We will be switching to the new UniProt website soon. Please explore and share your feedback.
Take me to the new website.
UniProtKB - Q0TR53 (OGA_CLOP1)
Protein
O-GlcNAcase NagJ
Gene
nagJ
Organism
Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
Status
Functioni
Binds carbohydrates (PubMed:16990278).
Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Can bind and deglycosylate O-glycosylated peptides from mammals.
3 PublicationsMiscellaneous
Metal-binding observed in X-ray crystal structures is artifactual.Curated
Catalytic activityi
- 3-O-(N-acetyl-β-D-glucosaminyl)-L-seryl-[protein] + H2O = L-seryl-[protein] + N-acetyl-D-glucosamine3 PublicationsEC:3.2.1.1693 Publications
- 3-O-(N-acetyl-β-D-glucosaminyl)-L-threonyl-[protein] + H2O = L-threonyl-[protein] + N-acetyl-D-glucosamine3 PublicationsEC:3.2.1.1693 Publications
Activity regulationi
Inhibited by O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenyl-carbamate (PUGNAc) and streptozotocin.2 Publications
Kineticsi
- KM=2.9 µM for 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide (4MU-NAG)1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 187 | Substrate; via carbonyl oxygen1 Publication | 1 | |
Binding sitei | 218 | Substrate1 Publication | 1 | |
Binding sitei | 297 | Substrate1 Publication | 1 | |
Active sitei | 298 | Proton donor1 Publication | 1 | |
Binding sitei | 335 | Substrate1 Publication | 1 | |
Binding sitei | 401 | Substrate1 Publication | 1 | |
Binding sitei | 429 | Substrate1 Publication | 1 |
GO - Molecular functioni
- [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity Source: UniProtKB-EC
- [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine O-N-acetyl-alpha-D-glucosaminase activity Source: UniProtKB-EC
- [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine O-N-acetyl-alpha-D-glucosaminase activity Source: UniProtKB-EC
- beta-N-acetylglucosaminidase activity Source: UniProtKB
- carbohydrate binding Source: UniProtKB
GO - Biological processi
- carbohydrate metabolic process Source: UniProtKB
- polysaccharide catabolic process Source: InterPro
- protein deglycosylation Source: UniProtKB
Keywordsi
Molecular function | Glycosidase, Hydrolase |
Enzyme and pathway databases
BRENDAi | 3.2.1.169, 1503 |
SABIO-RKi | Q0TR53 |
Protein family/group databases
CAZyi | CBM32, Carbohydrate-Binding Module Family 32 GH84, Glycoside Hydrolase Family 84 |
Names & Taxonomyi
Protein namesi | Recommended name: O-GlcNAcase NagJ (EC:3.2.1.1693 Publications)Alternative name(s): Beta-N-acetylglucosaminidase Beta-N-acetylhexosaminidase Beta-hexosaminidase GH84C1 Publication Hexosaminidase B N-acetyl-beta-D-glucosaminidase |
Gene namesi | Name:nagJ Ordered Locus Names:CPF_1442 |
Organismi | Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) |
Taxonomic identifieri | 195103 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Clostridia › Eubacteriales › Clostridiaceae › Clostridium › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 297 | D → A: 99% decrease in activity for 4MU-NAG. 1 Publication | 1 | |
Mutagenesisi | 298 | D → N: 99% decrease in activity for 4MU-NAG. 2 Publications | 1 | |
Mutagenesisi | 335 | Y → F: Strongly decreases affinity for 4MU-NAG. 99% decrease in activity for 4MU-NAG. 1 Publication | 1 | |
Mutagenesisi | 390 | N → A: No change in activity for 4MU-NAG. 1 Publication | 1 | |
Mutagenesisi | 396 | N → A: Strongly decreases affinity for 4MU-NAG. 99% decrease in activity for 4MU-NAG. 1 Publication | 1 | |
