OGA_BACTN
ID OGA_BACTN Reviewed; 737 AA.
AC Q89ZI2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=O-GlcNAcase BT_4395;
DE EC=3.2.1.169 {ECO:0000269|PubMed:16565725};
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-glucosaminidase;
DE Flags: Precursor;
GN OrderedLocusNames=BT_4395;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1] {ECO:0000312|EMBL:AAO79500.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-737 IN COMPLEX WITH SUBSTRATE
RP ANALOG, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF TYR-158; ASP-263; ASP-264; TYR-303 AND ASN-393, FUNCTION,
RP AND ACTIVE SITE.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000269|PubMed:16565725};
RX PubMed=16565725; DOI=10.1038/nsmb1079;
RA Dennis R.J., Taylor E.J., Macauley M.S., Stubbs K.A., Turkenburg J.P.,
RA Hart S.J., Black G.N., Vocadlo D.J., Davies G.J.;
RT "Structure and mechanism of a bacterial beta-glucosaminidase having O-
RT GlcNAcase activity.";
RL Nat. Struct. Mol. Biol. 13:365-371(2006).
CC -!- FUNCTION: Can hydrolyze the glycosidic link of O-GlcNAcylated proteins.
CC Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as
CC substrates (in vitro). {ECO:0000269|PubMed:16565725}.
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:0000269|PubMed:16565725};
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:0000269|PubMed:16565725};
CC -!- ACTIVITY REGULATION: Inhibited by 1,2-dideoxy-2'-methyl-alpha-D-
CC glucopyranoso-[2,1-d]-delta 2'-thiazoline (NAG-thiazoline) and O-(2-
CC acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenyl-carbamate
CC (PUGNAc). Not inhibited by Streptozotocin.
CC {ECO:0000269|PubMed:16565725}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.30 mM for p-nitrophenyl-O-GlcNAc (pNP-O-GlcNAc) (at pH 7.4)
CC {ECO:0000269|PubMed:16565725};
CC KM=0.28 mM for p-nitrophenyl-O-GlcNAc (pNP-O-GlcNAc) (at pH 6.5)
CC {ECO:0000269|PubMed:16565725};
CC Vmax=3.2 umol/min/mg enzyme (at pH 7.4)
CC {ECO:0000269|PubMed:16565725};
CC Vmax=19.9 umol/min/mg enzyme (at pH 6.5)
CC {ECO:0000269|PubMed:16565725};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:16565725};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16565725}.
CC -!- INTERACTION:
CC Q89ZI2; Q89ZI2: BT_4395; NbExp=2; IntAct=EBI-15576571, EBI-15576571;
CC -!- MISCELLANEOUS: Metal-binding observed in X-ray crystal structures is
CC artifactual. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 84 family. {ECO:0000255}.
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DR EMBL; AE015928; AAO79500.1; -; Genomic_DNA.
DR RefSeq; NP_813306.1; NC_004663.1.
DR RefSeq; WP_011109237.1; NC_004663.1.
DR PDB; 2CHN; X-ray; 1.95 A; A/B=22-737.
DR PDB; 2CHO; X-ray; 1.85 A; A/B=22-737.
DR PDB; 2J47; X-ray; 1.98 A; A=22-737.
DR PDB; 2J4G; X-ray; 2.25 A; A/B=23-737.
DR PDB; 2JIW; X-ray; 1.95 A; A/B=23-737.
DR PDB; 2VVN; X-ray; 1.85 A; A/B=1-737.
DR PDB; 2VVS; X-ray; 2.24 A; A=1-737.
DR PDB; 2W4X; X-ray; 2.42 A; A=22-737.
DR PDB; 2W66; X-ray; 2.27 A; A/B=22-737.
DR PDB; 2W67; X-ray; 2.25 A; A/B=22-737.
DR PDB; 2WCA; X-ray; 2.30 A; A=22-737.
DR PDB; 2WZH; X-ray; 2.20 A; A=1-737.
DR PDB; 2WZI; X-ray; 1.90 A; A/B=1-737.
DR PDB; 2X0H; X-ray; 2.21 A; A/B=1-737.
DR PDB; 2XJ7; X-ray; 2.00 A; A/B=22-737.
DR PDB; 2XM1; X-ray; 2.00 A; A/B=22-737.
DR PDB; 2XM2; X-ray; 1.95 A; A/B=22-737.
