ID   GMHBB_ECOLI             Reviewed;         191 AA.
AC   P63228; P31546;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 1.
DT   04-NOV-2026, entry version 151.
DE   RecName: Full=D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase;
DE            EC=3.1.3.82 {ECO:0000269|PubMed:11751812, ECO:0000269|PubMed:16990279, ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050615, ECO:0000269|PubMed:31449400};
DE   AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase;
DE            Short=HBP phosphatase;
GN   Name=gmhB; Synonyms=yaeD; OrderedLocusNames=b0200, JW0196;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Miyamoto K., Inokuchi H.;
RT   "Nucleotide sequence of 5'flanking region of the ribosomal RNA gene (rrnH)
RT   in E. coli.";
RL   Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA   Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA   Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT   - 6.0 min (189,987 - 281,416bp) region.";
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   FUNCTION AS A HEPTOSE 1,7-BISPHOSPHATE PHOSPHATASE, CATALYTIC ACTIVITY,
RP   PATHWAY, DISRUPTION PHENOTYPE, AND NOMENCLATURE.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=11751812; DOI=10.1128/jb.184.2.363-369.2002;
RA   Kneidinger B., Marolda C., Graninger M., Zamyatina A., McArthur F.,
RA   Kosma P., Valvano M.A., Messner P.;
RT   "Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia
RT   coli.";
RL   J. Bacteriol. 184:363-369(2002).
RN   [7]
RP   FUNCTION AS A PHOSPHATASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP   SPECIFICITY, COFACTOR, AND PATHWAY.
RX   PubMed=16990279; DOI=10.1074/jbc.m605449200;
RA   Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V.,
RA   Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V., Arrowsmith C.H.,
RA   Koonin E.V., Edwards A.M., Yakunin A.F.;
RT   "Genome-wide analysis of substrate specificities of the Escherichia coli
RT   haloacid dehalogenase-like phosphatase family.";
RL   J. Biol. Chem. 281:36149-36161(2006).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP   AND PATHWAY.
RC   STRAIN=K12;
RX   PubMed=20050615; DOI=10.1021/bi902018y;
RA   Wang L., Huang H., Nguyen H.H., Allen K.N., Mariano P.S.,
RA   Dunaway-Mariano D.;
RT   "Divergence of biochemical function in the HAD superfamily: D-glycero-D-
RT   manno-heptose-1,7-bisphosphate phosphatase (GmhB).";
RL   Biochemistry 49:1072-1081(2010).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH DIVALENT CATIONS AND SUBSTRATE
RP   ANALOGS, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP   REACTION MECHANISM, SUBUNIT, PATHWAY, DISRUPTION PHENOTYPE, ACTIVE SITE,
RP   AND MUTAGENESIS OF ASP-11; ASP-13; CYS-107 AND LYS-111.
RX   PubMed=20050699; DOI=10.1021/bi901780j;
RA   Taylor P.L., Sugiman-Marangos S., Zhang K., Valvano M.A., Wright G.D.,
RA   Junop M.S.;
RT   "Structural and kinetic characterization of the LPS biosynthetic enzyme D-
RT   alpha,beta-D-heptose-1,7-bisphosphate phosphatase (GmhB) from Escherichia
RT   coli.";
RL   Biochemistry 49:1033-1041(2010).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SUBSTRATE ANALOGS, CATALYTIC
RP   ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF ASP-13;
RP   CYS-92; CYS-107; CYS-109; ARG-110 AND LYS-137.
RX   PubMed=20050614; DOI=10.1021/bi902019q;
RA   Nguyen H.H., Wang L., Huang H., Peisach E., Dunaway-Mariano D., Allen K.N.;
RT   "Structural determinants of substrate recognition in the HAD superfamily
RT   member D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB).";
RL   Biochemistry 49:1082-1092(2010).
CC   -!- FUNCTION: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate
CC       (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate
CC       by removing the phosphate group at the C-7 position.
