ID R7RU71_9CLOT Unreviewed; 787 AA.
AC R7RU71;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:CDF58840.1};
DE EC=3.2.1.20 {ECO:0000313|EMBL:CDF58840.1};
GN ORFNames=TCEL_01059 {ECO:0000313|EMBL:CDF58840.1};
OS Thermobrachium celere DSM 8682.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermobrachium.
OX NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF58840.1, ECO:0000313|Proteomes:UP000014923};
RN [1] {ECO:0000313|EMBL:CDF58840.1, ECO:0000313|Proteomes:UP000014923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF58840.1,
RC ECO:0000313|Proteomes:UP000014923};
RA Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.;
RT "Draft genome sequence of the hydrogen-ethanol-producing anaerobic
RT alkalithermophilic Caloramator celere.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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:CDF58840.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAVN010000101; CDF58840.1; -; Genomic_DNA.
DR RefSeq; WP_018663634.1; NZ_HF952018.1.
DR AlphaFoldDB; R7RU71; -.
DR eggNOG; COG1501; Bacteria.
DR HOGENOM; CLU_000631_7_2_9; -.
DR OrthoDB; 176168at2; -.
DR Proteomes; UP000014923; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR CDD; cd06604; GH31_glucosidase_II_MalA; 1.
DR CDD; cd14752; GH31_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF166; ALPHA-GLUCOSIDASE; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:CDF58840.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:CDF58840.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014923}.
FT DOMAIN 26..208
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 250..573
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 581..667
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 684..748
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
SQ SEQUENCE 787 AA; 92483 MW; 219C73C549F1DBD6 CRC64;
MLGKMKEYLR RDNKFIFSFE NGEGIIEVIS DTIINVFVPI KYKEHNSKAI ENLKIKEASI
LEKRFEDRVE IETNDVVVVV YDNFKVDFYD KQRNPLCLDY DGERSPFIRR GNTSIAEGEG
ISTQADFKPH KIEVIKKMLG DEYFYGFGEK TGHLNKKGYY YEMWNTDDPK PHVESYTTLY
KSIPFFITLR DNKAFGIFFD NTFKTYFDMG KENSSYYYFA ADDGNLDYYF IYGPKVVDVV
EGYTYLTGRT PLPQMWTLGY QQCRWSYAPE SRVFEIAENF RKRDIPCDVI YLDIDYMDGY
RVFTWDKEKF NDPKAFTDRL KDMGFKVVTI IDPGVKKDKG YYVYDEGIEN GYFATDKDGI
PYVNEVWPGE ALYPDFSDER VRIWWSEKQK VMIDSGVAGI WNDMNEPASF RGPLPDDVQF
KNDGFPTDHR EIHNVYGHLM SKATYEGLKR YTNKRPFVIT RACFAGTQKY STVWTGDNHS
FFEHLRMAVP MLLNLGLSGF AFCGTDVGGF QFDCTPELLS RWVQVGCFTP LFRNHSCIHT
RDQEPWAFDE KTEEINRKYI KLRYKLLPYL YDLFYQAEEK GLPIMRPLFM HYMEDKNTYE
LNDEFLFGEN ILVAPILEQG KNFRAVYLPE GAWYDYWTGE RLEGRRVVVK NAPIDVCPIY
IKAGSIIPTY KDMNYIGEIE LDEVEFEVYK GNGSYLHYED DRETFNYKEG EYNLYKLVQT
EQKDFINIDF SILHKGYNKG YNKVKIRLKN IEAGKVTIDD VEVKVEVYGK DTVVTLEPKD
SQIKFYI
//
