HLDD_BURTA
ID HLDD_BURTA Reviewed; 330 AA.
AC Q2SY18;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=BTH_I1644;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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; CP000086; ABC38509.1; -; Genomic_DNA.
DR RefSeq; WP_009889856.1; NZ_CP008785.1.
DR PDB; 4EJ0; X-ray; 2.61 A; A/B/C/D/E/F/G/H/I/J=1-330.
DR PDBsum; 4EJ0; -.
DR AlphaFoldDB; Q2SY18; -.
DR SMR; Q2SY18; -.
DR PRIDE; Q2SY18; -.
DR EnsemblBacteria; ABC38509; ABC38509; BTH_I1644.
DR KEGG; bte:BTH_I1644; -.
DR HOGENOM; CLU_007383_1_3_4; -.
DR OMA; LRDFVYI; -.
DR OrthoDB; 1180629at2; -.
DR BRENDA; 5.1.3.20; 8156.
DR UniPathway; UPA00356; UER00440.
DR Proteomes; UP000001930; Chromosome I.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Isomerase; NADP.
FT CHAIN 1..330
FT /note="ADP-L-glycero-D-manno-heptose-6-epimerase"
FT /id="PRO_0000255724"
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"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:4EJ0"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:4EJ0"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:4EJ0"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:4EJ0"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:4EJ0"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:4EJ0"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 138..153
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4EJ0"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:4EJ0"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:4EJ0"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:4EJ0"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:4EJ0"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:4EJ0"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:4EJ0"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:4EJ0"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:4EJ0"
FT HELIX 315..327
FT /evidence="ECO:0007829|PDB:4EJ0"
SQ SEQUENCE 330 AA; 36966 MW; 143D7B34D082C794 CRC64;
MTLIVTGAAG FIGANLVKAL NERGETRIIA VDNLTRADKF KNLVDCEIDD YLDKTEFVER
FARGDFGKVR AVFHEGACSD TMETDGRYMM DNNFRYSRAV LDACLAQGAQ FLYASSAAIY
GGSSRFVEER EVEAPLNVYG YSKFLFDQVI RRVMPGAKSQ IAGFRYFNVY GPRESHKGRM
ASVAFHNFNQ FRAEGKVKLF GEYSGYGPGE QTRDFVSVED VAKVNLYFFD HPEKSGIFNL
GTGRAQPFND IAATVVNTLR ALEGQPALTL AEQVEQGLVE YVPFPDALRG KYQCFTQADQ
TKLRAAGYDA PFLTVQEGVD RYVRWLFGQL
