AC   MF_01601;
DC   Protein; auto
TR   HAMAP; MF_01601; -; 1; level=0
XX
Names: Heptose_epimerase
XX
ID   HLDD
DE   RecName: Full=ADP-L-glycero-D-manno-heptose-6-epimerase;
DE            EC=5.1.3.20;
DE   AltName: Full=ADP-L-glycero-beta-D-manno-heptose-6-epimerase;
DE            Short=ADP-glyceromanno-heptose 6-epimerase;
DE            Short=ADP-hep 6-epimerase;
DE            Short=AGME;
GN   Name=hldD;
XX
CC   -!- FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-
CC       manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an
CC       epimerization at carbon 6 of the heptose.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-
CC         manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967,
CC         ChEBI:CHEBI:61506; EC=5.1.3.20;
CC   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC       Note=Binds 1 NADP(+) per subunit.;
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 4/4.
CC   -!- SUBUNIT: Homopentamer.
CC   -!- DOMAIN: Contains a large N-terminal NADP-binding domain, and a smaller
CC       C-terminal substrate-binding domain.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. HldD subfamily.
XX
DR   Pfam; PF01370; Epimerase; 1; trigger=no
DR   NCBIfam; TIGR02197; heptose_epim; 1; trigger=no
XX
case <FT:18>
KW   Acetylation
end case
KW   Carbohydrate metabolism
KW   Isomerase
KW   NADP
XX
GO   GO:0008712; F:ADP-glyceromanno-heptose 6-epimerase activity
GO   GO:0005975; P:carbohydrate metabolic process
XX
FT   From: HLDD_ECOLI (P67910)
FT   BINDING         10..11
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   BINDING         31..32
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   BINDING         75..79
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   BINDING         201..204
FT                   /ligand="substrate"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT   Condition: Y
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT   Condition: K
FT   BINDING         38
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: [KQR]
FT   BINDING         53
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: [KQR]
FT   BINDING         92
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: N
FT   BINDING         144
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: K
FT   BINDING         169
FT                   /ligand="substrate"
FT   Condition: N
FT   BINDING         170
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: [VI]
FT   BINDING         178
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: K
FT   BINDING         180
FT                   /ligand="substrate"
FT   Condition: x
FT   BINDING         187
FT                   /ligand="substrate"
FT   Condition: [HKQ]
FT   BINDING         209
FT                   /ligand="substrate"
FT   Condition: [HR]
FT   BINDING         272
FT                   /ligand="substrate"
FT   Condition: Y
case <OC:Escherichia> or <OC:Shigella>
FT   MOD_RES         267
FT                   /note="N6-acetyllysine"
FT   Condition: K
end case
XX
Size: 291-340;
Related: None;
Template: P67910;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.27 2023/06/01
//