Mutagenesisi | 401 | D → A: Strongly decreases affinity for 4MU-NAG. 99% decrease in activity for 4MU-NAG. 1 Publication | 1 | |
Mutagenesisi | 490 | W → A: Strongly decreases affinity for 4MU-NAG. 97% decrease in activity for 4MU-NAG. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 30 | Sequence analysisAdd BLAST | 30 | |
ChainiPRO_0000257985 | 31 – 1001 | O-GlcNAcase NagJAdd BLAST | 971 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
BMRBi | Q0TR53 |
SMRi | Q0TR53 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q0TR53 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 916 – 1001 | Fibronectin type-IIIPROSITE-ProRule annotationAdd BLAST | 86 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 179 – 469 | Catalytic domainSequence analysisAdd BLAST | 291 | |
Regioni | 394 – 396 | Substrate binding1 Publication | 3 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 515 – 543 | Sequence analysisAdd BLAST | 29 | |
Coiled coili | 573 – 597 | Sequence analysisAdd BLAST | 25 |
Sequence similaritiesi
Belongs to the glycosyl hydrolase 84 family.Sequence analysis
Keywords - Domaini
Coiled coil, SignalPhylogenomic databases
eggNOGi | COG3291, Bacteria COG3525, Bacteria |
HOGENOMi | CLU_001501_2_0_9 |
OMAi | ARMEEAC |
OrthoDBi | 1158117at2 |
Family and domain databases
CDDi | cd00063, FN3, 1 hit |
Gene3Di | 2.60.40.10, 1 hit 3.30.379.10, 1 hit |
InterProi | View protein in InterPro IPR011496, Beta-N-acetylglucosaminidase IPR008965, CBM2/CBM3_carb-bd_dom_sf IPR002102, Cohesin_dom IPR000421, FA58C IPR003961, FN3_dom IPR036116, FN3_sf IPR008979, Galactose-bd-like_sf IPR017853, Glycoside_hydrolase_SF IPR029018, Hex-like_dom2 IPR015882, HEX_bac_N IPR013783, Ig-like_fold |
Pfami | View protein in Pfam PF00963, Cohesin, 1 hit PF00754, F5_F8_type_C, 1 hit PF00041, fn3, 1 hit PF02838, Glyco_hydro_20b, 1 hit PF07555, NAGidase, 1 hit |
SMARTi | View protein in SMART SM00060, FN3, 1 hit |
SUPFAMi | SSF49265, SSF49265, 1 hit SSF49384, SSF49384, 1 hit SSF49785, SSF49785, 1 hit SSF51445, SSF51445, 1 hit SSF55545, SSF55545, 1 hit |
PROSITEi | View protein in PROSITE PS50853, FN3, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q0TR53-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKRKMLKRLL TSAFACMFIA NGLITTTVRA VGPKTGEENQ VLVPNLNPTP
60 70 80 90 100
ENLEVVGDGF KITSSINLVG EEEADENAVN ALREFLTANN IEINSENDPN
110 120 130 140 150
STTLIIGEVD DDIPELDEAL NGTTAENLKE EGYALVSNDG KIAIEGKDGD
160 170 180 190 200
GTFYGVQTFK QLVKESNIPE VNITDYPTVS ARGIVEGFYG TPWTHQDRLD
210 220 230 240 250
QIKFYGENKL NTYIYAPKDD PYHREKWREP YPESEMQRMQ ELINASAENK
260 270 280 290 300
VDFVFGISPG IDIRFDGDAG EEDFNHLITK AESLYDMGVR SFAIYWDDIQ
310 320 330 340 350
DKSAAKHAQV LNRFNEEFVK AKGDVKPLIT VPTEYDTGAM VSNGQPRAYT
360 370 380 390 400
RIFAETVDPS IEVMWTGPGV VTNEIPLSDA QLISGIYNRN MAVWWNYPVT
410 420 430 440 450
DYFKGKLALG PMHGLDKGLN QYVDFFTVNP MEHAELSKIS IHTAADYSWN
460 470 480 490 500
MDNYDYDKAW NRAIDMLYGD LAEDMKVFAN HSTRMDNKTW AKSGREDAPE
510 520 530 540 550
LRAKMDELWN KLSSKEDASA LIEELYGEFA RMEEACNNLK ANLPEVALEE
560 570 580 590 600
CSRQLDELIT LAQGDKASLD MIVAQLNEDT EAYESAKEIA QNKLNTALSS
610 620 630 640 650
FAVISEKVAQ SFIQEALSFD LTLINPRTVK ITASSEETSG ENAPASFASD
660 670 680 690 700
GDMNTFWHSK WSSPAHEGPH HLTLELDNVY EINKVKYAPR QDSKNGRITG
710 720 730 740 750
YKVSVSLDGE NFTEVKTGTL EDNAAIKFIE FDSVDAKYVR LDVTDSVSDQ
760 770 780 790 800
ANGRGKFATA AEVNVHGKLK ENAEVTGSVS LEALEEVQVG ENLEVGVGID
810 820 830 840 850
ELVNAEAFAY DFTLNYDENA FEYVEAISDD GVFVNAKKIE DGKVRVLVSS
860 870 880 890 900
LTGEPLPAKE VLAKVVLRAE AKAEGSNLSV TNSSVGDGEG LVHEIAGTEK
