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Entry: A0A1F9X9L1_9BACT
LinkDB: A0A1F9X9L1_9BACT
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ID   A0A1F9X9L1_9BACT        Unreviewed;       510 AA.
AC   A0A1F9X9L1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   08-MAY-2019, entry version 9.
DE   RecName: Full=Bifunctional protein HldE {ECO:0000256|SAAS:SAAS00232998};
GN   ORFNames=A2297_05380 {ECO:0000313|EMBL:OGS24091.1};
OS   Elusimicrobia bacterium RIFOXYB2_FULL_48_7.
OC   Bacteria; Elusimicrobia.
OX   NCBI_TaxID=1797967 {ECO:0000313|EMBL:OGS24091.1};
RN   [1] {ECO:0000313|EMBL:OGS24091.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U.,
RA   Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected
RT   biogeochemical processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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|SAAS:SAAS00232982}.
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.
CC       {ECO:0000256|SAAS:SAAS00232967}.
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|SAAS:SAAS01122503};
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|SAAS:SAAS01122458};
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|SAAS:SAAS00232968}.
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|SAAS:SAAS00232972}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|SAAS:SAAS00232964}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       cytidylyltransferase family. {ECO:0000256|SAAS:SAAS00559817}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
CC       kinase PfkB family. {ECO:0000256|SAAS:SAAS00559925}.
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:OGS24091.1}.
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DR   EMBL; MGVM01000188; OGS24091.1; -; Genomic_DNA.
DR   UniPathway; UPA00356; UER00437.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR011611; PfkB_dom.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|SAAS:SAAS00233016};
KW   Carbohydrate metabolism {ECO:0000256|SAAS:SAAS00232977};
KW   Kinase {ECO:0000256|SAAS:SAAS00446051};
KW   Multifunctional enzyme {ECO:0000256|SAAS:SAAS00446072};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00232985};
KW   Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00233001};
KW   Transferase {ECO:0000256|SAAS:SAAS00061368}.
FT   DOMAIN       34    124       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
FT   DOMAIN      221    494       PfkB. {ECO:0000259|Pfam:PF00294}.
SQ   SEQUENCE   510 AA;  56864 MW;  7589D77276E260D1 CRC64;
     MNKLEASHKI ADLPHLLKTI EGLKKSGKSI VHCHGCFDLM HIGHIKYLQS AKRKGDILVV
     TVTPDRYVKR GPGRPVFNEI HRAEAIAALD CVDYVYINHS PTATETIRMI KPDIYVKGSD
     FGSVESDPTG RLGQEQKAVK SIGGKLEFTS DEVFSSTKII KENFDIMPKH IKQFLSDFTK
     KHDVNEVTKA LGNIQKLKVL IVGEPIMDEY NFCHLMQKAS KSTTVSTLFQ SKEMYAGGAL
     CVANHLAGFV DEVGMVAMLG KELTHENFIR SHLKPNVKLF PCVRDDGPTV TKRRYLEGVF
     MQKMFEVCHF NDYPINQATE AKTISLLKKL FPKYDMVIAA DFGHGFITPN IVKLLCTKAP
     YLVAMTQSNS ANLGYNLITK YRKADYIVID HVEMRLACHQ QHGEFEPMVK KISKQLHCPN
     INTTLGHEGT LIYSHGKFSR APALSWKVID TIGAGDAVLA LTSPLTFLDV DPEIVAFIGN
     CAGALAVQYL GNKETIDYGD LTKLIQSFLK
//
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