO:0000256|HAMAP-Rule:MF_01603}.
SEQUENCE 471 AA; 51183 MW; 6CC193DEBCAE545A CRC64;
MLDSFPNYHK ARVAVIGDIM VDRYFYGDVQ RISPEAPVPV VNVQRESLLP GGAANVAMNL
SALGAHIKLS GVVGRDADAE QLLTQIESVG VECCFNYSHN DTIVKARVMG EQQQLLRMDF
EKKFTIEDWE GTWAACQSQL NDVDVLVLSD YNKGTLHDCQ ALIKAAKKQS IPVLIDPKGS
DFRKYSGADL LTPNLSELIA IVGVIHSEAE LQEKAQQLIQ ELNIGALLVT RSEKGMTLFR
RALNEYHLPA ITKEVVDVTG AGDTVIATIA ASLAAGSDIE SAVMFSNIAA SIVVSKVGTT
AVTAPELEFE YHKHHYSHGL LNNEQLALAV NLARERGEKV VFTNGCFDIL HAGHVAYLDQ
ARKLGDRLIV AINSDESVTK LKGPGRPINS VDRRMAVLQG LASVDWVTCF TGDTPEALLE
ALQPDILVKG GDYTKEQVVG REIVQAYGGS IKVMAMVPEC STTKVIEKAR S


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