DR PDB; 4AIS; X-ray; 2.00 A; A/B=1-737.
DR PDB; 4AIU; X-ray; 2.25 A; A=1-737.
DR PDB; 4UR9; X-ray; 2.20 A; A/B=22-737.
DR PDB; 5ABE; X-ray; 2.00 A; A/B=22-737.
DR PDB; 5ABF; X-ray; 2.10 A; A/B=22-737.
DR PDB; 5ABG; X-ray; 2.00 A; A/B=22-737.
DR PDB; 5ABH; X-ray; 1.95 A; A/B=22-737.
DR PDB; 5FKY; X-ray; 1.80 A; A/B=22-737.
DR PDB; 5FL0; X-ray; 1.95 A; A/B=22-737.
DR PDB; 5FL1; X-ray; 1.95 A; A/B=22-737.
DR PDB; 5MI4; X-ray; 1.80 A; A=23-737.
DR PDB; 5MI5; X-ray; 2.15 A; A=23-737.
DR PDB; 5MI6; X-ray; 2.00 A; A=23-737.
DR PDB; 5MI7; X-ray; 2.10 A; A=23-737.
DR PDB; 7K41; X-ray; 2.00 A; A=22-737.
DR PDB; 7OU8; X-ray; 1.50 A; AAA/BBB=1-737.
DR PDBsum; 2CHN; -.
DR PDBsum; 2CHO; -.
DR PDBsum; 2J47; -.
DR PDBsum; 2J4G; -.
DR PDBsum; 2JIW; -.
DR PDBsum; 2VVN; -.
DR PDBsum; 2VVS; -.
DR PDBsum; 2W4X; -.
DR PDBsum; 2W66; -.
DR PDBsum; 2W67; -.
DR PDBsum; 2WCA; -.
DR PDBsum; 2WZH; -.
DR PDBsum; 2WZI; -.
DR PDBsum; 2X0H; -.
DR PDBsum; 2XJ7; -.
DR PDBsum; 2XM1; -.
DR PDBsum; 2XM2; -.
DR PDBsum; 4AIS; -.
DR PDBsum; 4AIU; -.
DR PDBsum; 4UR9; -.
DR PDBsum; 5ABE; -.
DR PDBsum; 5ABF; -.
DR PDBsum; 5ABG; -.
DR PDBsum; 5ABH; -.
DR PDBsum; 5FKY; -.
DR PDBsum; 5FL0; -.
DR PDBsum; 5FL1; -.
DR PDBsum; 5MI4; -.
DR PDBsum; 5MI5; -.
DR PDBsum; 5MI6; -.
DR PDBsum; 5MI7; -.
DR PDBsum; 7K41; -.
DR PDBsum; 7OU8; -.
DR AlphaFoldDB; Q89ZI2; -.
DR SMR; Q89ZI2; -.
DR DIP; DIP-29067N; -.
DR STRING; 226186.BT_4395; -.
DR DrugBank; DB08255; (3AR,5R,6S,7R,7AR)-5-(HYDROXYMETHYL)-2-PROPYL-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D][1,3]THIAZOLE-6,7-DIOL.
DR DrugBank; DB07432; [[(3R,4R,5S,6R)-3-(butanoylamino)-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-ylidene]amino] N-phenylcarbamate.
DR DrugBank; DB00428; Streptozocin.
DR CAZy; GH84; Glycoside Hydrolase Family 84.
DR PaxDb; Q89ZI2; -.
DR PRIDE; Q89ZI2; -.
DR EnsemblBacteria; AAO79500; AAO79500; BT_4395.
DR GeneID; 60925570; -.
DR KEGG; bth:BT_4395; -.
DR PATRIC; fig|226186.12.peg.4474; -.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_001501_2_0_10; -.
DR InParanoid; Q89ZI2; -.
DR OMA; CPTEYNK; -.
DR BRENDA; 3.2.1.169; 709.
DR EvolutionaryTrace; Q89ZI2; -.
DR PRO; PR:Q89ZI2; -.
DR Proteomes; UP000001414; 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; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0006517; P:protein deglycosylation; IMP:UniProtKB.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR011496; Beta-N-acetylglucosaminidase.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF07555; NAGidase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..737
FT /note="O-GlcNAcase BT_4395"
FT /id="PRO_0000257984"
FT REGION 148..433
FT /note="Catalytic domain"
FT /evidence="ECO:0000269|PubMed:16565725"
FT ACT_SITE 264
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:16565725"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16565725"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16565725"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16565725"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16565725"
FT BINDING 358..360
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16565725"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16565725"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16565725"
FT MUTAGEN 158
FT /note="Y->F: 99% decrease in activity for pNP-O-GlcNAc."
