GMHBA_CAMJE
ID GMHBA_CAMJE Reviewed; 172 AA.
AC Q6TG07; Q0P9A4; Q7BPS1; Q9PNE3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase {ECO:0000303|PubMed:31449400};
DE EC=3.1.3.83 {ECO:0000269|PubMed:31449400};
DE AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase;
DE Short=HBP phosphatase;
GN Name=gmhB; OrderedLocusNames=Cj1152c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43446 / MK104 / Serotype O:19;
RA Gilbert M.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GB11;
RX PubMed=14742567; DOI=10.1128/iai.72.2.1162-1165.2004;
RA Gilbert M., Godschalk P.C., Karwaski M.-F., Ang C.W., Van Belkum A., Li J.,
RA Wakarchuk W.W., Endtz H.P.;
RT "Evidence for acquisition of the lipooligosaccharide biosynthesis locus in
RT Campylobacter jejuni GB11, a strain isolated from a patient with Guillain-
RT Barre syndrome, by horizontal exchange.";
RL Infect. Immun. 72:1162-1165(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [4]
RP BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.
RX PubMed=12101286; DOI=10.1099/00221287-148-7-1979;
RA Valvano M.A., Messner P., Kosma P.;
RT "Novel pathways for biosynthesis of nucleotide-activated glycero-manno-
RT heptose precursors of bacterial glycoproteins and cell surface
RT polysaccharides.";
RL Microbiology 148:1979-1989(2002).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000303|PubMed:31449400};
RX PubMed=31449400; DOI=10.1021/acs.biochem.9b00548;
RA Huddleston J.P., Raushel F.M.;
RT "Biosynthesis of GDP-d-glycero-alpha-d-manno-heptose for the Capsular
RT Polysaccharide of Campylobacter jejuni.";
RL Biochemistry 58:3893-3902(2019).
CC -!- FUNCTION: Converts the D-glycero-alpha-D-manno-heptose 1,7-bisphosphate
CC intermediate into D-glycero-alpha-D-manno-heptose 1-phosphate by
CC removing the phosphate group at the C-7 position.
CC {ECO:0000269|PubMed:31449400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-
CC glycero-alpha-D-manno-heptose 1-phosphate + phosphate;
CC Xref=Rhea:RHEA:28522, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:60207, ChEBI:CHEBI:61574; EC=3.1.3.83;
CC Evidence={ECO:0000269|PubMed:31449400};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=186 uM for D-glycero-alpha-D-manno-heptose 1,7-bisphosphate (at pH
CC 7.4) {ECO:0000269|PubMed:31449400};
CC Note=kcat is 0.12 sec(-1) for D-glycero-alpha-D-manno-heptose 1,7-
CC bisphosphate. {ECO:0000269|PubMed:31449400};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-D-glycero-alpha-D-manno-
CC heptose biosynthesis; GDP-D-glycero-alpha-D-manno-heptose from D-
CC glycero-alpha-D-manno-heptose 7-phosphate: step 2/3.
CC {ECO:0000269|PubMed:31449400}.
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000305|PubMed:31449400}.
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 2/4.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LOS core biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GmhB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR82885.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAR99167.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAL35267.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF167344; AAR99167.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY422197; AAR82885.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL111168; CAL35267.1; ALT_INIT; Genomic_DNA.
DR PIR; B81320; B81320.
DR RefSeq; YP_002344543.1; NC_002163.1.
DR AlphaFoldDB; Q6TG07; -.
DR SMR; Q6TG07; -.
DR IntAct; Q6TG07; 9.
DR STRING; 192222.Cj1152c; -.
DR PaxDb; Q6TG07; -.
DR PRIDE; Q6TG07; -.
DR EnsemblBacteria; CAL35267; CAL35267; Cj1152c.
DR GeneID; 905442; -.
DR KEGG; cje:Cj1152c; -.
DR PATRIC; fig|192222.6.peg.1133; -.
DR eggNOG; COG0241; Bacteria.
DR HOGENOM; CLU_085077_3_1_7; -.
DR OMA; EHQICLE; -.
DR UniPathway; UPA00356; UER00438.
DR UniPathway; UPA00543; UER00607.
DR UniPathway; UPA00934; -.
DR UniPathway; UPA00976; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034200; F:D,D-heptose 1,7-bisphosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR004446; Heptose_bisP_phosphatase.
DR InterPro; IPR006543; Histidinol-phos.
DR InterPro; IPR013954; PNK3P.
DR PANTHER; PTHR42891; PTHR42891; 1.
DR Pfam; PF08645; PNK3P; 1.
DR PIRSF; PIRSF004682; GmhB; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00213; GmhB_yaeD; 1.
DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
PE 1: Evidence at protein level;
KW Capsule biogenesis/degradation; Carbohydrate metabolism; Cytoplasm;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..172
FT /note="D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-
FT phosphatase"
FT /id="PRO_0000209386"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 11
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 9..11
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 17..20
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 51..54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 99..100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 51
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
FT SITE 99
FT /note="Contributes to substrate recognition"
FT /evidence="ECO:0000250"
FT SITE 100
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
FT CONFLICT 137
FT /note="D -> N (in Ref. 1; AAR99167)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="N -> S (in Ref. 1; AAR99167 and 2; AAR82885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 20246 MW; AF6BB036E0829A81 CRC64;
MKTKALFLDR DGVINIDKKY VYKIEDFEFC DGIFELCRYF LARNYLLFIA TNQSGIARGY
YKESDFFKLC DYMLKEFAKQ DIKIDKIYHC PHLEGCECRK PKAGMLLKAK DEFDLDMKNS
IFIGDNLSDM QAGLNADIGT LILVNEEKKE GDFFRQFKNL KEILNFFKEK DI
