ID B9XM93_PEDPL Unreviewed; 791 AA.
AC B9XM93;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:EEF59086.1};
DE EC=3.2.1.20 {ECO:0000313|EMBL:EEF59086.1};
GN ORFNames=Cflav_PD2214 {ECO:0000313|EMBL:EEF59086.1};
OS Pedosphaera parvula (strain Ellin514).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF59086.1, ECO:0000313|Proteomes:UP000003688};
RN [1] {ECO:0000313|EMBL:EEF59086.1, ECO:0000313|Proteomes:UP000003688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin514 {ECO:0000313|EMBL:EEF59086.1,
RC ECO:0000313|Proteomes:UP000003688};
RX PubMed=21460084; DOI=10.1128/JB.00299-11;
RA Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A.,
RA Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Larimer F.W., Land M.L., Hauser L., Brettin T.S.,
RA Detter J.C., Han S., de Vos W.M., Janssen P.H., Smidt H.;
RT "Genome sequence of 'Pedosphaera parvula' Ellin514, an aerobic
RT Verrucomicrobial isolate from pasture soil.";
RL J. Bacteriol. 193:2900-2901(2011).
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:EEF59086.1}.
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; ABOX02000033; EEF59086.1; -; Genomic_DNA.
DR RefSeq; WP_007416932.1; NZ_ABOX02000033.1.
DR AlphaFoldDB; B9XM93; -.
DR STRING; 320771.Cflav_PD2214; -.
DR OrthoDB; 176168at2; -.
DR Proteomes; UP000003688; 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; 1.
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:SF54; BCDNA.GH04962; 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:EEF59086.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:EEF59086.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003688}.
FT DOMAIN 33..203
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 246..571
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 580..666
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 683..749
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
SQ SEQUENCE 791 AA; 89027 MW; 37312F2BF222670B CRC64;
MSKFNGATVK SIGQLQVRDI GSQAALVQSS RDTVQITALA PDLFRLRIAR ARSFSERPSW
AVSKTEWPAH VTKITQSGGE IVLATEKGRL SLNLKNGQWK LCDLHGNVAF DSLAGATGFQ
VTKAGVTLKL TADESIFGLG ETTGTYNKRG LIRELWNIDV LGHAKAIYPG LRSLYVSIPF
VISLRQGSAA GLFWDNPARQ LWDIGQTNQD NWQMTAASGE IDLYLFLGPE VGDVVARYTE
LTGRMPMPPM WALGYQQCRY SYETARRTEE VAKTFRDKKI PCDVIYLDIH HMDGYRVFTF
GKTYPKPGQL MSRLAKKGFK VVTIVDPGVK DDPDFNVLKR GLKENAFVKD PQGRKDYVGR
VWPGRSRFPD FLRRNVREWW GREQNKLLEL GVAGFWNDMN EPANFALPTK TLPEKCPHHT
DVGLMPHSDA HNLYGMQMAR ASREGALAHQ PNERPFVISR AGYAGVQRYA MVWTGDNSSV
WDHLNDAIQM FLNLSISGLA FCGGDIGGFL DNTTPELLLR WFQMATFTPF YRNHTNIKTI
DQEPWAFGPK VEAICRRYIE LRYQLLPYLY GLFSEAHRNG TPIMRPLFWH YQDDPVATAA
GDQFMLGDSL MVAPIVRQGA VARSVYLPRG EWFDFWTGQK HAGARHVLAD APIEKIPLYV
RGGAIIPMAA VQQFVDQKPL TTINLHIWPG ANGALNWYED DGVTMNYTSG DYLERQITSS
LEKNSGRIHL SVPTGRRASK VKIWRVILRG VSKHLRAKTN NRPVATHFDQ LTNICSLELP
NTNSGMEITL K
//