ID A7ILV5_XANP2 Unreviewed; 482 AA.
AC A7ILV5;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 118.
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 OrderedLocusNames=Xaut_3773 {ECO:0000313|EMBL:ABS68998.1};
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245 {ECO:0000313|EMBL:ABS68998.1, ECO:0000313|Proteomes:UP000002417};
RN [1] {ECO:0000313|EMBL:ABS68998.1, ECO:0000313|Proteomes:UP000002417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2 {ECO:0000313|Proteomes:UP000002417};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-2007) 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-heptose.
CC {ECO:0000256|ARBA:ARBA00003753, ECO:0000256|HAMAP-Rule:MF_01603}.
CC -!- FUNCTION: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-
CC phosphate at the C-1 position to selectively form D-glycero-beta-D-
CC manno-heptose-1,7-bisphosphate. {ECO:0000256|ARBA:ARBA00002319,
CC ECO:0000256|HAMAP-Rule:MF_01603}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H(+) = ADP-
CC D-glycero-beta-D-manno-heptose + diphosphate; Xref=Rhea:RHEA:27465,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:59967, ChEBI:CHEBI:61593; EC=2.7.7.70;
CC Evidence={ECO:0000256|ARBA:ARBA00000534, ECO:0000256|HAMAP-
CC Rule:MF_01603};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-
CC 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 -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004713}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-
CC heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-
CC glycero-beta-D-manno-heptose 7-phosphate: step 1/4. {ECO:0000256|HAMAP-
CC Rule:MF_01603}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-
CC heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-
CC glycero-beta-D-manno-heptose 7-phosphate: step 3/4. {ECO:0000256|HAMAP-
CC Rule:MF_01603}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01603}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC cytidylyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01603}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
CC kinase PfkB family. {ECO:0000256|HAMAP-Rule:MF_01603}.
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DR EMBL; CP000781; ABS68998.1; -; Genomic_DNA.
DR AlphaFoldDB; A7ILV5; -.
DR STRING; 78245.Xaut_3773; -.
DR KEGG; xau:Xaut_3773; -.
DR eggNOG; COG0615; Bacteria.
DR eggNOG; COG2870; Bacteria.
DR HOGENOM; CLU_021150_2_1_5; -.
DR OrthoDB; 9802794at2; -.
DR PhylomeDB; A7ILV5; -.
DR UniPathway; UPA00356; UER00437.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000002417; 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 GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR NCBIfam; TIGR02198; rfaE_dom_I; 1.
DR NCBIfam; TIGR02199; rfaE_dom_II; 1.
DR PANTHER; PTHR46969; BIFUNCTIONAL PROTEIN HLDE; 1.
DR PANTHER; PTHR46969:SF1; BIFUNCTIONAL PROTEIN HLDE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01603};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01603};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01603};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01603};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01603};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01603}; Reference proteome {ECO:0000313|Proteomes:UP000002417};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01603}.
FT DOMAIN 13..307
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
FT DOMAIN 353..447
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
FT REGION 1..325
FT /note="Ribokinase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT REGION 353..482
FT /note="Cytidylyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT ACT_SITE 270
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT BINDING 201..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
SQ SEQUENCE 482 AA; 48901 MW; 43B5BFC341E010CA CRC64;
MAGKGAAGAV GPIAVIGDVM VDRYIVGSVS RISPEAPVPV LVHGAERIVP GGAANVAANA
AALGAQVILV GLTGADPEAE ALKDALSAYR DIDLSSLVAD GGRPTITKTR VMSGRQQIVR
IDAEVLTPPA DDTVARLVAT VEEAVGRSSV VVLSDYAKGV LSDVVIGAAI AAAQAKGVPV
IVDPKRRTFE AYRGATLVTP NRLELAAATG LPDTTDAEAA LAAEAASGQF GGDVLVTRAE
KGMTLWRRNG QVLHVPAQAR EVFDVSGAGD TALAALAVSL ASGHTLETSV HFANAAAAVA
VGKIGTAVVT RAELNAALDA SVPEGAAPGA LVDRARAAAV IAGWQAAGAR VVFTNGCFDL
VHPGHVAILE AAAREGDRLV VALNTDASVQ RLKGPTRPVQ DEAARARVIG ALRCVDLVVL
FEEDTPLEII TALGPDVLVK GADYREDQVV GGDVVKSRGG RVALIPLVEG RSTSALVAKA
KG
//