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HLDD_BURCM
ID   HLDD_BURCM              Reviewed;         330 AA.
AC   Q0BH85;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Bamb_0929;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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: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; CP000440; ABI86488.1; -; Genomic_DNA.
DR   RefSeq; WP_011656283.1; NZ_CP009798.1.
DR   AlphaFoldDB; Q0BH85; -.
DR   SMR; Q0BH85; -.
DR   STRING; 339670.Bamb_0929; -.
DR   EnsemblBacteria; ABI86488; ABI86488; Bamb_0929.
DR   GeneID; 44691612; -.
DR   KEGG; bam:Bamb_0929; -.
DR   PATRIC; fig|339670.21.peg.645; -.
DR   eggNOG; COG0451; Bacteria.
DR   OMA; LRDFVYI; -.
DR   UniPathway; UPA00356; UER00440.
DR   Proteomes; UP000000662; Chromosome 1.
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_1000069344"
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;  37060 MW;  A6520F2CF111D8CC CRC64;
     MTVIVTGAAG FIGANIVKAL NERGESRIIA VDNLTRADKF RNLVDCEIDD YLDKTEFVER
     FTRGDFGKVR AVFHEGACSD TMETDGRYMM DNNFRYSRAV LDACLAQGAQ FLYASSAAIY
     GGSTRFVEER EVEAPLNVYG YSKFLFDQVI RRVLPSAKSQ IAGFRYFNVY GPRETHKGRM
     ASVAFHNFNQ FRAEGKVKLF GEYNGYAPGE QTRDFVSVED VAKVNLFFFD HPEKSGIFNL
     GTGRAQPFND IASTVVNTLR ALDNLPPLTL AQQVEQGLIE YVAFPDALRG KYQCFTQADQ
     TKLRSAGYDA PFLTVQEGVD RYVRWLSGQV
 
 
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