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Database: UniProt
Entry: C2EQI6_9LACO
LinkDB: C2EQI6_9LACO
Original site: C2EQI6_9LACO 
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
//
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