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Database: UniProt
Entry: G8PQE2_PSEUV
LinkDB: G8PQE2_PSEUV
Original site: G8PQE2_PSEUV 
ID   G8PQE2_PSEUV            Unreviewed;       428 AA.
AC   G8PQE2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AEV38456.1};
GN   OrderedLocusNames=PSE_3952 {ECO:0000313|EMBL:AEV38456.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Stappiaceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV38456.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT   interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV38456.1, ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV38456.1,
RC   ECO:0000313|Proteomes:UP000005634};
RX   PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA   Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT   for symbiosis.";
RL   Environ. Microbiol. 15:2095-2113(2013).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family.
CC       {ECO:0000256|ARBA:ARBA00010833}.
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DR   EMBL; CP003147; AEV38456.1; -; Genomic_DNA.
DR   RefSeq; WP_014286360.1; NC_016642.1.
DR   AlphaFoldDB; G8PQE2; -.
DR   STRING; 911045.PSE_3952; -.
DR   KEGG; psf:PSE_3952; -.
DR   eggNOG; COG1626; Bacteria.
DR   HOGENOM; CLU_015270_1_0_5; -.
DR   Proteomes; UP000005634; Chromosome.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:InterPro.
DR   GO; GO:0004573; F:Glc3Man9GlcNAc2 oligosaccharide glucosidase activity; IEA:InterPro.
DR   GO; GO:0005991; P:trehalose metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001661; Glyco_hydro_37.
DR   InterPro; IPR004888; Glycoside_hydrolase_63.
DR   PANTHER; PTHR10412; MANNOSYL-OLIGOSACCHARIDE GLUCOSIDASE; 1.
DR   PANTHER; PTHR10412:SF11; MANNOSYL-OLIGOSACCHARIDE GLUCOSIDASE; 1.
DR   Pfam; PF01204; Trehalase; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
SQ   SEQUENCE   428 AA;  48430 MW;  93734E78D9C1B13E CRC64;
     MSAQLDNQAI SILKENDLGG YTIPTKGLYP YQWNWDSAFV ALGFATFNMN RAWEEIELLF
     EGQWDDGMVP HIIFRKDDPS YFPGPSVWGT TNPKIPTSGH SQPPVAATVV RRLFEQDTSA
     AGKEKIKALF PKLLAWHRWY HTYRDPEGHG VIAIMHPWES GRDNLPDWDN AASHVDISDI
     GEYTRKDTSH VNPEMRPKKI DYDRYLAIVK FGRDNNWDPK IVAEQCPFFV ADPGNTFILL
     RADRDLLAMA EALGETEAAE ELKGWIALTE KGIAKLWNEE KQAFCTYDLR NDVLGDGISS
     ASFLAPYAGI REEKYINPTR EHFDRIAAKV NYTMPSYDPD HPLFESMRYW RGPVWGIINY
     LIATGFAELG DTARAERLRT DTVALIEKSD FAEYFDPITG EGAGGNSFSW TSAIWLTWAT
     PSLTAKAA
//
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