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Database: UniProt
Entry: B9XM93_PEDPL
LinkDB: B9XM93_PEDPL
Original site: B9XM93_PEDPL 
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}.
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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
//
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