GenomeNet

Database: UniProt
Entry: A0A1J0VFY7_9GAMM
LinkDB: A0A1J0VFY7_9GAMM
Original site: A0A1J0VFY7_9GAMM 
ID   A0A1J0VFY7_9GAMM        Unreviewed;       476 AA.
AC   A0A1J0VFY7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   05-JUN-2019, entry version 22.
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=BOX17_08020 {ECO:0000313|EMBL:APE30906.1};
OS   Halomonas aestuarii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1897729 {ECO:0000313|EMBL:APE30906.1, ECO:0000313|Proteomes:UP000181985};
RN   [1] {ECO:0000313|Proteomes:UP000181985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hb3 {ECO:0000313|Proteomes:UP000181985};
RA   Koh H.-W., Rani S., Park S.-J.;
RT   "Halolamina sediminis sp. nov., an extremely halophilic archaeon
RT   isolated from solar salt.";
RL   Submitted (NOV-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   -----------------------------------------------------------------------
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; CP018139; APE30906.1; -; Genomic_DNA.
DR   RefSeq; WP_071943430.1; NZ_CP018139.1.
DR   KEGG; hsi:BOX17_08020; -.
DR   KO; K03272; -.
DR   UniPathway; UPA00356; UER00437.
DR   Proteomes; UP000181985; 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 {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:UP000181985};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00446051, ECO:0000313|EMBL:APE30906.1};
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:UP000181985};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00061368, ECO:0000313|EMBL:APE30906.1}.
FT   DOMAIN       12    302       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    318       Ribokinase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01603}.
FT   REGION      344    476       Cytidylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01603}.
FT   ACT_SITE    264    264       {ECO:0000256|HAMAP-Rule:MF_01603}.
SQ   SEQUENCE   476 AA;  50798 MW;  1BE2C0F70A29CF37 CRC64;
     MKLDLTALEH SRLLVVGDVM LDRYWHGGTS RISPEAPVPV VRVDESEDRP GGAANVALNI
     SSLGAHAALA GLVGDDDNAD RLVSRLEDAG VNTRFARSPG IPTITKLRVM SRNQQLIRLD
     FEEGLGDVDT SGLLAQVEAA LPDCDLVILS DYGKGTLNRV EELIQLIRGA GKRVLVDPKG
     SDFRRYRGAS VITPNLGEFE AVMGHCRDDA ELAARGEAMR AELELEALLI TRSEKGMTLI
     REGHDPLHLP TRAREVYDVT GAGDTVIGVL GLALAAGHGF PEAMTLANLA AGLVVAKPGT
     ATLSIAELYT ALHGDKLAEF GVIEEAPLIE AVRAAQARGE RVVMTNGCFD ILHAGHVAYL
     EQARRLGDRL VVAVNDDASI GRLKGPKRPI NPLVRRMQVL AGLGAVDWVV PFGENTPQRL
     IEAVLPDVLV KGGDYRPEDI AGGEAVRQAG GEVKVLGFED GVSTTAMIST ILDRET
//
DBGET integrated database retrieval system