ID A0A178MFB6_9PROT Unreviewed; 491 AA.
AC A0A178MFB6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=A6A04_05575 {ECO:0000313|EMBL:OAN46584.1};
OS Paramagnetospirillum marisnigri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=1285242 {ECO:0000313|EMBL:OAN46584.1, ECO:0000313|Proteomes:UP000078428};
RN [1] {ECO:0000313|EMBL:OAN46584.1, ECO:0000313|Proteomes:UP000078428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP-1 {ECO:0000313|EMBL:OAN46584.1,
RC ECO:0000313|Proteomes:UP000078428};
RA Koziaeva V., Dziuba M.V., Ivanov T.M., Kuznetsov B., Grouzdev D.S.;
RT "Draft genome sequence of freshwater magnetotactic bacteria
RT Magnetospirillum marisnigri SP-1 and Magnetospirillum moscoviense BB-1.";
RL Submitted (APR-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-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: 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAN46584.1}.
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DR EMBL; LWQT01000088; OAN46584.1; -; Genomic_DNA.
DR RefSeq; WP_068494709.1; NZ_LWQT01000088.1.
DR AlphaFoldDB; A0A178MFB6; -.
DR STRING; 1285242.A6A04_05575; -.
DR OrthoDB; 9802794at2; -.
DR UniPathway; UPA00356; UER00437.
DR Proteomes; UP000078428; 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; HUPs; 1.
DR HAMAP; MF_01603; HldE; 1.
DR InterPro; IPR023030; Bifunc_HldE.
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.
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:UP000078428};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01603}.
FT DOMAIN 18..314
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
FT DOMAIN 359..464
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
FT REGION 1..330
FT /note="Ribokinase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT REGION 359..491
FT /note="Cytidylyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT ACT_SITE 276
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
FT BINDING 206..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01603"
SQ SEQUENCE 491 AA; 51769 MW; 46D0BC633E0CBC1F CRC64;
MTEFSALVDR VEKLRNTGVL CIGDAMLDRF VYGSVDRISP EAPIPVVFIE RETAMLGGAG
NVVRNLVALG AAPAFVSVVG DDVAGREVTR LVGEHGEIDP CIVVETGRQT TIKTRFFASH
QQLLRADRES RMPVSDAIRE QLLTRVERLL PKAGVMVLSD YGKGVLAPPV TAELIRRAIA
AGKRVVVDPK GSDYSIYAGA TIVTPNRKEL AEATSMPVDG DEAVVAAASH LIATCDIEAV
LVTRSQDGMT LVTRDGTVNH LAAEAREVFD VSGAGDTVVA TLAAAMASGA TLVEGARLAN
VAAGIVVGKV GTAVAYAEEV VAALHHGDLA QGESKIMWSA ISAAELVDRW KRKGQKVGFT
NGCFDLLHPG HVSILTQARA ACDRLVVGLN SDASVQRLKG PTRPVQPETA RATVLSSLAM
VDLVVIFGED TPLSLIETLR PDVLVKGADY TIDTVVGAEQ VQSWGGKVVL AELVDGQSTT
NTIRRMNGGP S
//
