ID U2TC95_9FIRM Unreviewed; 323 AA.
AC U2TC95;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=HMPREF1985_01629 {ECO:0000313|EMBL:ERL04120.1};
OS Mitsuokella sp. oral taxon 131 str. W9106.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Mitsuokella.
OX NCBI_TaxID=1321781 {ECO:0000313|EMBL:ERL04120.1, ECO:0000313|Proteomes:UP000016614};
RN [1] {ECO:0000313|EMBL:ERL04120.1, ECO:0000313|Proteomes:UP000016614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W9106 {ECO:0000313|EMBL:ERL04120.1,
RC ECO:0000313|Proteomes:UP000016614};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:ERL04120.1}.
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DR EMBL; AWVT01000014; ERL04120.1; -; Genomic_DNA.
DR RefSeq; WP_021772007.1; NZ_KI273061.1.
DR AlphaFoldDB; U2TC95; -.
DR STRING; 1321781.HMPREF1985_01629; -.
DR PATRIC; fig|1321781.3.peg.1538; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_1_3_9; -.
DR OrthoDB; 9766450at2; -.
DR UniPathway; UPA00356; UER00440.
DR Proteomes; UP000016614; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000016614}.
FT DOMAIN 2..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 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 10..11
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 31..32
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 53
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 145
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 171
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 179
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 202..205
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 279
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
SQ SEQUENCE 323 AA; 36680 MW; 3D58418B306F4350 CRC64;
MIIVTGGAGF IGSNIVKELN RRGRTDILVI DDLKDGQNYR NLRGLQFIDY QHKDDFLQSI
ENDDFDGTDI DAVFHEGACS DTMEYDVNFM MRTNYEYSKL LLHFCLQHRI PFLYASSAST
YGAGKNGFRE GDECEDALNP YAFSKLVFDR YVRQVVPEAH SQIVGLRYFN VYGPQEHHKG
KMASIFYQLV DQIQETGKAR LFKGTDGYAD GEQRRDFVYV KDVVRVNLWF WENGGPSGIY
NCGTGHAHSY NEAAKAVIKA LGKGEIAYRE FPAILRGKYQ NFTEADPTHL LNAGYDGGFT
EMEAAVREYV GFLNRGGYYS YGE
//
