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Database: UniProt
Entry: A0A0Q7E3V2_9CAUL
LinkDB: A0A0Q7E3V2_9CAUL
Original site: A0A0Q7E3V2_9CAUL 
ID   A0A0Q7E3V2_9CAUL        Unreviewed;       333 AA.
AC   A0A0Q7E3V2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=ADP-L-glycero-D-manno-heptose-6-epimerase {ECO:0000256|HAMAP-Rule:MF_01601};
DE            EC=5.1.3.20 {ECO:0000256|HAMAP-Rule:MF_01601};
DE   AltName: Full=ADP-L-glycero-beta-D-manno-heptose-6-epimerase {ECO:0000256|HAMAP-Rule:MF_01601};
DE            Short=ADP-glyceromanno-heptose 6-epimerase {ECO:0000256|HAMAP-Rule:MF_01601};
DE            Short=ADP-hep 6-epimerase {ECO:0000256|HAMAP-Rule:MF_01601};
DE            Short=AGME {ECO:0000256|HAMAP-Rule:MF_01601};
GN   Name=hldD {ECO:0000256|HAMAP-Rule:MF_01601};
GN   ORFNames=ASC65_03715 {ECO:0000313|EMBL:KQW83762.1};
OS   Brevundimonas sp. Root1279.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736443 {ECO:0000313|EMBL:KQW83762.1, ECO:0000313|Proteomes:UP000050923};
RN   [1] {ECO:0000313|Proteomes:UP000050923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1279 {ECO:0000313|Proteomes:UP000050923};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW83762.1, ECO:0000313|Proteomes:UP000050923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1279 {ECO:0000313|EMBL:KQW83762.1,
RC   ECO:0000313|Proteomes:UP000050923};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:0000256|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:0000256|HAMAP-
CC         Rule:MF_01601};
CC   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01601};
CC       Note=Binds 1 NADP(+) per subunit. {ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_01601}.
CC   -!- SUBUNIT: Homopentamer. {ECO:0000256|HAMAP-Rule:MF_01601}.
CC   -!- DOMAIN: Contains a large N-terminal NADP-binding domain, and a smaller
CC       C-terminal substrate-binding domain. {ECO:0000256|HAMAP-Rule:MF_01601}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. HldD subfamily. {ECO:0000256|HAMAP-Rule:MF_01601}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01601}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQW83762.1}.
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DR   EMBL; LMEB01000004; KQW83762.1; -; Genomic_DNA.
DR   RefSeq; WP_056449679.1; NZ_LMEB01000004.1.
DR   AlphaFoldDB; A0A0Q7E3V2; -.
DR   STRING; 1736443.ASC65_03715; -.
DR   UniPathway; UPA00356; UER00440.
DR   Proteomes; UP000050923; Unassembled WGS sequence.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 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   NCBIfam; TIGR02197; heptose_epim; 1.
DR   PANTHER; PTHR43103:SF3; ADP-L-GLYCERO-D-MANNO-HEPTOSE-6-EPIMERASE; 1.
DR   PANTHER; PTHR43103; NUCLEOSIDE-DIPHOSPHATE-SUGAR EPIMERASE; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_01601};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01601};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01601};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050923}.
FT   DOMAIN          6..254
FT                   /note="NAD-dependent epimerase/dehydratase"
FT                   /evidence="ECO:0000259|Pfam:PF01370"
FT   ACT_SITE        149
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT   BINDING         14..15
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT   BINDING         35..36
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT   BINDING         44
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT   BINDING         79..83
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT   BINDING         153
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT   BINDING         181
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT   BINDING         189
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT   BINDING         212..215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT   BINDING         291
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
SQ   SEQUENCE   333 AA;  37020 MW;  E6F0E213340D525C CRC64;
     MARRMIVVTG GAGFIGSNIV ARLCAEGRRD VVVCDRMESA ALGKWKNLAK HPIADFWQPE
     ELFEQLERHA DRVEAIIHMG AISSTTEADA DLIMRTNFSL SRDLWDWCVL RDARLIYASS
     AATYGDGLEG FEDDDSLGGL TALRPLNAYG YSKYLFDQYA AKQAEEGQAP SQWAGLKFFN
     VYGPNEYHKG GMKSVVAQIW PKVAAGEPVT LFRSHNPNYA DGGQLRDFVF VDDVVDIINW
     LLETPDVSGV FNAGSGQARS FLDLAHATFA AAGKEPRVEY VDTPESIRDK YQYFTEARME
     RIRAAGFGGQ STPLEEGVRR YVQNFLSGAD PYR
//
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