GenomeNet

Database: UniProt
Entry: A0A161QKV8_9BRAD
LinkDB: A0A161QKV8_9BRAD
Original site: A0A161QKV8_9BRAD 
ID   A0A161QKV8_9BRAD        Unreviewed;       489 AA.
AC   A0A161QKV8;
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=A4A58_17805 {ECO:0000313|EMBL:KZD20594.1};
OS   Tardiphaga robiniae.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Tardiphaga.
OX   NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD20594.1, ECO:0000313|Proteomes:UP000076574};
RN   [1] {ECO:0000313|EMBL:KZD20594.1, ECO:0000313|Proteomes:UP000076574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vaf07 {ECO:0000313|EMBL:KZD20594.1,
RC   ECO:0000313|Proteomes:UP000076574};
RA   Kopat V., Chirak E., Kimeklis A., Andronov E.;
RT   "Microsymbionts genomes from the relict species Vavilovia formosa
RT   (Stev.) Fed.";
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:KZD20594.1}.
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; LVYV01000055; KZD20594.1; -; Genomic_DNA.
DR   RefSeq; WP_068738150.1; NZ_LVYV01000055.1.
DR   EnsemblBacteria; KZD20594; KZD20594; A4A58_17805.
DR   BioCyc; GCF_001618955:A4A58_RS27195-MONOMER; -.
DR   UniPathway; UPA00356; UER00437.
DR   Proteomes; UP000076574; 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:UP000076574};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00446051, ECO:0000313|EMBL:KZD20594.1};
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:UP000076574};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01603,
KW   ECO:0000256|SAAS:SAAS00061368, ECO:0000313|EMBL:KZD20594.1}.
FT   DOMAIN       15    314       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   DOMAIN      358    450       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
FT   NP_BIND     205    208       ATP. {ECO:0000256|HAMAP-Rule:MF_01603}.
FT   REGION        1    329       Ribokinase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01603}.
FT   REGION      357    489       Cytidylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01603}.
FT   ACT_SITE    275    275       {ECO:0000256|HAMAP-Rule:MF_01603}.
SQ   SEQUENCE   489 AA;  51983 MW;  6BCB06FD516D9B71 CRC64;
     MFDFDALSHA IADQTVLCVG DLMLDEFVYG EVSRISPEAP APVIAVQRSE INIGGAGNVA
     RNIAALGAKC IFVGLVGEDD AGATLKNALA QEPLIEALLV TDSSRPTTRK VRFVSEHFST
     HMLRADWELA APASAAIEKQ LIDTILPQLA RVDIVLLSDY AKGVLTARVI RNVIDAAKKL
     GKRVIVDPKS ANFAIYRGAT LLTPNRKEFV EATRSRADSD INIATAAQEA MILADCAAML
     VTQSEHGMTL VPRDGEPIHV PALPVRVRDV SGAGDTVAAM LAVALAAGAD WEAALRAATA
     AAAVAVSKKG TAVVTPSELR RRILPHAFLA AEEKIVASTE LNAQLADWRK QQLRIGFTNG
     CFDILHPGHV KVLTAARATC DRLIVGLNSD ASVKRLKGEG RPVQDERARA EVLAALEAVD
     LVVIFEEDTP LNLITQIAPA TLVKGGDYTR EQVVGHEVVA ANGGEVILID ILQGHSTTSL
     VERARSGQS
//
DBGET integrated database retrieval system