HLDD_VIBCH
ID HLDD_VIBCH Reviewed; 314 AA.
AC Q06963; O87143; Q57098; Q7DCY0;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
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}; Synonyms=gmhD, rfaD;
GN OrderedLocusNames=VC_0240;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=El Tor O17 / Serotype O1;
RX PubMed=1372980; DOI=10.1073/pnas.89.7.2566;
RA Stroeher U.H., Karageorgos L.E., Morona R., Manning P.A.;
RT "Serotype conversion in Vibrio cholerae O1.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2566-2570(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51394 / MO45 / Serotype O139;
RX PubMed=8793876; DOI=10.1111/j.1365-2958.1996.tb02518.x;
RA Bik E.M., Bunschoten A.E., Willems R.J.L., Chang A.C.Y., Mooi F.R.;
RT "Genetic organization and functional analysis of the otn DNA essential for
RT cell-wall polysaccharide synthesis in Vibrio cholerae O139.";
RL Mol. Microbiol. 20:799-811(1996).
RN [3]
RP SEQUENCE REVISION.
RA Mooi F.R.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51394 / MO45 / Serotype O139;
RX PubMed=9034311; DOI=10.1016/s0378-1119(96)00625-7;
RA Vimont S., Dumontier S., Escuyer V., Berche P.;
RT "The rfaD locus: a region of rearrangement in Vibrio cholerae O139.";
RL Gene 185:43-47(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=169-98 / Serotype O22, and ATCC 51394 / MO45 / Serotype O139;
RX PubMed=10521656; DOI=10.1016/s0378-1119(99)00344-3;
RA Yamasaki S., Shimizu T., Hoshino K., Ho S.-T., Shimada T., Nair G.B.,
RA Takeda Y.;
RT "The genes responsible for O-antigen synthesis of Vibrio cholerae O139 are
RT closely related to those of Vibrio cholerae O22.";
RL Gene 237:321-332(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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 -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
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; X59554; CAA42133.1; -; Genomic_DNA.
DR EMBL; X90547; CAA62134.1; -; Genomic_DNA.
DR EMBL; U47542; AAB02641.1; -; Genomic_DNA.
DR EMBL; AB012956; BAA33585.1; -; Genomic_DNA.
DR EMBL; AB012957; BAA36488.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF93416.1; -; Genomic_DNA.
DR PIR; JC4066; JC4066.
DR PIR; T44311; T44311.
DR RefSeq; NP_229897.1; NC_002505.1.
DR RefSeq; WP_000587795.1; NZ_LT906614.1.
DR AlphaFoldDB; Q06963; -.
DR SMR; Q06963; -.
DR STRING; 243277.VC_0240; -.
DR DNASU; 2614708; -.
DR EnsemblBacteria; AAF93416; AAF93416; VC_0240.
DR GeneID; 57738976; -.
DR KEGG; vch:VC_0240; -.
DR PATRIC; fig|243277.26.peg.221; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_1_3_6; -.
DR OMA; LRDFVYI; -.
DR BioCyc; VCHO:VC0240-MON; -.
DR UniPathway; UPA00356; UER00440.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000000584; Chromosome 1.
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:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
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..314
FT /note="ADP-L-glycero-D-manno-heptose-6-epimerase"
FT /id="PRO_0000205811"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT ACT_SITE 183
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 174
FT /ligand="substrate"
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 183
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 206..209
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT VARIANT 66..70
FT /note="FGFID -> LGPIE (in strain: 169-98 / Serotype O22)"
FT VARIANT 68
FT /note="F -> S (in strain: MO45 / ATCC 51394 / Serotype
FT O139)"
FT VARIANT 161
FT /note="D -> G (in strain: 169-98 / Serotype O22)"
FT VARIANT 211
FT /note="N -> H (in strain: 169-98 / Serotype O22)"
FT VARIANT 233
FT /note="G -> S (in strain: 169-98 / Serotype O22)"
FT VARIANT 271
FT /note="D -> E (in strain: 169-98 / Serotype O22)"
FT VARIANT 299
FT /note="S -> T (in strain: 169-98 / Serotype O22)"
SQ SEQUENCE 314 AA; 35245 MW; A377F2B9B6A6E83C CRC64;
MIIVTGGAGM IGSNIIKALN ERGITDILVV DHLKNGRKFK NLVDLQIADY MDRDDFLAQI
MAGDDFGFID AIFHEGACSA TTEWDGKYVM LNNYEYSKEL LHYCLDREIP FLYASSAATY
GETDTFIEEP QYEGALNVYG YSKQQFDNYV RRLWLDAKQH DETLSQITGF RYFNVYGPRE
QHKGSMASVA FHLNNQMNAG ENPKLFAGSE NFKRDFVYVG DVAAVNLWFL DHGVSGIFNC
GTGKAESFNE VAKAVIAFHG RGEVETIPFP DHLKGAYQEF TEADLTKLRA AGCDVQFKSV
AEGVAEYMAL INRK
