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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
 
 
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