Q5FA94

PR
Gene name
nagZ
Protein name
Beta-hexosaminidase
Names
Beta-N-acetylhexosaminidase, N-acetyl-beta-glucosaminidase
Species
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
KEGG Pathway
ngo:NGO_0135
EC number
3.2.1.52: Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

294-361 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

5 structures for Q5FA94

Entry ID Method Resolution Chain Position Source
6JTI X-ray 220 A A/B/C/D/E/F 1-361 PDB
6JTJ X-ray 218 A A/B/C/D/E/F 1-361 PDB
6JTK X-ray 220 A A/B/C/D/E/F 1-361 PDB
6JTL X-ray 240 A A/B 1-361 PDB
AF-Q5FA94-F1 Predicted AlphaFoldDB

No variants for Q5FA94

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5FA94

No associated diseases with Q5FA94

6 regional properties for Q5FA94

Type Name Position InterPro Accession
conserved_site Twin-arginine translocation pathway, signal sequence 1 - 30 IPR006311
domain Molybdopterin oxidoreductase 93 - 613 IPR006656
domain Molybdopterin dinucleotide-binding domain 811 - 919 IPR006657
domain Molybdopterin oxidoreductase, 4Fe-4S domain 36 - 92 IPR006963
binding_site Molybdopterin oxidoreductase, molybdopterin cofactor binding site 41 - 58 IPR027467
domain Nitrate reductase NapA-like, molybdopterin-binding domain 808 - 925 IPR041957

Functions

Description
EC Number 3.2.1.52 Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

2 GO annotations of molecular function

Name Definition
beta-N-acetylhexosaminidase activity Catalysis of the hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
N-acetyl-beta-D-galactosaminidase activity Catalysis of the reaction: H2O + an N-acetyl-beta-D-galactosalaminyl-

7 GO annotations of biological process

Name Definition
carbohydrate metabolic process The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
cell cycle The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division.
cell division The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
cell wall organization A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
peptidoglycan biosynthetic process The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls.
peptidoglycan turnover The continual breakdown and regeneration of peptidoglycan required to maintain the cell wall.
regulation of cell shape Any process that modulates the surface configuration of a cell.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTVPHIPRGP VMADIAAFRL TEEEKQRLLD PAIGGIILFR RNFQNIEQLK TLTAEIKALR
70 80 90 100 110 120
TPELIIAVDH EGGRVQRFIE GFTRLPAMNV LGQIWDKDGA SAAETAAGQV GRVLATELSA
130 140 150 160 170 180
CGIDLSFTPV LDLDWGNCAV IGNRSFHRNP EAVARLALAL QKGLAKGGMK SCGKHFPGHG
190 200 210 220 230 240
FVEGDSHLVL PEDGRSLDEL EAADLAPFRI MSREGMAAVM PAHVVYPQVD TKPAGFSEIW
250 260 270 280 290 300
LKQILRRDIG FKGVIFSDDL TMEGACGAGG IKERARISFE AGCDIVLVCN RPDLVDELRD
310 320 330 340 350 360
GFTIPDNQDL AGRWQYMENS LGHEAVQAVM QTMGFQAAQA FVAGLASPQD TAGGVKVGEA
F