910 920 930 940 950
TVNIIEGTSP EIVVNPVRDF KASEINKKNV TVTWTEPETT EGLEGYILYK
960 970 980 990 1000
DGKKVAEIGK DETSYTFKKL NRHTIYNFKI AAKYSNGEVS SKESLTLRTA
R
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000246 Genomic DNA Translation: ABG84519.1 |
RefSeqi | WP_003456570.1, NC_008261.1 |
Genome annotation databases
EnsemblBacteriai | ABG84519; ABG84519; CPF_1442 |
GeneIDi | 29571445 |
KEGGi | cpf:CPF_1442 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000246 Genomic DNA Translation: ABG84519.1 |
RefSeqi | WP_003456570.1, NC_008261.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2CBI | X-ray | 2.25 | A/B | 31-624 | [»] | |
2CBJ | X-ray | 2.35 | A/B | 31-624 | [»] | |
2J1A | X-ray | 1.49 | A | 625-767 | [»] | |
2J1E | X-ray | 2.40 | A | 625-767 | [»] | |
2J62 | X-ray | 2.26 | A/B | 31-624 | [»] | |
2J7M | X-ray | 2.30 | A | 625-767 | [»] | |
2JH2 | X-ray | 2.50 | A/B/C | 768-909 | [»] | |
2O4E | NMR | - | A | 768-909 | [»] | |
2OZN | X-ray | 1.60 | A | 768-909 | [»] | |
2V5C | X-ray | 2.10 | A/B | 31-624 | [»] | |
2V5D | X-ray | 3.30 | A | 31-767 | [»] | |
2VUR | X-ray | 2.20 | A/B | 31-624 | [»] | |
2W1N | X-ray | 1.80 | A | 765-1001 | [»] | |
2WB5 | X-ray | 2.31 | A/B | 31-624 | [»] | |
2X0Y | X-ray | 2.25 | A/B | 31-624 | [»] | |
2XPK | X-ray | 2.40 | A/B | 31-624 | [»] | |
2YDQ | X-ray | 2.60 | A | 31-618 | [»] | |
2YDR | X-ray | 2.75 | A | 31-618 | [»] | |
2YDS | X-ray | 2.55 | A | 31-618 | [»] | |
4ZXL | X-ray | 2.60 | A | 39-617 | [»] | |
5OXD | X-ray | 2.60 | A | 31-618 | [»] | |
6RHE | X-ray | 3.10 | A | 31-619 | [»] | |
7KHV | X-ray | 2.30 | A/B/C/D/E/F | 31-624 | [»] | |
BMRBi | Q0TR53 | |||||
SMRi | Q0TR53 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 195103.CPF_1442 |
Protein family/group databases
CAZyi | CBM32, Carbohydrate-Binding Module Family 32 GH84, Glycoside Hydrolase Family 84 |
Protocols and materials databases
DNASUi | 4202790 |
Genome annotation databases
EnsemblBacteriai | ABG84519; ABG84519; CPF_1442 |
GeneIDi | 29571445 |
KEGGi | cpf:CPF_1442 |
Phylogenomic databases
eggNOGi | COG3291, Bacteria COG3525, Bacteria |
HOGENOMi | CLU_001501_2_0_9 |
OMAi | ARMEEAC |
OrthoDBi | 1158117at2 |
Enzyme and pathway databases
BRENDAi | 3.2.1.169, 1503 |
SABIO-RKi | Q0TR53 |
Miscellaneous databases
EvolutionaryTracei | Q0TR53 |
Family and domain databases
CDDi | cd00063, FN3, 1 hit |
Gene3Di | 2.60.40.10, 1 hit 3.30.379.10, 1 hit |
InterProi | View protein in InterPro IPR011496, Beta-N-acetylglucosaminidase IPR008965, CBM2/CBM3_carb-bd_dom_sf IPR002102, Cohesin_dom IPR000421, FA58C IPR003961, FN3_dom IPR036116, FN3_sf IPR008979, Galactose-bd-like_sf IPR017853, Glycoside_hydrolase_SF IPR029018, Hex-like_dom2 IPR015882, HEX_bac_N IPR013783, Ig-like_fold |
Pfami | View protein in Pfam PF00963, Cohesin, 1 hit PF00754, F5_F8_type_C, 1 hit PF00041, fn3, 1 hit PF02838, Glyco_hydro_20b, 1 hit PF07555, NAGidase, 1 hit |
SMARTi | View protein in SMART SM00060, FN3, 1 hit |
SUPFAMi | SSF49265, SSF49265, 1 hit SSF49384, SSF49384, 1 hit SSF49785, SSF49785, 1 hit SSF51445, SSF51445, 1 hit SSF55545, SSF55545, 1 hit |
PROSITEi | View protein in PROSITE PS50853, FN3, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | OGA_CLOP1 | |
Accessioni | Q0TR53Primary (citable) accession number: Q0TR53 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 31, 2006 |
Last sequence update: | September 5, 2006 | |
Last modified: | February 23, 2022 | |
This is version 111 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families