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Database: UniProt
Entry: A0A0K9XIA5_9ACTN
LinkDB: A0A0K9XIA5_9ACTN
Original site: A0A0K9XIA5_9ACTN 
ID   A0A0K9XIA5_9ACTN        Unreviewed;       442 AA.
AC   A0A0K9XIA5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:KNB53110.1};
GN   ORFNames=AC230_10435 {ECO:0000313|EMBL:KNB53110.1};
OS   Streptomyces caatingaensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1678637 {ECO:0000313|EMBL:KNB53110.1, ECO:0000313|Proteomes:UP000037288};
RN   [1] {ECO:0000313|Proteomes:UP000037288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMAA 1322 {ECO:0000313|Proteomes:UP000037288};
RA   Santos S.N., Gacesa R., Taketani R.G., Long P.F., Melo I.S.;
RT   "Draft genome sequence of Streptomyces sp. CMAA 1322, a bacterium isolated
RT   from Caatinga biome, from dry forest semiarid of Brazil.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KNB53110.1}.
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DR   EMBL; LFXA01000004; KNB53110.1; -; Genomic_DNA.
DR   RefSeq; WP_049715890.1; NZ_LFXA01000004.1.
DR   AlphaFoldDB; A0A0K9XIA5; -.
DR   STRING; 1678637.AC230_10435; -.
DR   PATRIC; fig|1678637.3.peg.2251; -.
DR   OrthoDB; 9767022at2; -.
DR   Proteomes; UP000037288; 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; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; 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:SF5; 6-PHOSPHO-BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 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:UP000037288}.
FT   DOMAIN          193..427
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   ACT_SITE        169
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   ACT_SITE        247
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         168
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         198
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            109
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   442 AA;  47864 MW;  E5712C7A58D25085 CRC64;
     MRLTILGGGG FRVPLVHRAL LDDARRDAPG RVTELVLFDT DSMRARVITS VLTAQADGVP
     GAPSVRVARD LDEALRGADF VFSAIRVGGT AGRVRDERIA LDEGVLGQET VGAGGVLYGL
     RTLPVALDIA RRVAENAPDA WVINFTNPAG MVTEAMASVL GERVIGICDS PVGLVRRAAR
     AAGADPDRVE YDYVGLNHLG WLRSLTLDGR ELLPGLLENP EALASFEEGK LFGSAWLRAL
     GALPNEYLHY YYFRRETLSA VRESAQTRGE FLDRQQADFF RRAAAASSPA AAYDLWRRTR
     LEREETYGAD SRAASGGWRR DSCDLEGGGY ERVALALMRG VAGDERSRLI LDVRNEGTVP
     ELDREAVIET VCEVSAKGAR PLPCAPLRED QLGLMFQVKA VERGVIDAAA GRDPRAALRA
     LALHPLVDSP AVAARILERA EV
//
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