| Basic Information | |
|---|---|
| Species | Aquilegia coerulea |
| Cazyme ID | Aquca_002_00330.2 |
| Family | GH89 |
| Protein Properties | Length: 845 Molecular Weight: 96193.5 Isoelectric Point: 5.4965 |
| Chromosome | Chromosome/Scaffold: 2 Start: 2961360 End: 2972257 |
| Description | alpha-N-acetylglucosaminidase family / NAGLU family |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GH89 | 100 | 442 | 0 |
| PEIRIGGSSGVELSAGLHWYLKNWCGAHISWDKTGGAQLFSVPKPGFLPLVQASGVLIQRPVPWNYYQNAVASSYTFAWWDWERWEKEIDWMAVQGINLP LAFTGQEAIWQKVFQIFNISSSELNDFFGGPAFLAWSRMGNLHGWGGPLPQSWFDQQLSLQKKILGRMYELGMTPVLPAFSGNVPAALKSIYPSAKIARL GNWFTVRGDTRWCCTYLLDAMDPLFVEIGKAFVEMEITEYGRSSHIYNCDTFDENTPPVDDPEYISSLGAAIYRAMQSGDVDAVWLMQGWLFSYDPFWRP EQMKALLHSVPVGKLVVLDLFAEVKPLWITSEQFYGVPYIWKV | |||
| GH89 | 459 | 834 | 0 |
| WLMVPFFRCMLHNFAGNIEMYGVLDAIASGPVEARTSENSTMASVGVGMSMEGIEQNPVVYDLMSEMAFQHDKLDVKLWLDVYPMRRYGSSDASIRDAWS ILYHTVYNCTDGAYNKNRDVIVAFPDVDPFSISLEDAYMSGKHQLMSEAVIRRVPLRDSTEAYDRPHIWYSTSDVIHALGLFLASGDDLAESNTYRYDLI DLTRQALAKYANQVFMKIIENYRMNDVHGVTFYSKHFLDLVTDMDTLLACHEGFLLGPWLESSKQHAQTQEQKIQFEWNARTQITMWFDNTEEEASLLRD YGNKYWSGLLKDYYGPRAAVYFKHLLESLENGVGFQLKAWRREWIKLTNDWQKSVKIFPVRSTGNALDTSRWLYEK | |||
| Full Sequence |
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| Protein Sequence Length: 845 Download |
| MDSAISSSRF FFILIILFIV FISANSSTIG VNHISQILET HDRERAPNSV QVAASHGVLS 60 RLLPSHSSSF EFQIISKEQC GGKSCFIISN HPSFGINGAP EIRIGGSSGV ELSAGLHWYL 120 KNWCGAHISW DKTGGAQLFS VPKPGFLPLV QASGVLIQRP VPWNYYQNAV ASSYTFAWWD 180 WERWEKEIDW MAVQGINLPL AFTGQEAIWQ KVFQIFNISS SELNDFFGGP AFLAWSRMGN 240 LHGWGGPLPQ SWFDQQLSLQ KKILGRMYEL GMTPVLPAFS GNVPAALKSI YPSAKIARLG 300 NWFTVRGDTR WCCTYLLDAM DPLFVEIGKA FVEMEITEYG RSSHIYNCDT FDENTPPVDD 360 PEYISSLGAA IYRAMQSGDV DAVWLMQGWL FSYDPFWRPE QMKALLHSVP VGKLVVLDLF 420 AEVKPLWITS EQFYGVPYIW KVAIDIANLK WSLSFVSDWL MVPFFRCMLH NFAGNIEMYG 480 VLDAIASGPV EARTSENSTM ASVGVGMSME GIEQNPVVYD LMSEMAFQHD KLDVKLWLDV 540 YPMRRYGSSD ASIRDAWSIL YHTVYNCTDG AYNKNRDVIV AFPDVDPFSI SLEDAYMSGK 600 HQLMSEAVIR RVPLRDSTEA YDRPHIWYST SDVIHALGLF LASGDDLAES NTYRYDLIDL 660 TRQALAKYAN QVFMKIIENY RMNDVHGVTF YSKHFLDLVT DMDTLLACHE GFLLGPWLES 720 SKQHAQTQEQ KIQFEWNART QITMWFDNTE EEASLLRDYG NKYWSGLLKD YYGPRAAVYF 780 KHLLESLENG VGFQLKAWRR EWIKLTNDWQ KSVKIFPVRS TGNALDTSRW LYEKYLRKPD 840 ALDQ* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam12971 | NAGLU_N | 1.0e-23 | 51 | 150 | 100 | + Alpha-N-acetylglucosaminidase (NAGLU) N-terminal domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This N-terminal domain has an alpha-beta fold. | ||
| pfam12972 | NAGLU_C | 7.0e-94 | 537 | 835 | 299 | + Alpha-N-acetylglucosaminidase (NAGLU) C-terminal domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This C-terminal domain has an all alpha helical fold. | ||
| pfam05089 | NAGLU | 4.0e-178 | 165 | 531 | 367 | + Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This central domain has a tim barrel fold. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI15090.1 | 0 | 24 | 843 | 21 | 845 | unnamed protein product [Vitis vinifera] |
| GenBank | EEC78143.1 | 0 | 33 | 842 | 32 | 813 | hypothetical protein OsI_17702 [Oryza sativa Indica Group] |
| RefSeq | XP_002280399.1 | 0 | 24 | 843 | 21 | 812 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002318632.1 | 0 | 26 | 844 | 26 | 812 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002511461.1 | 0 | 1 | 841 | 1 | 805 | alpha-n-acetylglucosaminidase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2vcc_A | 0 | 70 | 825 | 190 | 866 | A Chain A, Cpgh89 (E483q, E601q), From Clostridium Perfringens, In Complex With Its Substrate Glcnac-Alpha-1,4-Galactose |
| PDB | 2vcb_A | 0 | 70 | 825 | 190 | 866 | A Chain A, Cpgh89 (E483q, E601q), From Clostridium Perfringens, In Complex With Its Substrate Glcnac-Alpha-1,4-Galactose |
| PDB | 2vca_A | 0 | 70 | 825 | 190 | 866 | A Chain A, Cpgh89 (E483q, E601q), From Clostridium Perfringens, In Complex With Its Substrate Glcnac-Alpha-1,4-Galactose |
| PDB | 2vc9_A | 0 | 70 | 825 | 190 | 866 | A Chain A, Family 89 Glycoside Hydrolase From Clostridium Perfringens In Complex With 2-Acetamido-1,2-Dideoxynojirmycin |
| PDB | 4a4a_A | 0 | 70 | 825 | 213 | 889 | A Chain A, Cpgh89 (E483q, E601q), From Clostridium Perfringens, In Complex With Its Substrate Glcnac-Alpha-1,4-Galactose |
