HLDD_PSEAB
ID HLDD_PSEAB Reviewed; 330 AA.
AC Q02QH1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 83.
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}; Synonyms=rfaD;
GN OrderedLocusNames=PA14_20890;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABJ12588.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000438; ABJ12588.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q02QH1; -.
DR SMR; Q02QH1; -.
DR PRIDE; Q02QH1; -.
DR EnsemblBacteria; ABJ12588; ABJ12588; PA14_20890.
DR KEGG; pau:PA14_20890; -.
DR HOGENOM; CLU_007383_1_3_6; -.
DR UniPathway; UPA00356; UER00440.
DR Proteomes; UP000000653; 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.
FT CHAIN 1..330
FT /note="ADP-L-glycero-D-manno-heptose-6-epimerase"
FT /id="PRO_0000323480"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT ACT_SITE 177
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 54
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 168
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 169
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 177
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 200..203
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
SQ SEQUENCE 330 AA; 37173 MW; E7A9197629ADDABF CRC64;
MSIIVTGAAG FIGSNLLQAL NRRGETDIIA VDDLTDGEQF RNLADADIAD YLDQNDFLER
YARGDFGTVR ALFHQGACAS TLESNGRYMM ENNYRYSCRL LESSLELGVP FLYASSAAVY
GAGRTFREAR QYERPLNVYG YSKFLFDQRV RRALPQARSQ VVGLRYFNVY GPREEHKGRM
ASVAYHCYQQ LRRDGRVELF GEHGGFPPGG HLRDFVAVED VARVNLHFFD HPQRSGIFNL
GSGQARTFNE VALAVINSVR ANADQPPLSL QQAVESGLLG YREFPESLRA RYQSHTCADL
ELLREAGYRD DFQSLEEGVA GYCRWLARSA
