ID A0A0G0E4F0_9BACT Unreviewed; 307 AA.
AC A0A0G0E4F0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=ADP-L-glycero-D-manno-heptose-6-epimerase {ECO:0000256|HAMAP-Rule:MF_01601};
DE EC=5.1.3.20 {ECO:0000256|HAMAP-Rule:MF_01601};
DE AltName: Full=ADP-L-glycero-beta-D-manno-heptose-6-epimerase {ECO:0000256|HAMAP-Rule:MF_01601};
DE Short=ADP-glyceromanno-heptose 6-epimerase {ECO:0000256|HAMAP-Rule:MF_01601};
DE Short=ADP-hep 6-epimerase {ECO:0000256|HAMAP-Rule:MF_01601};
DE Short=AGME {ECO:0000256|HAMAP-Rule:MF_01601};
GN Name=hldD {ECO:0000256|HAMAP-Rule:MF_01601};
GN ORFNames=US11_C0004G0008 {ECO:0000313|EMBL:KKQ01738.1};
OS Candidatus Roizmanbacteria bacterium GW2011_GWA2_36_23.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1618480 {ECO:0000313|EMBL:KKQ01738.1, ECO:0000313|Proteomes:UP000034344};
RN [1] {ECO:0000313|EMBL:KKQ01738.1, ECO:0000313|Proteomes:UP000034344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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. {ECO:0000256|HAMAP-
CC Rule:MF_01601}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01601};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01601};
CC Note=Binds 1 NADP(+) per subunit. {ECO:0000256|HAMAP-Rule:MF_01601};
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. {ECO:0000256|HAMAP-
CC Rule:MF_01601}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000256|HAMAP-Rule:MF_01601}.
CC -!- DOMAIN: Contains a large N-terminal NADP-binding domain, and a smaller
CC C-terminal substrate-binding domain. {ECO:0000256|HAMAP-Rule:MF_01601}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. HldD subfamily. {ECO:0000256|HAMAP-Rule:MF_01601}.
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:KKQ01738.1}.
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DR EMBL; LBRS01000004; KKQ01738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0E4F0; -.
DR STRING; 1618480.US11_C0004G0008; -.
DR PATRIC; fig|1618480.3.peg.319; -.
DR UniPathway; UPA00356; UER00440.
DR Proteomes; UP000034344; Unassembled WGS sequence.
DR GO; GO:0008712; F:ADP-glyceromanno-heptose 6-epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
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-UniRule.
DR CDD; cd05248; ADP_GME_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR HAMAP; MF_01601; Heptose_epimerase; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR011912; Heptose_epim.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR02197; heptose_epim; 1.
DR PANTHER; PTHR43103:SF3; ADP-L-GLYCERO-D-MANNO-HEPTOSE-6-EPIMERASE; 1.
DR PANTHER; PTHR43103; NUCLEOSIDE-DIPHOSPHATE-SUGAR EPIMERASE; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01601};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01601};
KW NADP {ECO:0000256|HAMAP-Rule:MF_01601}.
FT DOMAIN 4..243
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 12..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 33..34
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 55
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 76..80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 93
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 145
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 170
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 201..204
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
SQ SEQUENCE 307 AA; 35574 MW; 9A728A7E9662F808 CRC64;
MKNIIVTGGA GFIGSNLVKA LNEKGYENII IVDHLADNRK RNNLAGRKYV RYYDKKEFLT
LIERGEDFKT DVVFHLGACS DTTETNEDYM ISNNTVYSQK LFEYCIRGKA RLIYASSAAT
YGDGAQGYSD DVFELKPLNL YGYSKHLFDK WVLSTISRPP QCVGLKFFNV YGPNEYHKDK
MASVIFHGYT QVKKEGKIKL FKSYRKDFKD GQQKRDFIYV KDVIKICLFF LENGGINGIF
NVGTGKARSF LDLANSVFKS LNKQPQIKFI DMPESLKDKY QYFTEAPMNK LRQIGYKEKF
YEQWLHR
//
