ID A0A1I3DAY2_9BURK Unreviewed; 975 AA.
AC A0A1I3DAY2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Beta-mannosidase {ECO:0000313|EMBL:SFH83749.1};
GN ORFNames=SAMN05192543_101200 {ECO:0000313|EMBL:SFH83749.1};
OS Paraburkholderia megapolitana.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=420953 {ECO:0000313|EMBL:SFH83749.1, ECO:0000313|Proteomes:UP000199548};
RN [1] {ECO:0000313|EMBL:SFH83749.1, ECO:0000313|Proteomes:UP000199548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 23650 {ECO:0000313|EMBL:SFH83749.1,
RC ECO:0000313|Proteomes:UP000199548};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; FOQU01000001; SFH83749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3DAY2; -.
DR STRING; 420953.SAMN05192543_101200; -.
DR OrthoDB; 9805202at2; -.
DR Proteomes; UP000199548; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR043534; EBDG/EBM.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041351; Ig_GlcNase.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43536; MANNOSYLGLYCOPROTEIN ENDO-BETA-MANNOSIDASE; 1.
DR PANTHER; PTHR43536:SF1; MANNOSYLGLYCOPROTEIN ENDO-BETA-MANNOSIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF18368; Ig_GlcNase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 3.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000199548};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..975
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011543774"
FT DOMAIN 86..223
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 292..407
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 423..557
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 836..940
FT /note="Exo-beta-D-glucosaminidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF18368"
FT REGION 40..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 975 AA; 103248 MW; C61A1B53204329BB CRC64;
MQSKQRRRFL VYSTTLAGSG WLAACGDGLQ SADRALGEAG AGATPAAPAA PVTPGAPGAP
VTPGTPGPGA IPASPPANLA ASGEIAGQWT FIAASERPTL TGAQLASAAG APGMSAATVP
GTALTSMIAN GKYPDPFYGK IVTDTIPDTL KDTNYWYRTT FATPPLRPGQ RLWLRFDGVN
YMASIWLNGA LVGTLEGAFK HGYFDVTKLV AATGGVAYLA VSAIKLDFSE GPLKPSYASG
VTRGGRNGGP TGVTLKNGPT FFCTAGWDWL PTIPDRDIGI WQPVSWFTTG AVRIADLRVD
STLADDLGSA ALQLDLSLDN RSGTSLAATV TGKIGTDIAF SHAITIPAAD QPTTITLTSA
DVPQLSLANP KLWWPNGYGE PNLYAVSVSI ALQGQVSDTR SVNIGLRRIE YSRNIGFGPQ
LSITVNKLPI LIMGGNWGLD EALKRIPRER LFNQVRLHRD ANLNLIRNWN GQSTSRDFFD
ACDTYGILVW QDFFYSTEGP APVNVTRDLD NIRDVIVHYR NHPSVLLWCG GNEGSPPAAL
VSGLDSLVKT LDPKRLCLTS SAGDTGAGAV NGYSSGGPYN WEPPSAAFSR GYGTSSTAFH
NEVGSHSIPT LEFVQAMLPP SSWECPDDFW ADRDINGNGA YLAGQQGGGG YIAMTGARYG
AIANLADFVR KAQMMNYECI RSLYEANAAV MIGPATGKIT SPATGVIMWM TNPAQPSFVW
QMYSHDLEQH ASFFAVQHGC RRINAILDAS TFDVTIANHT AKTVSGSVEM RVYNLDSTLA
GKVTQNIASV ASTSYQVAAN LGTQIAAATS DVCIVTLTLR DASGATVADN LYWCQKNGQD
TDYTLLDTMK AAAIAIRASA AELDDVTTRI TANVQNIGSS IALMTHLQLF DSSSGQRILP
AFFSDNYLNL VPGASTQIVI DVPHAKGKPV SGAGLRVDGW KLDRMNSKLG LSGVPVIFNE
RALAVTSPVS TFGKC
//
