OGA_OCEGH
ID OGA_OCEGH Reviewed; 447 AA.
AC Q2CEE3;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Protein O-GlcNAcase {ECO:0000303|PubMed:20863279};
DE Short=OGA {ECO:0000303|PubMed:20863279};
DE EC=3.2.1.169 {ECO:0000269|PubMed:20863279};
DE AltName: Full=Beta-N-acetylglucosaminidase;
DE AltName: Full=Beta-N-acetylhexosaminidase;
DE AltName: Full=Beta-hexosaminidase;
DE AltName: Full=N-acetyl-beta-D-glucosaminidase;
DE AltName: Full=N-acetyl-beta-glucosaminidase;
GN ORFNames=OG2516_04129 {ECO:0000312|EMBL:EAR51054.1};
OS Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 /
OS HTCC2516).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Oceanicola.
OX NCBI_TaxID=314256 {ECO:0000312|EMBL:EAR51054.1};
RN [1] {ECO:0000312|EMBL:EAR51054.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516
RC {ECO:0000312|EMBL:EAR51054.1};
RX PubMed=20418400; DOI=10.1128/jb.00412-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT batsensis HTCC2597(TDelta).";
RL J. Bacteriol. 192:3549-3550(2010).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH
RP THE SUBSTRATE ANALOG PUGNAC, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516
RC {ECO:0000303|PubMed:20863279};
RX PubMed=20863279; DOI=10.1042/bj20101338;
RA Schimpl M., Schuttelkopf A.W., Borodkin V.S., van Aalten D.M.;
RT "Human OGA binds substrates in a conserved peptide recognition groove.";
RL Biochem. J. 432:1-7(2010).
CC -!- FUNCTION: Cleaves GlcNAc from O-glycosylated proteins. Can use p-
CC nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrate
CC (in vitro). {ECO:0000269|PubMed:20863279}.
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:20863279};
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:20863279};
CC -!- ACTIVITY REGULATION: Inhibited by PUGNac (O-(2-acetamido-2-deoxy-D-
CC glucopyranosylidene)amino-N-phenylcarbamate).
CC {ECO:0000269|PubMed:20863279}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.5 mM for p-nitrophenyl-GlcNAc {ECO:0000269|PubMed:20863279};
CC KM=2.9 mM for 4-methylumbelliferone-GlcNAc
CC {ECO:0000269|PubMed:20863279};
CC pH dependence:
CC Optimum pH is 7.4-7.6. {ECO:0000269|PubMed:20863279};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 84 family. {ECO:0000305}.
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DR EMBL; AAOT01000018; EAR51054.1; -; Genomic_DNA.
DR RefSeq; WP_007254354.1; NZ_CH724107.1.
DR PDB; 2XSA; X-ray; 2.00 A; A=1-447.
DR PDB; 2XSB; X-ray; 2.11 A; A=1-447.
DR PDB; 7KHS; X-ray; 1.78 A; A/B/C/D=1-447.
DR PDBsum; 2XSA; -.
DR PDBsum; 2XSB; -.
DR PDBsum; 7KHS; -.
DR AlphaFoldDB; Q2CEE3; -.
DR SMR; Q2CEE3; -.
DR STRING; 314256.OG2516_04129; -.
DR CAZy; GH84; Glycoside Hydrolase Family 84.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_001501_5_1_5; -.
DR OrthoDB; 1158117at2; -.
DR EvolutionaryTrace; Q2CEE3; -.
DR Proteomes; UP000003635; Unassembled WGS sequence.
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:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0006517; P:protein deglycosylation; IMP:UniProtKB.
DR InterPro; IPR011496; Beta-N-acetylglucosaminidase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF07555; NAGidase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..447
FT /note="Protein O-GlcNAcase"
FT /id="PRO_0000430934"
FT ACT_SITE 116
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q0TR53"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000312|PDB:2XSB"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0TR53"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0TR53"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000312|PDB:2XSB"
FT BINDING 219..221
FT /ligand="substrate"
FT /evidence="ECO:0000312|PDB:2XSB"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000312|PDB:2XSB"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000312|PDB:2XSB"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:7KHS"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:2XSA"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:7KHS"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:7KHS"
FT TURN 42..49
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 54..69
FT /evidence="ECO:0007829|PDB:7KHS"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 89..104
FT /evidence="ECO:0007829|PDB:7KHS"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 132..146
FT /evidence="ECO:0007829|PDB:7KHS"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:7KHS"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 173..181
FT /evidence="ECO:0007829|PDB:7KHS"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:7KHS"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:7KHS"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2XSB"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:7KHS"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 263..274
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 280..291
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:7KHS"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 306..315
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:7KHS"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 347..372
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 376..404
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:7KHS"
FT HELIX 427..434
FT /evidence="ECO:0007829|PDB:7KHS"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:7KHS"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:7KHS"
SQ SEQUENCE 447 AA; 50038 MW; B06BDD37C16C2F94 CRC64;
MLTGVIEGFY GRDWRRDERA TVMDWIAAAG MNTYIYGPKD DVHVRARWRV PYDAAGLARL
TELRDAAAAR GMVFYVSLAP CLDVTYSDPQ DRAALLARVD QLARAGLRNL VLLFDDIPSV
LPEADRHRFD SFAEAQADLS NMVLRHLRGA GHVVFCPTEY CGRMAGGDPR GSAYLQRLGS
TLDPAIDIFW TGPEIVSEEI VAAHLAAVGE VLRRRPVIWD NFHANDYDIR RVFAGPLGGR
SRDILPLVAG WITNPNNEAE ANFPAIHTTG AYLADPDYAP ERAIAAAVAA WQPRFRLAFG
DGAVPSDLVA LLCDLFWQPF ALGPETTRIL SALRAALTVP RPDPSDPAWR AALEDLRDLK
RRINKLFTLM TEIENRDLFH TFHNYLWEAQ EEVGHLVAYC DWLDEAPPPG AVFPATDRIH
NFYRRGFGVA VQDILQRDRQ GRYHHGV
