GMHBB_ECOLI
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 03-AUG-2022, entry version 135.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 (1.50 ANGSTROMS) IN COMPLEX WITH DIVALENT CATIONS AND
RP SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, REACTION MECHANISM, SUBUNIT, PATHWAY, DISRUPTION PHENOTYPE,
RP ACTIVE SITE, 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 (1.64 ANGSTROMS) OF 1-187 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, AND
RP MUTAGENESIS OF ASP-13; 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=0.20 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_STEB01000032.1.
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 PDBsum; 2GMW; -.
DR PDBsum; 3ESQ; -.
DR PDBsum; 3ESR; -.
DR PDBsum; 3L1U; -.
DR PDBsum; 3L1V; -.
DR PDBsum; 3L8E; -.
DR PDBsum; 3L8F; -.
DR PDBsum; 3L8G; -.
DR AlphaFoldDB; P63228; -.
DR SMR; P63228; -.
DR BioGRID; 4259752; 286.
DR BioGRID; 849279; 4.
DR DIP; DIP-47998N; -.
DR IntAct; P63228; 11.
DR STRING; 511145.b0200; -.
DR jPOST; P63228; -.
DR PaxDb; P63228; -.
DR PRIDE; P63228; -.
DR EnsemblBacteria; AAC73311; AAC73311; b0200.
DR EnsemblBacteria; BAA77877; BAA77877; BAA77877.
DR GeneID; 58388385; -.
DR GeneID; 944879; -.
DR KEGG; ecj:JW0196; -.
DR KEGG; eco:b0200; -.
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; EHQICLE; -.
DR PhylomeDB; P63228; -.
DR BioCyc; EcoCyc:EG11736-MON; -.
DR BioCyc; MetaCyc:EG11736-MON; -.
DR BRENDA; 3.1.3.82; 2026.
DR UniPathway; UPA00356; UER00438.
DR UniPathway; UPA00958; -.
DR EvolutionaryTrace; P63228; -.
DR PRO; PR:P63228; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0034200; F:D,D-heptose 1,7-bisphosphate 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:0009244; P:lipopolysaccharide core region biosynthetic process; IMP:EcoCyc.
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 PANTHER; PTHR42891; PTHR42891; 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 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 13..15
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
