KEGG   ENZYME: 3.2.1.169Help
Entry
EC 3.2.1.169                Enzyme                                 

Name
protein O-GlcNAcase;
OGA;
glycoside hydrolase O-GlcNAcase;
O-GlcNAcase;
BtGH84;
O-GlcNAc hydrolase
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
BRITE hierarchy
Sysname
[protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine/threonine N-acetylglucosaminyl hydrolase
Reaction(IUBMB)
(1) [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine  [RN:R09672];
(2) [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-theronine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine [RN:R09673]
Reaction(KEGG)
Substrate
[protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine [CPD:C19802];
H2O [CPD:C00001];
[protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-theronine
Product
[protein]-L-serine [CPD:C02189];
N-acetyl-D-glucosamine [CPD:C00140];
[protein]-L-threonine [CPD:C19803]
Comment
Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins.
History
EC 3.2.1.169 created 2011
Orthology
K15719  protein O-GlcNAcase / histone acetyltransferase
Genes
HSA: 10724(OGA)
PTR: 450691(MGEA5)
PPS: 100979884(MGEA5)
GGO: 101124144(MGEA5)
PON: 100459796(MGEA5)
NLE: 100586192(MGEA5)
MCC: 712370(MGEA5)
MCF: 102142813(MGEA5)
CSAB: 103216418(MGEA5)
RRO: 104656503(MGEA5)
RBB: 108515105(MGEA5)
CJC: 100392114(MGEA5)
SBQ: 101029093(MGEA5)
MMU: 76055(Mgea5)
RNO: 154968(Mgea5)
CGE: 100751586(Mgea5)
NGI: 103744007(Mgea5)
HGL: 101702515(Mgea5)
CCAN: 109691315(Mgea5)
OCU: 100351779(MGEA5)
TUP: 102491291(MGEA5)
CFA: 477802(MGEA5)
AML: 100472078(MGEA5)
UMR: 103679457(MGEA5)
ORO: 101374982(MGEA5)
FCA: 101098493(MGEA5)
PTG: 102959286(MGEA5)
AJU: 106966947(MGEA5)
BTA: 538561(OGA)
BOM: 102279409(MGEA5)
BIU: 109578999(MGEA5)
PHD: 102316524(MGEA5)
CHX: 102179540(MGEA5)
OAS: 101113978(MGEA5)
SSC: 100152585(MGEA5)
CFR: 102507074(MGEA5)
CDK: 105084341(MGEA5)
BACU: 103001043(MGEA5)
LVE: 103070168(MGEA5)
OOR: 101288973(MGEA5)
ECB: 100060245(MGEA5)
EPZ: 103551392(MGEA5)
EAI: 106828857(MGEA5)
MYB: 102258473(MGEA5)
MYD: 102763853(MGEA5)
HAI: 109379646(MGEA5)
RSS: 109443972(MGEA5)
PALE: 102892734(OGA)
LAV: 100660277(MGEA5)
TMU: 101348318
MDO: 100023348(MGEA5)
SHR: 100924785(MGEA5)
OAA: 100086916(MGEA5)
GGA: 423851(MGEA5)
MGP: 100550244(MGEA5)
CJO: 107306849 107315982(MGEA5)
APLA: 101798266(MGEA5) 101803302
ACYG: 106035955(MGEA5) 106043195
TGU: 100222791(MGEA5)
GFR: 102039689(MGEA5) 102041996
FAB: 101807026(MGEA5) 101820674
PHI: 102099607 102100524(MGEA5)
PMAJ: 107203361 107206955(MGEA5)
CCW: 104690840 104697891(MGEA5)
FPG: 101911645 101920070(MGEA5)
FCH: 102050212 102050673(MGEA5)
CLV: 102086261 102092419(MGEA5)
EGZ: 104125639(MGEA5) 104130005
AAM: 106487392 106496884(MGEA5)
ASN: 102378650 102387046(OGA)
PSS: 102451920(OGA)
CMY: 102948301(MGEA5)
