ID I8VSQ7_9BACE Unreviewed; 925 AA.
AC I8VSQ7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Exo-1,4-beta-D-glucosaminidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1062_03427 {ECO:0000313|EMBL:EIY28442.1};
OS Bacteroides cellulosilyticus CL02T12C19.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=997874 {ECO:0000313|EMBL:EIY28442.1, ECO:0000313|Proteomes:UP000003741};
RN [1] {ECO:0000313|EMBL:EIY28442.1, ECO:0000313|Proteomes:UP000003741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL02T12C19 {ECO:0000313|EMBL:EIY28442.1,
RC ECO:0000313|Proteomes:UP000003741};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides cellulosilyticus CL02T12C19.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:EIY28442.1}.
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DR EMBL; AGXG01000077; EIY28442.1; -; Genomic_DNA.
DR RefSeq; WP_007217814.1; NZ_JH724087.1.
DR AlphaFoldDB; I8VSQ7; -.
DR PATRIC; fig|997874.3.peg.3516; -.
DR HOGENOM; CLU_005015_2_0_10; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000003741; 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 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 112..184
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 249..380
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 431..543
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 821..918
FT /note="Exo-beta-D-glucosaminidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF18368"
SQ SEQUENCE 925 AA; 106399 MW; 15DECE4E1052349F CRC64;
MRNILFILLL CNVMLLKAQS LELEHWRIIN SSEIADADAK VSQPSYPTTG WYQATVPTTV
LNALVKENVY PDPRIGLNNY LIPDVSDEFN ARMDLAKYNY LKSGRNPWQD PYWYRTEITL
PKSYKGKKVW LTLYGINYRA DVWVNGRLLA DKNDIVGMFR RFKLDITDYA LPGANNCVAV
KIYQVDHPGV PTPGTQLKVF GPVRGHSYDI FKDETLKISG GWDCAPVVRD RNMGIYQKVT
IEATDEVVIE NPFIVTTLPK QDTSLADVNI KLEVKNTSGK AIEGKVNALI TLVNDVKFPT
YTKHMEGYLK PIKITKKVSL GAGEKKVVEL TSEDFPSLLI KNPYLWYPNG YGEQYLHHIK
LSYNTGGKVS DTKEFDFGIR EVEVGLNRVE VDGDKAEVEY GRVYYVNGKR VFCKGGWIQP
DILLEESDKR IYDEARLMAE ANINLIGSED MPSPSETWFE SFDKYGLMWW HVFYQCYRMT
PGTETENNPL DHNLAIACVE DMMLRYRNHP SIISWVGVNE VLMNENLYRL TKEKVKSLDT
TRIYIPTTSY HWDVDALTPY LKEDLPTGTT DDGAPDYNWA PSSYFFDKVR EVYLQMFRNE
LGMPSVPMYN SLRKFIPTAE STANVNSPIF PLDSIWAEHG AWDVSNYCYR SYDNAIRTMF
GDPKTAKEYA DNAQFLSADG YRAMFEAANH RMWDITSGVM IWKINSCWPD VCWQIYDWYL
APNASYYFAR KAMEPVHVQL NANDFKISVI NASHRVLDDV KVTAKVINND MRVAWQHSQQ
LTVSPDCYKE IITVPQHGKY SYNYFVKLEL HDKAGKLLSE NLYWFYSQHM DFFWFTSMEK
PELKKEVKVS KEEGEYVFSI CLKNESARLS HFNHLTLQDA RGEEINPVFW SDNFITLFPG
DEKVITARVA VSDAGGVAPT FVLSR
//
