OGA_CLOPE
ID OGA_CLOPE Reviewed; 1001 AA.
AC Q8XL08;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=O-GlcNAcase NagJ;
DE EC=3.2.1.169 {ECO:0000250|UniProtKB:Q0TR53};
DE AltName: Full=Beta-N-acetylglucosaminidase;
DE AltName: Full=Beta-N-acetylhexosaminidase;
DE AltName: Full=Beta-hexosaminidase;
DE AltName: Full=Hexosaminidase B;
DE AltName: Full=N-acetyl-beta-D-glucosaminidase;
DE AltName: Full=N-acetyl-beta-glucosaminidase;
DE Flags: Precursor;
GN Name=nagJ {ECO:0000312|EMBL:BAB80940.1}; OrderedLocusNames=CPE1234;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1] {ECO:0000312|EMBL:BAB80940.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC -!- FUNCTION: Binds carbohydrates. Capable of hydrolyzing the glycosidic
CC link of O-GlcNAcylated proteins. Can bind and deglycosylate O-
CC glycosylated peptides from mammals. Can use p-nitrophenyl-beta-GlcNAc
CC and 4-methylumbelliferone-GlcNAc as substrates (in vitro).
CC {ECO:0000250|UniProtKB:Q0TR53}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H2O =
CC L-seryl-[protein] + N-acetyl-D-glucosamine; Xref=Rhea:RHEA:48876,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:90838, ChEBI:CHEBI:506227;
CC EC=3.2.1.169; Evidence={ECO:0000250|UniProtKB:Q0TR53};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H2O
CC = L-threonyl-[protein] + N-acetyl-D-glucosamine;
CC Xref=Rhea:RHEA:48892, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:90840,
CC ChEBI:CHEBI:506227; EC=3.2.1.169;
CC Evidence={ECO:0000250|UniProtKB:Q0TR53};
CC -!- INTERACTION:
CC Q8XL08; P26831: nagH; NbExp=3; IntAct=EBI-15722628, EBI-15722600;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 84 family. {ECO:0000255}.
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DR EMBL; BA000016; BAB80940.1; -; Genomic_DNA.
DR RefSeq; WP_003467250.1; NC_003366.1.
DR AlphaFoldDB; Q8XL08; -.
DR BMRB; Q8XL08; -.
DR SMR; Q8XL08; -.
DR DIP; DIP-46266N; -.
DR IntAct; Q8XL08; 3.
DR STRING; 195102.gene:10490497; -.
DR DrugBank; DB04699; gamma-Butyrolactone.
DR CAZy; CBM32; Carbohydrate-Binding Module Family 32.
DR CAZy; GH84; Glycoside Hydrolase Family 84.
DR EnsemblBacteria; BAB80940; BAB80940; BAB80940.
DR KEGG; cpe:CPE1234; -.
DR HOGENOM; CLU_001501_2_0_9; -.
DR OMA; ARMEEAC; -.
DR BRENDA; 3.2.1.52; 1503.
DR EvolutionaryTrace; Q8XL08; -.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0102167; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0102571; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0102166; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IEA:UniProt.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR011496; Beta-N-acetylglucosaminidase.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR002102; Cohesin_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
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; IPR013783; Ig-like_fold.
DR Pfam; PF00963; Cohesin; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07555; NAGidase; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1001
FT /note="O-GlcNAcase NagJ"
FT /id="PRO_0000257986"
FT DOMAIN 916..1001
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 179..469
FT /note="Catalytic domain"
FT /evidence="ECO:0000250|UniProtKB:Q0TR53"
FT COILED 515..543
FT /evidence="ECO:0000255"
FT COILED 573..597
FT /evidence="ECO:0000255"
FT ACT_SITE 298
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q0TR53, ECO:0000305"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0TR53"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0TR53"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0TR53"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0TR53"
FT BINDING 394..396
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q2CEE3"
FT BINDING 401
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q2CEE3"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0TR53"
SQ SEQUENCE 1001 AA; 111109 MW; E0C0A1575073946E CRC64;
MKRKMLKRLL TSAFACMFIA NGLITTTVRA VGPKTGEENQ VLVPNLNPTP ENLEVVGDGF
KITSSINLVG EEEADENAVN ALREFLTANN IEINSENDPN STTLIIGEVD DDIPELDEAL
NGTTAENLKE EGYALVSNDG KIAIEGKDGD GTFYGVQTFK QLVKESNIPE VNITDYPTVS
ARGIVEGFYG TPWTHKDRLD QIKFYGENKL NTYIYAPKDD PYHREKWREP YPENEMQRMQ
ELIDASAENK VDFVFGISPG IDIRFDGEAG EEDFNHLIAK AESLYDMGVR SFAIYWDDIQ
DKSAAKHAQV LNRFNEEFVK AKGDVKPLIT VPTEYDTGAM VSNGQPRTYT RIFAETVDPS
IEVMWTGPGV VTNEIPLSDA QLISGIYNRN MAVWWNYPVT DYFKGKLALG PMHGLDKGLN
QYVDFFTVNP MEHAELSKIS IHTAADYSWN MDNYDYDKAW NRAIDMLYGD LAEDMKVFAN
HSTRMDNKTW AKSGREDAPE LRAKMDELWN KLSSKEDASA LIEELYGEFA RMEEACNNLK
ANLPEVALEE CSRQLDELIT LAQGDKASLD MIVAQLNEDT EAYESAKEIA QNKLNTALSS
FAVISEKVAQ SFIQEALSFD LTLINPRTVK ITASSEETSG ENAPASFASD GDMNTFWHSK
WSSPAHEGPH HLTLELDNVY EINKVKYAPR QDSKNGRITG YKVSVSLDGE NFTEVKTGTL
EDNAAIKFIE FDSVDAKYVR LDVTDSVSDQ ANGRGKFATA AEVNVHGKLK EAAEVTGSVS
LEALEEVQVG ENIEVGVGID ELVNAEAFAY DFTLNYDENA FEYVEAISDD GVFVNAKKIE
DGKVRVLVSS LTGEPLPAKE VLAKVVLRAE AKTEGSNLSV TNSSVGDGEG LVHEIAGTEK
TVNIIEGTSP EIVVNPVRDF KASEINKKNV TVTWTEPETT EGLEGYILYK DGKKVAEIGK
DETSYTFKKL NRHTIYNFKI AAKYSNGEVS SKESLTLRTA R