FT /evidence="ECO:0000269|PubMed:16565725"
FT MUTAGEN 263
FT /note="D->A: 99% decrease in activity for pNP-O-GlcNAc."
FT /evidence="ECO:0000269|PubMed:16565725"
FT MUTAGEN 263
FT /note="D->N: 99% decrease in activity for pNP-O-GlcNAc."
FT /evidence="ECO:0000269|PubMed:16565725"
FT MUTAGEN 264
FT /note="D->A: 99% decrease in activity for pNP-O-GlcNAc."
FT /evidence="ECO:0000269|PubMed:16565725"
FT MUTAGEN 264
FT /note="D->N: 99% decrease in activity for pNP-O-GlcNAc."
FT /evidence="ECO:0000269|PubMed:16565725"
FT MUTAGEN 303
FT /note="Y->F: 113% increase in activity for pNP-O-GlcNAc."
FT /evidence="ECO:0000269|PubMed:16565725"
FT MUTAGEN 393
FT /note="N->A: 95% decrease in activity for pNP-O-GlcNAc."
FT /evidence="ECO:0000269|PubMed:16565725"
FT STRAND 31..41
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:5FKY"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5MI4"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:5FKY"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:5FKY"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5ABF"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 203..218
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:5FKY"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 237..252
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:5FKY"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:5ABF"
FT HELIX 314..321
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 341..351
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 402..413
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 420..431
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 436..444
FT /evidence="ECO:0007829|PDB:5FKY"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 465..477
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 483..505
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 510..538
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 542..565
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:5FKY"
FT TURN 579..581
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 582..601
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:5FKY"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:5FL1"
FT STRAND 628..631
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 634..637
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:5FL1"
FT STRAND 653..667
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 681..688
FT /evidence="ECO:0007829|PDB:5MI4"
FT STRAND 690..692
FT /evidence="ECO:0007829|PDB:5FL1"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:5MI4"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 709..714
FT /evidence="ECO:0007829|PDB:5FKY"
FT STRAND 719..721
FT /evidence="ECO:0007829|PDB:5FL1"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:5FL1"
FT STRAND 730..734
FT /evidence="ECO:0007829|PDB:5FKY"
SQ SEQUENCE 737 AA; 84485 MW; 2DD4FC69C8C94378 CRC64;
MKNNKIYLLG ACLLCAVTTF AQNVSLQPPP QQLIVQNKTI DLPAVYQLNG GEEANPHAVK
VLKELLSGKQ SSKKGMLISI GEKGDKSVRK YSRQIPDHKE GYYLSVNEKE IVLAGNDERG
TYYALQTFAQ LLKDGKLPEV EIKDYPSVRY RGVVEGFYGT PWSHQARLSQ LKFYGKNKMN
TYIYGPKDDP YHSAPNWRLP YPDKEAAQLQ ELVAVANENE VDFVWAIHPG QDIKWNKEDR
DLLLAKFEKM YQLGVRSFAV FFDDISGEGT NPQKQAELLN YIDEKFAQVK PDINQLVMCP
TEYNKSWSNP NGNYLTTLGD KLNPSIQIMW TGDRVISDIT RDGISWINER IKRPAYIWWN
FPVSDYVRDH LLLGPVYGND TTIAKEMSGF VTNPMEHAES SKIAIYSVAS YAWNPAKYDT
WQTWKDAIRT ILPSAAEELE CFAMHNSDLG PNGHGYRREE SMDIQPAAER FLKAFKEGKN
YDKADFETLQ YTFERMKESA DILLMNTENK PLIVEITPWV HQFKLTAEMG EEVLKMVEGR
NESYFLRKYN HVKALQQQMF YIDQTSNQNP YQPGVKTATR VIKPLIDRTF ATVVKFFNQK
FNAHLDATTD YMPHKMISNV EQIKNLPLQV KANRVLISPA NEVVKWAAGN SVEIELDAIY
PGENIQINFG KDAPCTWGRL EISTDGKEWK TVDLKQKESR LSAGLQKAPV KFVRFTNVSD
EEQQVYLRQF VLTIEKK
