HLDD_PARXL
ID HLDD_PARXL Reviewed; 330 AA.
AC Q13VD0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Bxeno_A3421;
GN ORFNames=Bxe_A0988;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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}.
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DR EMBL; CP000270; ABE31959.1; -; Genomic_DNA.
DR RefSeq; WP_011489473.1; NZ_CP008760.1.
DR AlphaFoldDB; Q13VD0; -.
DR SMR; Q13VD0; -.
DR STRING; 266265.Bxe_A0988; -.
DR EnsemblBacteria; ABE31959; ABE31959; Bxe_A0988.
DR KEGG; bxb:DR64_3149; -.
DR KEGG; bxe:Bxe_A0988; -.
DR PATRIC; fig|266265.5.peg.3592; -.
DR eggNOG; COG0451; Bacteria.
DR OMA; LRDFVYI; -.
DR OrthoDB; 1180629at2; -.
DR UniPathway; UPA00356; UER00440.
DR Proteomes; UP000001817; 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; Reference proteome.
FT CHAIN 1..330
FT /note="ADP-L-glycero-D-manno-heptose-6-epimerase"
FT /id="PRO_0000255725"
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; 37432 MW; 3559451174BA1518 CRC64;
MTLIVTGAAG FIGSNLVKAL NERGEQRIIA VDNLTRADKF KNLVDCEIDD YLDKTEFVER
FRRGDFGKVR AIFHEGACSD TMETDGRYMM DNNFRYSREV LDVCLAQNIQ FLYASSAATY
GGSSRFVEER EVEQPLNVYG YSKFLFDQVI RRVLPTAKSQ IAGFRYFNVY GPRETHKARM
ASVAFHNFNQ FRAEGKVKLF GEYNGYAAGE QTRDFVSVED VVKVNLFFFD NPDKSGIFNL
GSGRAQPFND IASTVVNTLR SLNNEPALSL AEQVQRGLIE YISFPDALRG KYQCFTQADQ
SKLRAAGYDA PFLSVQEGVD RYVRWLFGQV
