| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G443903_T03 |
| Family | GH89 |
| Protein Properties | Length: 832 Molecular Weight: 94872.8 Isoelectric Point: 5.9828 |
| Chromosome | Chromosome/Scaffold: 2 Start: 5005786 End: 5014906 |
| Description | alpha-N-acetylglucosaminidase family / NAGLU family |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GH89 | 102 | 808 | 0 |
| PEILILGASGVEISAGFHWYLKHYCAAHISWDKTGGAQLSTIPRPGSLPRVPDGGVLIQRPIDWSYYQNAVTSSYSFAWWDWDRWEKEIDWMALQGINLP LAFTGQESIWQRIFERYNISKSDLDDFFGGPAFLAWSRMANMHGWGGPLPQTWLDDQLVLQKKILSRMYSFGMFPVLPAFSGNIPAALKSKFPSAKVTHL GNWFTVDSNPRWCCTYLLDASDPLFVEIGKMFIEEQIREYGRTSHIYNCDTFDENTPPLSDPNYISSLGAATFRGMQSGDNDAIWLMQGWLFTYDPFWEP PQMKALLHSVPVGKMIVLDLYAEVKPVWINSDQLYGVPYIWCMLHNFAADFEMYGVLDALASGPIDARLSDNSTMVGVGMSMEGIEQNPIVYDLMSEMAF HHRQVDLQVWVKTYPTRRYGKPVKGLQDAWWILYRTLYNCTDGKNDKNRDVIVAFPDVEPFVIATPGLHVNTRQMYSTVPSKNYIRKDVSSDAYEHPHLW YDTNAVIHALELFLQHGDEVSDSNTFRYDLVDLTRQVLAKYANDVFLKIIESYKSNNMNQVTILCQHFLSLVNDLDTLLSSHEGFLLGPWLESAKGLARN SEQEIQYEWNARTQITMWFDNTETKASLLRDYANKYWSGLLQDYYGPRAAIYFKHLLLSMENNAPFALKEWRREWISLTNNWQSDRKVFSTTATGDPLNI SQSLYTK | |||
| Full Sequence |
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| Protein Sequence Length: 832 Download |
| MRPRPSRFLQ LLLVVVIACA VPGVRCSDRR FPHLDRVREL QRREGSSSAE QEAAARGLLA 60 RLLPSHSTSF EFRVISTSTE LCGGKTCFVI NNHPLFDGEG TPEILILGAS GVEISAGFHW 120 YLKHYCAAHI SWDKTGGAQL STIPRPGSLP RVPDGGVLIQ RPIDWSYYQN AVTSSYSFAW 180 WDWDRWEKEI DWMALQGINL PLAFTGQESI WQRIFERYNI SKSDLDDFFG GPAFLAWSRM 240 ANMHGWGGPL PQTWLDDQLV LQKKILSRMY SFGMFPVLPA FSGNIPAALK SKFPSAKVTH 300 LGNWFTVDSN PRWCCTYLLD ASDPLFVEIG KMFIEEQIRE YGRTSHIYNC DTFDENTPPL 360 SDPNYISSLG AATFRGMQSG DNDAIWLMQG WLFTYDPFWE PPQMKALLHS VPVGKMIVLD 420 LYAEVKPVWI NSDQLYGVPY IWCMLHNFAA DFEMYGVLDA LASGPIDARL SDNSTMVGVG 480 MSMEGIEQNP IVYDLMSEMA FHHRQVDLQV WVKTYPTRRY GKPVKGLQDA WWILYRTLYN 540 CTDGKNDKNR DVIVAFPDVE PFVIATPGLH VNTRQMYSTV PSKNYIRKDV SSDAYEHPHL 600 WYDTNAVIHA LELFLQHGDE VSDSNTFRYD LVDLTRQVLA KYANDVFLKI IESYKSNNMN 660 QVTILCQHFL SLVNDLDTLL SSHEGFLLGP WLESAKGLAR NSEQEIQYEW NARTQITMWF 720 DNTETKASLL RDYANKYWSG LLQDYYGPRA AIYFKHLLLS MENNAPFALK EWRREWISLT 780 NNWQSDRKVF STTATGDPLN ISQSLYTKYL SNADLLGLVE GTGSPWKSAS L* 840 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam12971 | NAGLU_N | 3.0e-17 | 64 | 152 | 89 | + 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 | 8.0e-99 | 511 | 809 | 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 | 0 | 167 | 505 | 339 | + 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 | CAE04506.2 | 0 | 3 | 816 | 2 | 813 | OSJNBb0059K02.16 [Oryza sativa (japonica cultivar-group)] |
| GenBank | EEC78143.1 | 0 | 3 | 816 | 2 | 813 | hypothetical protein OsI_17702 [Oryza sativa Indica Group] |
| GenBank | EEE61812.1 | 0 | 23 | 816 | 322 | 1113 | hypothetical protein OsJ_16433 [Oryza sativa Japonica Group] |
| RefSeq | XP_002280399.1 | 0 | 33 | 818 | 30 | 813 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002511461.1 | 0 | 33 | 814 | 29 | 804 | 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 | 56 | 799 | 175 | 866 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 2vcb_A | 0 | 56 | 799 | 175 | 866 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 2vca_A | 0 | 56 | 799 | 175 | 866 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 2vc9_A | 0 | 56 | 799 | 175 | 866 | A Chain A, Family 89 Glycoside Hydrolase From Clostridium Perfringens In Complex With 2-Acetamido-1,2-Dideoxynojirmycin |
| PDB | 4a4a_A | 0 | 56 | 799 | 198 | 889 | A Chain A, Cpgh89 (E483q, E601q), From Clostridium Perfringens, In Complex With Its Substrate Glcnac-Alpha-1,4-Galactose |
