ID D4DUT1_NEIEG Unreviewed; 348 AA.
AC D4DUT1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 68.
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=rfaD {ECO:0000313|EMBL:EFE48407.1};
GN Synonyms=hldD {ECO:0000256|HAMAP-Rule:MF_01601};
GN ORFNames=NEIELOOT_02764 {ECO:0000313|EMBL:EFE48407.1}, NELON_08220
GN {ECO:0000313|EMBL:AJE18877.1};
OS Neisseria elongata subsp. glycolytica ATCC 29315.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=546263 {ECO:0000313|EMBL:EFE48407.1, ECO:0000313|Proteomes:UP000005536};
RN [1] {ECO:0000313|EMBL:EFE48407.1, ECO:0000313|Proteomes:UP000005536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29315 {ECO:0000313|EMBL:EFE48407.1,
RC ECO:0000313|Proteomes:UP000005536};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000031392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29315 {ECO:0000313|Proteomes:UP000031392};
RA Veyrier F.J., Taha M.-K.;
RT "Complete Genome sequence of Neisseria elongata subsp. glycolytica.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AJE18877.1, ECO:0000313|Proteomes:UP000031392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29315 {ECO:0000313|EMBL:AJE18877.1,
RC ECO:0000313|Proteomes:UP000031392};
RX PubMed=26162030;
RA Veyrier F.J., Biais N., Morales P., Belkacem N., Guilhen C., Ranjeva S.,
RA Sismeiro O., Pehau-Arnaudet G., Rocha E.P., Werts C., Taha M.K.,
RA Boneca I.G.;
RT "Common Cell Shape Evolution of Two Nasopharyngeal Pathogens.";
RL PLoS Genet. 11:E1005338-E1005338(2015).
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}.
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DR EMBL; CP007726; AJE18877.1; -; Genomic_DNA.
DR EMBL; ADBF01000254; EFE48407.1; -; Genomic_DNA.
DR RefSeq; WP_003774947.1; NZ_CP007726.1.
DR AlphaFoldDB; D4DUT1; -.
DR STRING; 546263.NELON_08220; -.
DR KEGG; nel:NELON_08220; -.
DR PATRIC; fig|546263.7.peg.1762; -.
DR HOGENOM; CLU_007383_1_3_4; -.
DR UniPathway; UPA00356; UER00440.
DR Proteomes; UP000005536; Unassembled WGS sequence.
DR Proteomes; UP000031392; 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 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:UP000031392}.
FT DOMAIN 3..244
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT ACT_SITE 180
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 11..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 32..33
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 54
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 77..81
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 94
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 145
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 172
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 180
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 203..206
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01601"
SQ SEQUENCE 348 AA; 39707 MW; 5E204ED6065E6496 CRC64;
MTIIVTGAAG FIGSNIVKGL NARGISDIVA VDNLSNGQKF KNLADCDIAH YLDKHEFIRQ
VREHLFPFDD IEAVFHEGAC SDTMNHDGKY MMDNNYQYTL DLLDWCQDER IPFLYASSAA
VYGKGETFRE ERELEEPLNV YGYSKFLFDQ VVRRRIEEGL TAQVAGFRYF NVYGMREQHK
GRMASVAFHH FNQYRGQGYV NLFGGYDGYP EGGQSRDFVS VEDVVKVNLF FLDNPEKSGI
FNLGTGRSQP FNDLAAATVN ACRAAEGKDR LPLESLVKHG LIRYTEFPDA LKGKYQSFTQ
ADITRLRDAG YEEEFLTVEQ GVDRYVDWLF EHHSPLQSCP KSKKQFSF
//
