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Database: UniProt
Entry: A0A139SI51_9BACT
LinkDB: A0A139SI51_9BACT
Original site: A0A139SI51_9BACT 
ID   A0A139SI51_9BACT        Unreviewed;       433 AA.
AC   A0A139SI51;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Alpha-glucosidase/alpha-galactosidase {ECO:0000313|EMBL:KXU34160.1};
DE   Flags: Fragment;
GN   ORFNames=AXK12_07715 {ECO:0000313|EMBL:KXU34160.1};
OS   Cephaloticoccus capnophilus.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC   Cephaloticoccus.
OX   NCBI_TaxID=1548208 {ECO:0000313|EMBL:KXU34160.1, ECO:0000313|Proteomes:UP000071392};
RN   [1] {ECO:0000313|EMBL:KXU34160.1, ECO:0000313|Proteomes:UP000071392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CV41 {ECO:0000313|EMBL:KXU34160.1,
RC   ECO:0000313|Proteomes:UP000071392};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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:KXU34160.1}.
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DR   EMBL; LSZP01000060; KXU34160.1; -; Genomic_DNA.
DR   RefSeq; WP_068713115.1; NZ_LSZP01000060.1.
DR   AlphaFoldDB; A0A139SI51; -.
DR   STRING; 1548208.AXK12_07715; -.
DR   OrthoDB; 9808275at2; -.
DR   Proteomes; UP000071392; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; 3.90.1820.10; AglA-like glucosidase; 1.
DR   InterPro; IPR019802; GlycHydrolase_4_CS.
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:SF6; ALPHA-GALACTOSIDASE; 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.
DR   PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 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   Metal-binding {ECO:0000256|PIRSR:PIRSR601088-3};
KW   NAD {ECO:0000256|RuleBase:RU361152};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000071392}.
FT   DOMAIN          136..357
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         111
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         141
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            51
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KXU34160.1"
SQ   SEQUENCE   433 AA;  47734 MW;  089101F84A466697 CRC64;
     LKAKVSSTLN RRTALRGANY VFCVVRTGGL EAFTHDIDIP LKYGIDQCVG DTLCAGGIMY
     GQRGIAVLLD ICKDIREVAA PNCLLLNYAN PMAMMTWAAS VYGGVRCVGL CHGVQGGIHE
     IARAIGASAK DLDVICVGIN HQTWFTEVKH NGVDVPMDRI LAGFENHPEA ARDEKVRIDM
     MRRFGYFSTE SNGHLSEYLP WYRKRPAEIK KWIDTSTNAW IHGETGGYLR YVTEGRHWFE
     EEFGEGRLPA TLEFTAENRS PEHGSYILEA METGRVYRGF FNLVNRNTIS NLPADAIIEA
     PGFVDRFGFN MPQFGDLPLG CAAVCNASIS VQRMGAHAAA TGDINLLRQA MLMDPLVSAV
     CNPPEVWQLV DEMLVAQAEW LPQYSEAIKG AKARLAKGPL IKTKAGYKGA ARKKIRTTAE
     IRAQEKGNPR GGH
//
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