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HLDD_SHEPW
ID   HLDD_SHEPW              Reviewed;         317 AA.
AC   B8CVJ3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=swp_5055;
OS   Shewanella piezotolerans (strain WP3 / JCM 13877).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP3 / JCM 13877;
RX   PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA   Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA   Bartlett D.H., Yu J., Hu S., Xiao X.;
RT   "Environmental adaptation: genomic analysis of the piezotolerant and
RT   psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT   WP3.";
RL   PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ31669.1; -; Genomic_DNA.
DR   RefSeq; WP_020914998.1; NC_011566.1.
DR   AlphaFoldDB; B8CVJ3; -.
DR   SMR; B8CVJ3; -.
DR   STRING; 225849.swp_5055; -.
DR   EnsemblBacteria; ACJ31669; ACJ31669; swp_5055.
DR   KEGG; swp:swp_5055; -.
DR   eggNOG; COG0451; Bacteria.
DR   HOGENOM; CLU_007383_1_3_6; -.
DR   OMA; LRDFVYI; -.
DR   OrthoDB; 1180629at2; -.
DR   UniPathway; UPA00356; UER00440.
DR   Proteomes; UP000000753; 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..317
FT                   /note="ADP-L-glycero-D-manno-heptose-6-epimerase"
FT                   /id="PRO_1000190411"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         10..11
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         31..32
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         38
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         53
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         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         167
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         175
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         198..201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
SQ   SEQUENCE   317 AA;  35632 MW;  2966DBE451A61DCD CRC64;
     MIVVTGAAGF IGSNLVKALN DMGRNDIIAV DDLTDGTKMF NLADCEIADY LDKDQFLEQI
     IAGEFDGKIE VIFHQGACSS TTEWDGKFMM SNNYEYSKTL LQFCDRTKCQ YIYASSASVY
     GGSEKFIEQR DLEKPLNVYA YSKFLFDQYV RQQKPNCQVA GLRYFNVYGP REQHKGGMAS
     VAFHFNNQLN ANGICRLFEG VDGYENGQQL RDFVYVEDVV KVNLWLWQNS EVSGIFNCGT
     GQAQSFNDVA NAVIAHHGKG AVEYIPFPDK LKGAYQSYTQ ADLTKLRAAG YTAEFKTVEQ
     AVPEYLSWLA TQHFIGE
 
 
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