CC       {ECO:0000269|PubMed:11751812, ECO:0000269|PubMed:16990279,
CC       ECO:0000269|PubMed:20050615, ECO:0000269|PubMed:31449400}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-
CC         glycero-beta-D-manno-heptose 1-phosphate + phosphate;
CC         Xref=Rhea:RHEA:28518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:60208, ChEBI:CHEBI:61593; EC=3.1.3.82;
CC         Evidence={ECO:0000269|PubMed:11751812, ECO:0000269|PubMed:16990279,
CC         ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050615,
CC         ECO:0000269|PubMed:31449400};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:16990279, ECO:0000269|PubMed:20050614};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:16990279, ECO:0000269|PubMed:20050614};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:16990279};
CC       Note=Magnesium. Can also use other divalent metal cations as manganese
CC       and cobalt. {ECO:0000269|PubMed:16990279};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:16990279};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5 uM for beta-HBP (at pH 7.5 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:16990279, ECO:0000269|PubMed:20050615,
CC         ECO:0000269|PubMed:20050699, ECO:0000269|PubMed:31449400};
CC         KM=67 uM for alpha-HBP (at pH 7.5 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:16990279, ECO:0000269|PubMed:20050615,
CC         ECO:0000269|PubMed:20050699, ECO:0000269|PubMed:31449400};
CC         KM=0.2 mM for HBP (at pH 8) {ECO:0000269|PubMed:16990279,
CC         ECO:0000269|PubMed:20050615, ECO:0000269|PubMed:20050699};
CC         KM=0.42 mM for fructose-1,6-bisphosphate (at pH 9)
CC         {ECO:0000269|PubMed:16990279, ECO:0000269|PubMed:20050615,
CC         ECO:0000269|PubMed:20050699};
CC         KM=610 uM for sedoheptulose-1,7-bisphosphate (at pH 7.5)
CC         {ECO:0000269|PubMed:16990279, ECO:0000269|PubMed:20050615,
CC         ECO:0000269|PubMed:20050699};
CC         KM=1501 uM for fructose-1,6-bisphosphate (at pH 7.5)
CC         {ECO:0000269|PubMed:16990279, ECO:0000269|PubMed:20050615,
CC         ECO:0000269|PubMed:20050699};
CC         Note=kcat is 35.7 sec(-1) and 4.6 sec(-1) with beta-HBP and alpha-HBP
CC         as substrate, respectively. Thus, the enzyme displays 100-fold more
CC         efficiency towards the beta- than the alpha-anomer (PubMed:20050615,
CC         PubMed:31449400). kcat is 0.51 sec(-1) and 0.039 sec(-1) with
CC         sedoheptulose-1,7-bisphosphate and fructose-1,6-bisphosphate as
CC         substrate, respectively (PubMed:20050615).
CC         {ECO:0000269|PubMed:20050615, ECO:0000269|PubMed:31449400};
CC       pH dependence:
CC         Optimum pH is between 6 and 7.5. {ECO:0000269|PubMed:16990279,
CC         ECO:0000269|PubMed:20050699};
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       {ECO:0000269|PubMed:11751812, ECO:0000269|PubMed:16990279,
CC       ECO:0000269|PubMed:20050615}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000269|PubMed:11751812, ECO:0000269|PubMed:20050699}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20050614,
CC       ECO:0000269|PubMed:20050699}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene result in the formation
CC       of an altered LPS core, but does not appear to disrupt full-length LPS
CC       production to an extent that the outer membrane permeability barrier is
CC       compromised. {ECO:0000269|PubMed:11751812,
CC       ECO:0000269|PubMed:20050699}.
CC   -!- MISCELLANEOUS: Phosphatase activity is essential for nucleotide
CC       activation (fourth step). Zinc ion does not directly participate in
CC       catalysis, but probably functions to stabilize the loop conformation.
CC   -!- SIMILARITY: Belongs to the GmhB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA03661.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D15061; BAA03661.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73311.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA77877.1; -; Genomic_DNA.
DR   EMBL; U70214; AAB08628.1; -; Genomic_DNA.
DR   PIR; H64744; H64744.
DR   RefSeq; NP_414742.1; NC_000913.3.
DR   RefSeq; WP_001140187.1; NZ_CP009789.1.
DR   PDB; 2GMW; X-ray; 1.50 A; A/B=1-191.
DR   PDB; 3ESQ; X-ray; 1.70 A; A=1-191.
DR   PDB; 3ESR; X-ray; 1.95 A; A=1-191.
DR   PDB; 3L1U; X-ray; 1.95 A; A/B=1-191.
DR   PDB; 3L1V; X-ray; 1.95 A; A/B=1-191.
DR   PDB; 3L8E; X-ray; 1.64 A; A/B=1-187.
DR   PDB; 3L8F; X-ray; 1.79 A; A=1-187.
DR   PDB; 3L8G; X-ray; 2.18 A; A=1-187.
DR   AlphaFoldDB; P63228; -.
DR   MDposit; P63228; -.
DR   SMR; P63228; -.
DR   BioGRID; 4259752; 293.
DR   BioGRID; 849279; 4.
DR   DIP; DIP-47998N; -.
DR   FunCoup; P63228; 305.
DR   IntAct; P63228; 11.
DR   STRING; 511145.b0200; -.
DR   jPOST; P63228; -.
DR   PaxDb; 511145-b0200; -.
DR   EnsemblBacteria; AAC73311; AAC73311; b0200.
DR   GeneID; 93777223; -.
DR   GeneID; 944879; -.
DR   KEGG; ecj:JW0196; -.
DR   KEGG; eco:b0200; -.
DR   KEGG; ecoc:C3026_00930; -.
DR   PATRIC; fig|1411691.4.peg.2078; -.
DR   EchoBASE; EB1687; -.
DR   eggNOG; COG0241; Bacteria.
DR   HOGENOM; CLU_085077_3_0_6; -.
DR   InParanoid; P63228; -.
DR   OMA; AACYIER; -.
DR   OrthoDB; 9781367at2; -.
DR   PhylomeDB; P63228; -.
DR   BioCyc; EcoCyc:EG11736-MONOMER; -.
DR   BioCyc; MetaCyc:EG11736-MONOMER; -.
