ID B1C363_9FIRM Unreviewed; 1277 AA.
AC B1C363;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=O-GlcNAcase BT_4395 {ECO:0000313|EMBL:EDS74621.1};
DE EC=3.2.1.52 {ECO:0000313|EMBL:EDS74621.1};
GN ORFNames=CLOSPI_01676 {ECO:0000313|EMBL:EDS74621.1};
OS Thomasclavelia spiroformis DSM 1552.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=428126 {ECO:0000313|EMBL:EDS74621.1, ECO:0000313|Proteomes:UP000004910};
RN [1] {ECO:0000313|EMBL:EDS74621.1, ECO:0000313|Proteomes:UP000004910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS74621.1,
RC ECO:0000313|Proteomes:UP000004910};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium spiroforme (DSM 1552).";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS74621.1, ECO:0000313|Proteomes:UP000004910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS74621.1,
RC ECO:0000313|Proteomes:UP000004910};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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:EDS74621.1}.
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DR EMBL; ABIK02000013; EDS74621.1; -; Genomic_DNA.
DR AlphaFoldDB; B1C363; -.
DR STRING; 428126.CLOSPI_01676; -.
DR CAZy; CBM32; Carbohydrate-Binding Module Family 32.
DR CAZy; GH84; Glycoside Hydrolase Family 84.
DR eggNOG; COG1538; Bacteria.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_280299_0_0_9; -.
DR OrthoDB; 9760892at2; -.
DR Proteomes; UP000004910; Unassembled WGS sequence.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IEA:UniProt.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 1.20.1270.90; AF1782-like; 2.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 1.20.58.460; Hyaluronidase post-catalytic domain-like; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR InterPro; IPR011496; O-GlcNAcase_cat.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR13170; O-GLCNACASE; 1.
DR PANTHER; PTHR13170:SF16; PROTEIN O-GLCNACASE; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07554; FIVAR; 3.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07555; NAGidase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF140657; Hyaluronidase post-catalytic domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:EDS74621.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EDS74621.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004910};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1277
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038519372"
FT DOMAIN 750..896
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 1277 AA; 140394 MW; 8B44302F4EB7DBFD CRC64;
MEIKMKVKRK TSKVLKSGLA ATFVFSLIAT NPSQILALSN VSNATENVTA DIYPKPQSVS
YLSDVGMSLE GEVNVVVHGE QETATLPALE KILKDNGISY VIGQEIDENK ANILVSSSKD
HCDECASEDS ALSQKEGYIL TASDDENSKG EITIVGADVD GAYYGVITLG QILDQSIDNK
FAEIVVSDYP EIEFRGFIEG FYGIPWTHEE RMSLMSDTGK YKMNTYIYAP KDDPYHRAQW
RELYPEKEAA QIAELAEAGK NSNFNFCWTI HPGDHINLYS EEDFQAALNK LEQLYELGVR
QFGVLFDDIS NNQNGTAQAN FINRIDDEFV KVKGDVKPLI TVGTRYCAAW GPSMTGYLKP
FVETLHDDVE VMWTGSGTMS NISRDIYEWP KQQIGSDKDF AVWWNYPVND YCDGKLLMGP
MNSLSTDLNN VNSFFSNPMN QAEASKVSLF SIADYTWNTD AYDYMESWHR SIKELVPEIA
EEFERFASNI SYLNDGIQMD ESAYLDEKVN ALKVALSSGT NIKEAAQVLL EEFEVILADC
DKLKDVGNEA LQTEINPFVG AYRELAIAGI NSMQALIAIE DGDSALALAR VSVAQESYDA
MSNYTVNRLE DAGERNVVVE VGTHSLKPIV RTVIDTANEK IGELLFPQTV AEMITNVDGL
ESKEVTVTDG NFILEGVNAT LNNGEYLGVI LPQARNVSQI SVTGANLADL DLEYSINGLD
WQKAEVSKDN GISMSTKVST TYVRLVNNTN APIDVTIDAL QINPIYATEA SASTNMGTYQ
TYNISNIIDS NRETKFWNNA NPSVGQYIQI DFGAAMPLYD ITAYFASGDY IKNGKVQISV
DGNEWRDVGA LEYENVGANK VSSLNANGKE ARYVRYVVTG SQDVWVQLFE VEYNQTVGDM
GNHVVKLTDS NTDGLHAKVC DQDITTAFAP TGIEDGDYLT YQMSRINNVA DLIVVQDPNN
ISEAKVSVKD INGTWREVGI LDNQVVTLPV DGRITEVKLE FDSTKPLPII YEIVATQRTA
VETDKTALKI AVDLANAITD EDLAKLIPAV ADEFKVARDE ANAVYNDASA SQVEVNNAFD
RLASAMHMLD FVKGDKTALK AFIDKVTGLE AAKYTEATWT AFETELNEAI AVYDDENAMQ
EEVNTAYSEL VTAFLNLRLI PDKSLLEDLI NQANGLNGVN YTKATFDGLT KALNEAKAVY
ENPNATQEEV DNAKVTLEKA IAGLQIVTTD NTVSTPVNNG DTTASVKTGD DVNMLGTSAG
LALLSIAGAK VLRKKED
//
