HLDD_AROAE
ID HLDD_AROAE Reviewed; 319 AA.
AC Q5P2S1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=AZOSEA22680;
GN ORFNames=ebA3999;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(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; CR555306; CAI08393.1; -; Genomic_DNA.
DR RefSeq; WP_011238080.1; NC_006513.1.
DR AlphaFoldDB; Q5P2S1; -.
DR SMR; Q5P2S1; -.
DR STRING; 76114.ebA3999; -.
DR EnsemblBacteria; CAI08393; CAI08393; ebA3999.
DR KEGG; eba:ebA3999; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_1_3_4; -.
DR OMA; LRDFVYI; -.
DR OrthoDB; 1180629at2; -.
DR UniPathway; UPA00356; UER00440.
DR Proteomes; UP000006552; 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; Reference proteome.
FT CHAIN 1..319
FT /note="ADP-L-glycero-D-manno-heptose-6-epimerase"
FT /id="PRO_0000255718"
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 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 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 281
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
SQ SEQUENCE 319 AA; 35591 MW; C6E7A2F9D223363C CRC64;
MIIVTGGAGF IGSNIVQGLN ARGITDILVV DDLTDGHKCL NLADADIHDY MDKDDFLRRV
EANEDFGPVE AIFHEGACSS TTEWDGRFVM AVNYEYTKSL LGWAVARKVP LLYASSASVY
GMGPTFRESR EFEHPLNMYA YSKFLFDCHL RRFAPGIDSQ VVGLRYFNVY GPREQHKGSM
ASVAYHFHNQ LNDSGRLRLF EGADGYGPGE QQRDFIHVDD VVAVNLWLLD NPGVRGIFNV
GTGRAQSFNE VAHAALSWHK GSTAGGGIDY IAFPEHLRGR YQSYTQADIT ALRQAGYEGE
FMPVEVGVPR YLEWLALRD
