ID C2EQI6_9LACO Unreviewed; 445 AA.
AC C2EQI6;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=6-phospho-alpha-glucosidase {ECO:0000313|EMBL:EEJ71200.1};
DE EC=3.2.1.122 {ECO:0000313|EMBL:EEJ71200.1};
GN Name=aglB {ECO:0000313|EMBL:EEJ71200.1};
GN ORFNames=HMPREF0548_1932 {ECO:0000313|EMBL:EEJ71200.1};
OS Lactobacillus ultunensis DSM 16047.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=525365 {ECO:0000313|EMBL:EEJ71200.1, ECO:0000313|Proteomes:UP000005583};
RN [1] {ECO:0000313|EMBL:EEJ71200.1, ECO:0000313|Proteomes:UP000005583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16047 {ECO:0000313|EMBL:EEJ71200.1,
RC ECO:0000313|Proteomes:UP000005583};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|RuleBase:RU361152};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEJ71200.1}.
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DR EMBL; ACGU01000108; EEJ71200.1; -; Genomic_DNA.
DR RefSeq; WP_007126689.1; NZ_GG693256.1.
DR AlphaFoldDB; C2EQI6; -.
DR STRING; 525365.HMPREF0548_1932; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR PATRIC; fig|525365.8.peg.2006; -.
DR eggNOG; COG1486; Bacteria.
DR HOGENOM; CLU_045951_2_0_9; -.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000005583; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050081; F:maltose-6'-phosphate glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001088; Glyco_hydro_4.
DR InterPro; IPR022616; Glyco_hydro_4_C.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR PANTHER; PTHR32092:SF14; MALTOSE-6'-PHOSPHATE GLUCOSIDASE; 1.
DR Pfam; PF02056; Glyco_hydro_4; 1.
DR Pfam; PF11975; Glyco_hydro_4C; 1.
DR PRINTS; PR00732; GLHYDRLASE4.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|PIRSR:PIRSR601088-3};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361152};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361152};
KW Iron {ECO:0000256|PIRSR:PIRSR601088-3};
KW Manganese {ECO:0000256|PIRSR:PIRSR601088-3};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601088-3};
KW NAD {ECO:0000256|RuleBase:RU361152};
KW Nickel {ECO:0000256|PIRSR:PIRSR601088-3};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 197..420
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT ACT_SITE 172
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT SITE 111
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 445 AA; 50954 MW; 391A364F594C46DB CRC64;
MNGKKYSVVI AGGGSTFTPG FVLDLIKSQD KFPMRQLKFY DNDEERQRKI GEAVKIIMKE
RAPQIKFSYT TDPKEAFTDV DFVMGSIRVG KYHMRSLDEK IPLKYGVNGQ ETTGPGGMAY
GLRSIPAIIQ IIDWMQEYSP NAWMINYSNT IAIVAEACRR LRPNAKVINI CDMPIDDMDR
MAAICGLDSW HDIDFNYYGL NHFGWWKEVR NKKTGEDLMP KLKEYVKDHG YWVGGDYDKD
TEPSWEATFR KVADDYKMDP ETLPNNYMQY YYFPQYEVAN ADPKHTRTDE IREHRQKIVF
GECERIVKAG TAKNNIWDIS GLHSEYIVDI IHAIAYNTHE KFLANCPNNG AISNMDPDSI
VEVPALFGAD GIQPMATGKA GRFQRGLMME QQTCEKLVVD AYEQHSYQKM LQAFALNKTV
PDASVAKKIL DDMIPVNAPY WPELK
//