CPIC: 101934313(MGEA5)
ACS: 100559082(mgea5)
PVT: 110077588(MGEA5)
PBI: 103061735(OGA)
GJA: 107114456(MGEA5)
XLA: 108696157(mgea5.L) 108697432(mgea5.S)
XTR: 100145437(mgea5)
NPR: 108784409(MGEA5)
DRE: 324487(oga)
CCAR: 109069987 109083210(mgea5)
LCO: 104922274(mgea5) 104925209
CSEM: 103383859 103387380(mgea5)
SFM: 108920620 108930276(mgea5)
LCM: 102346400(MGEA5) 102358152
CMK: 103190567(mgea5)
CIN: 100179919
SPU: 585537
APLC: 110981261
SKO: 100378403
DME: Dmel_CG5871(Oga)
DSI: Dsimw501_GD19407(Dsim_GD19407)
MDE: 101893356
AAG: 5571796
AME: 411905
BIM: 100749208
BTER: 100645450
SOC: 105196907
AEC: 105154917
PBAR: 105430117
HST: 105189349
CFO: 105248789
LHU: 105675868
PGC: 109860249
NVI: 100119788
TCA: 655306
DPA: 109539113
NVL: 108558025
BMOR: 101735953
PRAP: 110998763
API: 100163269(MGEA5)
DNX: 107165302
ZNE: 110832426
FCD: 110863215
TUT: 107360407
BMY: Bm1_40605
CRG: 105347264
MYI: 110449102
OBI: 106884279
LAK: 106176558
SHX: MS3_06552
EGL: EGR_04224
EPA: 110245582
HMG: 100215737
AQU: 100640131
ABAC: LuPra_00231(nagJ)
 » show all
Taxonomy
Reference
1  [PMID:11148210]
  Authors
Gao Y, Wells L, Comer FI, Parker GJ, Hart GW
  Title
Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human  brain.
  Journal
J Biol Chem 276:9838-45 (2001)
  Sequence
[hsa:10724]
Reference
2  [PMID:11788610]
  Authors
Wells L, Gao Y, Mahoney JA, Vosseller K, Chen C, Rosen A, Hart GW
  Title
Dynamic O-glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic beta-N-acetylglucosaminidase, O-GlcNAcase.
  Journal
J Biol Chem 277:1755-61 (2002)
  Sequence
[hsa:10724]
Reference
3  [PMID:16533067]
  Authors
Cetinbas N, Macauley MS, Stubbs KA, Drapala R, Vocadlo DJ
  Title
Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants.
  Journal
Biochemistry 45:3835-44 (2006)
DOI:10.1021/bi052370b
Reference
4  [PMID:16565725]
  Authors
Dennis RJ, Taylor EJ, Macauley MS, Stubbs KA, Turkenburg JP, Hart SJ, Black GN, Vocadlo DJ, Davies GJ
  Title
Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity.
  Journal
Nat Struct Mol Biol 13:365-71 (2006)
DOI:10.1038/nsmb1079
  Sequence
[bth:BT_4395]
Reference
5  [PMID:16584714]
  Authors
Kim EJ, Kang DO, Love DC, Hanover JA
  Title
Enzymatic characterization of O-GlcNAcase isoforms using a fluorogenic GlcNAc substrate.
  Journal
Carbohydr Res 341:971-82 (2006)
DOI:10.1016/j.carres.2006.03.004
Reference
6  [PMID:8034696]
  Authors
Dong DL, Hart GW
  Title
Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol.
  Journal
J Biol Chem 269:19321-30 (1994)
  Sequence
[rno:154968]
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.169
IUBMB Enzyme Nomenclature: 3.2.1.169
ExPASy - ENZYME nomenclature database: 3.2.1.169
BRENDA, the Enzyme Database: 3.2.1.169

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