HLDD_POLNA
ID HLDD_POLNA Reviewed; 335 AA.
AC A1VR25;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=ADP-L-glycero-D-manno-heptose-6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601};
DE EC=5.1.3.20 {ECO:0000255|HAMAP-Rule:MF_01601};
DE AltName: Full=ADP-L-glycero-beta-D-manno-heptose-6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601};
DE Short=ADP-glyceromanno-heptose 6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601};
DE Short=ADP-hep 6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601};
DE Short=AGME {ECO:0000255|HAMAP-Rule:MF_01601};
GN Name=hldD {ECO:0000255|HAMAP-Rule:MF_01601}; OrderedLocusNames=Pnap_2801;
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2;
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT tar-contaminated sediment, reveals physiological and metabolic versatility
RT and evolution through extensive horizontal gene transfer.";
RL Environ. Microbiol. 11:2253-2270(2009).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_01601};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01601};
CC Note=Binds 1 NADP(+) per subunit. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01601}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000255|HAMAP-Rule:MF_01601}.
CC -!- DOMAIN: Contains a large N-terminal NADP-binding domain, and a smaller
CC C-terminal substrate-binding domain. {ECO:0000255|HAMAP-Rule:MF_01601}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. HldD subfamily. {ECO:0000255|HAMAP-Rule:MF_01601}.
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DR EMBL; CP000529; ABM38103.1; -; Genomic_DNA.
DR RefSeq; WP_011802180.1; NC_008781.1.
DR AlphaFoldDB; A1VR25; -.
DR SMR; A1VR25; -.
DR STRING; 365044.Pnap_2801; -.
DR EnsemblBacteria; ABM38103; ABM38103; Pnap_2801.
DR KEGG; pna:Pnap_2801; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_1_3_4; -.
DR OMA; LRDFVYI; -.
DR OrthoDB; 1180629at2; -.
DR UniPathway; UPA00356; UER00440.
DR Proteomes; UP000000644; Chromosome.
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 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 Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02197; heptose_epim; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Isomerase; NADP; Reference proteome.
FT CHAIN 1..335
FT /note="ADP-L-glycero-D-manno-heptose-6-epimerase"
FT /id="PRO_1000069362"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 11..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 32..33
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 75..79
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 92
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 143
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 173
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 204..207
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
SQ SEQUENCE 335 AA; 36997 MW; 601444195060E4BF CRC64;
MKIVVTGAAG FIGSNLVKGL NARGIDDIIA VDDLTQGDKF RNLADLRIAD YMDAGDFYDR
FAEGAFGHVE AVFHEGACSD TMEPDGKYMM ANNYTLSCNL FRACQNQNTR LLYASSAATY
GGSDTFSESP EFEKPLNVYG YSKLLFDQHM RRELGMRFEN AQTQVAGFRY FNVYGPREQH
KGRMASVAFH QFNQFQADGK VKLFGDYGGY GPGGQMRDFV FIDDVVAVNL WFFDHPEKSG
IFNLGTGRAQ PFNDVAIAVV NTLRQSQNAA PLSLEDAVRG GMIDYVGFPE ALVGKYQSYT
QADLGALRAA GCQHVFADVQ SGVTAYMQWL SNAKN
