MNGB_ALKHC
ID MNGB_ALKHC Reviewed; 896 AA.
AC Q9KER1; Q9KER0;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Putative mannosylglycerate hydrolase;
DE EC=3.2.1.- {ECO:0000250|UniProtKB:P54746};
DE AltName: Full=2-O-(6-phospho-mannosyl)-D-glycerate hydrolase;
DE AltName: Full=Alpha-mannosidase mngB;
GN Name=mngB; OrderedLocusNames=BH0788/BH0789;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
CC -!- FUNCTION: May hydrolyze 6-phospho-mannosyl-D-glycerate to mannose-6-
CC phosphate and glycerate. {ECO:0000250|UniProtKB:P54746}.
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:0000250|UniProtKB:P54746};
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB04507.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
CC Sequence=BAB04508.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
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DR EMBL; BA000004; BAB04507.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BA000004; BAB04508.1; ALT_FRAME; Genomic_DNA.
DR PIR; D83748; D83748.
DR PIR; E83748; E83748.
DR AlphaFoldDB; Q9KER1; -.
DR SMR; Q9KER1; -.
DR STRING; 272558.10173403; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR PRIDE; Q9KER1; -.
DR EnsemblBacteria; BAB04507; BAB04507; BAB04507.
DR EnsemblBacteria; BAB04508; BAB04508; BAB04508.
DR KEGG; bha:BH0788; -.
DR KEGG; bha:BH0789; -.
DR eggNOG; COG0383; Bacteria.
DR HOGENOM; CLU_1674403_0_0_9; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
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 Gene3D; 1.20.1270.50; -; 1.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR041509; GH38_beta-1.
DR InterPro; IPR041147; GH38_C.
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; PF17677; Glyco_hydro38C2; 1.
DR Pfam; PF18438; Glyco_hydro_38; 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 3: Inferred from homology;
KW Glycosidase; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..896
FT /note="Putative mannosylglycerate hydrolase"
FT /id="PRO_0000343407"
FT ACT_SITE 125
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
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 125
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 896 AA; 102540 MW; FF55FA8327A0972B CRC64;
MKKTAHIISH SHWDREWYMP FEGHRYYLIQ LMDDLLELFA TDPNFRSFHM DGQTIMLEDY
LNIRPEKEAE VRKYIQDGRL VIGPWYILQD AFLTSAEANV RNLLYGIKDT ETFGQKREQI
GYFPDTFGIY GQAPQLLAQA GIRAAVFGRG VTPTGFNNQV QHDDYSSPFS ELIWEAPDGS
QVIGILLANW YSNGNEIPTD EDEAQTFWVK KLRDAERFAS TSQLLFMNGC DHQPVQKDVT
QAIKVAETLF PDVAFKHSNF HDYLTQIKEE LPKELQKITG ELRNQKTDGW STLVNTASAR
IYLKQANDRC QTLLTNVLEP MCLLVENKSL HRDFSEYYWK LLMENHPHDS ICGCSIDAVH
REMKTRFEKV EAGATTFIAE QGKEIAAQIN TLHDSEEAIP LVVLKTNGTS GKRVVRHKVA
MKKIYFDEMD FRHIPDRLKE IVMPTYRLEF PNKGSVPIEV QDAGVRFGYD LPRDGFRRPY
YARELEVTFS YDSDLYLGYE CGFLVPVEEK QTEARKELIG DPSMNTLENE AMKVMIHRNG
SYSILDKTTG FEYRHLGIYE DVGDIGNEYM FKASSDGVRY TTEACEASIR IIENNSLCAT
VEICQTLSVP AAADERLKEE QERLVWHPDR KAGRSKERTD ITLRTELTLE QGAKGLKVNV
NIDNTAKDHR MRALFPVERA RGNHYADSIY EIVERPNTPD PKWQNPAFDH HMQRLVSLDN
GEYGLTIATK GLHEYEIVSD SIAVTLLRSV GELGDWGLFE TPEAQCFGQN EAQFVLLPHK
GDVLSANVYV AAYDDPVEPT VIQTEQSMGP LPHATNLFQW SGEGLVLTAC KPTMDGRGMI
LRWFNPKREG EALIVQSTHF LQIYRSTILE EQIEKLGTEN VQIEVRPQEI VTLRFE