DR   BRENDA; 3.1.3.82; 2026.
DR   UniPathway; UPA00356; UER00438.
DR   UniPathway; UPA00958; -.
DR   EvolutionaryTrace; P63228; -.
DR   PRO; PR:P63228; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0034200; F:D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IMP:EcoCyc.
DR   CDD; cd07503; HAD_HisB-N; 1.
DR   FunFam; 3.40.50.1000:FF:000037; D,D-heptose 1,7-bisphosphate phosphatase; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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   NCBIfam; NF006506; gmhB; 1.
DR   NCBIfam; TIGR00213; GmhB_yaeD; 1.
DR   NCBIfam; TIGR01662; HAD-SF-IIIA; 1.
DR   NCBIfam; TIGR01656; Histidinol-ppas; 1.
DR   PANTHER; PTHR42891; D-GLYCERO-BETA-D-MANNO-HEPTOSE-1,7-BISPHOSPHATE 7-PHOSPHATASE; 1.
DR   PANTHER; PTHR42891:SF1; D-GLYCERO-BETA-D-MANNO-HEPTOSE-1,7-BISPHOSPHATE 7-PHOSPHATASE; 1.
DR   Pfam; PF13242; Hydrolase_like; 1.
DR   PIRSF; PIRSF004682; GmhB; 1.
DR   SFLD; SFLDG01134; C1.5.5:_Heptose_Bisphosphate_P; 1.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cytoplasm; Hydrolase;
KW   Lipopolysaccharide biosynthesis; Magnesium; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..191
FT                   /note="D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-
FT                   phosphatase"
FT                   /id="PRO_0000209389"
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:20050699"
FT   ACT_SITE        13
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000269|PubMed:20050614,
FT                   ECO:0000269|PubMed:20050699"
FT   BINDING         11..13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20050614,
FT                   ECO:0000269|PubMed:20050699"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   BINDING         19..22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   BINDING         53..56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20050614,
FT                   ECO:0000269|PubMed:20050699"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   BINDING         110..111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   BINDING         137
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   SITE            53
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000269|PubMed:20050614,
FT                   ECO:0000269|PubMed:20050699"
FT   SITE            110
FT                   /note="Contributes to substrate recognition"
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   SITE            111
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   MUTAGEN         11
FT                   /note="D->N: Inactive."
FT                   /evidence="ECO:0000269|PubMed:20050699"
FT   MUTAGEN         13
FT                   /note="D->A: Inactive."
FT                   /evidence="ECO:0000269|PubMed:20050614,
FT                   ECO:0000269|PubMed:20050699"
FT   MUTAGEN         13
FT                   /note="D->N: Inactive."
FT                   /evidence="ECO:0000269|PubMed:20050614,
FT                   ECO:0000269|PubMed:20050699"
FT   MUTAGEN         92
FT                   /note="C->A: Reduces the catalytic efficiencies towards the
FT                   alpha and beta-anomers of HBP."
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   MUTAGEN         107
FT                   /note="C->A: More than 3-fold reduction in the affinity
FT                   binding of HBP. Reduces the catalytic efficiencies towards
FT                   the alpha and beta-anomers of HBP."
FT                   /evidence="ECO:0000269|PubMed:20050614,
FT                   ECO:0000269|PubMed:20050699"
FT   MUTAGEN         109
FT                   /note="C->A: Reduces the catalytic efficiencies towards the
FT                   alpha and beta-anomers of HBP."
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   MUTAGEN         110
FT                   /note="R->A: Significant reduction in the catalytic
FT                   efficiency of hydrolysis of the physiological substrate
FT                   HBP."
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   MUTAGEN         111
FT                   /note="K->N: Inactive."
FT                   /evidence="ECO:0000269|PubMed:20050699"
FT   MUTAGEN         137
FT                   /note="K->A: 8-fold reduction in the affinity binding of
FT                   HBP."
FT                   /evidence="ECO:0000269|PubMed:20050614"
FT   STRAND          7..10
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   TURN            14..16
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   HELIX           35..44
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   STRAND          48..54
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   HELIX           57..60
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   HELIX           65..81
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   STRAND          87..92
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   HELIX           115..124
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   STRAND          132..137
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   HELIX           138..146
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   STRAND          150..159
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   HELIX           163..168
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   STRAND          170..174
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   HELIX           176..178
FT                   /evidence="ECO:0007829|PDB:2GMW"
FT   HELIX           179..184
FT                   /evidence="ECO:0007829|PDB:2GMW"
SQ   SEQUENCE   191 AA;  21294 MW;  E7814B34A23128FA CRC64;
     MAKSVPAIFL DRDGTINVDH GYVHEIDNFE FIDGVIDAMR ELKKMGFALV VVTNQSGIAR
     GKFTEAQFET LTEWMDWSLA DRDVDLDGIY YCPHHPQGSV EEFRQVCDCR KPHPGMLLSA
     RDYLHIDMAA SYMVGDKLED MQAAVAANVG TKVLVRTGKP ITPEAENAAD WVLNSLADLP
     QAIKKQQKPA Q
//