MNGB_ECOLI
ID MNGB_ECOLI Reviewed; 877 AA.
AC P54746; P75753;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Mannosylglycerate hydrolase;
DE EC=3.2.1.- {ECO:0000269|PubMed:14645248};
DE AltName: Full=2-O-(6-phospho-mannosyl)-D-glycerate hydrolase;
DE AltName: Full=Alpha-mannosidase mngB;
GN Name=mngB; Synonyms=ybgG; OrderedLocusNames=b0732, JW0721;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
RX PubMed=9063979; DOI=10.1271/bbb.60.309;
RA Utsumi R., Horie T., Katoh A., Kaino Y., Tanabe H., Noda M.;
RT "Isolation and characterization of the heat-responsive genes in Escherichia
RT coli.";
RL Biosci. Biotechnol. Biochem. 60:309-315(1996).
RN [5]
RP FUNCTION AS A MANNOSIDASE, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=14645248; DOI=10.1074/jbc.m310980200;
RA Sampaio M.-M., Chevance F., Dippel R., Eppler T., Schlegel A., Boos W.,
RA Lu Y.-J., Rock C.O.;
RT "Phosphotransferase-mediated transport of the osmolyte 2-O-alpha-mannosyl-
RT D-glycerate in Escherichia coli occurs by the product of the mngA (hrsA)
RT gene and is regulated by the mngR (farR) gene product acting as
RT repressor.";
RL J. Biol. Chem. 279:5537-5548(2004).
CC -!- FUNCTION: May hydrolyze 6-phospho-mannosyl-D-glycerate to mannose-6-
CC phosphate and glycerate. {ECO:0000269|PubMed:14645248}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate + H2O = (R)-
CC glycerate + alpha-D-mannose 6-phosphate; Xref=Rhea:RHEA:27866,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16659, ChEBI:CHEBI:60331,
CC ChEBI:CHEBI:60332; Evidence={ECO:0000269|PubMed:14645248};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000250};
CC -!- INDUCTION: Repressed by MngR. Induced by mannosyl-D-glycerate.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR EMBL; U00096; AAC73826.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35398.1; -; Genomic_DNA.
DR EMBL; D64014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C64809; C64809.
DR RefSeq; NP_415260.1; NC_000913.3.
DR RefSeq; WP_000648976.1; NZ_SSZK01000033.1.
DR AlphaFoldDB; P54746; -.
DR SMR; P54746; -.
DR BioGRID; 4263542; 13.
DR IntAct; P54746; 14.
DR STRING; 511145.b0732; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR PaxDb; P54746; -.
DR PRIDE; P54746; -.
DR EnsemblBacteria; AAC73826; AAC73826; b0732.
DR EnsemblBacteria; BAA35398; BAA35398; BAA35398.
DR GeneID; 945359; -.
DR KEGG; ecj:JW0721; -.
DR KEGG; eco:b0732; -.
DR PATRIC; fig|1411691.4.peg.1541; -.
DR EchoBASE; EB3025; -.
DR eggNOG; COG0383; Bacteria.
DR HOGENOM; CLU_003442_2_1_6; -.
DR InParanoid; P54746; -.
DR OMA; VVTRPNK; -.
DR PhylomeDB; P54746; -.
DR BioCyc; EcoCyc:EG13236-MON; -.
DR BioCyc; MetaCyc:EG13236-MON; -.
DR PRO; PR:P54746; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004559; F:alpha-mannosidase activity; IDA:EcoCyc.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR Gene3D; 1.20.1270.50; -; 1.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW Glycosidase; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..877
FT /note="Mannosylglycerate hydrolase"
FT /id="PRO_0000168700"
FT ACT_SITE 126
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT CONFLICT 87..100
FT /note="WYTQTDTTIVSAES -> GIPRPIPRLFCGNP (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 877 AA; 100015 MW; B67201C6F8CB1C0A CRC64;
MKAVSRVHIT PHMHWDREWY FTTEESRILL VNNMEEILCR LEQDNEYKYY VLDGQTAILE
DYFAVKPENK DRVKKQVEAG KLIIGPWYTQ TDTTIVSAES IVRNLMYGMR DCLAFGEPMK
IGYLPDSFGM SGQLPHIYNG FGITRTMFWR GCSERHGTDK TEFLWQSSDG SEVTAQVLPL
GYAIGKYLPA DENGLRKRLD SYFDVLEKAS VTKEILLPNG HDQMPLQQNI FEVMDKLREI
YPQRKFVMSR FEEVFEKIEA QRDNLATLKG EFIDGKYMRV HRTIGSTRMD IKIAHARIEN
KIVNLLEPLA TLAWTLGFEY HHGLLEKMWK EILKNHAHDS IGCCCSDKVH REIVARFELA
EDMADNLIRF YMRKIADNMP QSDADKLVLF NLMPWPREEV INTTVRLRAS QFNLRDDRGQ
PVPYFIRHAR EIDPGLIDRQ IVHYGNYDPF MEFDIQINQI VPSMGYRTLY IEANQPGNVI
AAKSDAEGIL ENAFWQIALN EDGSLQLVDK DSGVRYDRVL QIEESSDDGD EYDYSPAKEE
WVITAANAKP QCDIIHEAWQ SRAVIRYDMA VPLNLSERSA RQSTGRVGVV LVVTLSHNSR
RIDVDINLDN QADDHRLRVL VPTPFNTDSV LADTQFGSLT RPVNDSAMNN WQQEGWKEAP
VPVWNMLNYV ALQEGRNGMA VFSEGLREFE VIGEEKKTFA ITLLRGVGLL GKEDLLLRPG
RPSGIKMPVP DSQLRGLLSC RLSLLSYTGT PTAAGVAQQA RAWLTPVQCY NKIPWDVMKL
NKAGFNVPES YSLLKMPPVG CLISALKKAE DRQEVILRLF NPAESATCDA TVAFSREVIS
CSETMMDEHI TTEENQGSNL SGPFLPGQSR TFSYRLA
