HAMAP rule MF_01241
General rule information
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Accession | MF_01241 |
Dates | 21-MAY-2003 (Created)
12-MAR-2024 (Last updated, Version 27) |
Name | GlcN6P_deamin |
Scope(s) |
Bacteria |
Template(s) | P0A759 (NAGB_ECOLI); P59686 (NAGB_LYSSH); [ Recover all ] |
Triggered by |
HAMAP; MF_01241 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | NAGB |
Protein name | RecName: Full=Glucosamine-6-phosphate deaminase; EC=3.5.99.6; AltName: Full=GlcN6P deaminase; Short=GNPDA; AltName: Full=Glucosamine-6-phosphate isomerase; |
Gene name | Name=nagB; |
Comments
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FUNCTION | Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. |
CATALYTIC ACTIVITY | Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6- phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6; |
case <FTGroup:1> | |
ACTIVITY REGULATION | Allosterically activated by N-acetylglucosamine 6- phosphate (GlcNAc6P). |
end case | |
PATHWAY | Amino-sugar metabolism; N-acetylneuraminate degradation; D- fructose 6-phosphate from N-acetylneuraminate: step 5/5. |
case <OC:Gammaproteobacteria> and <FT:10> | |
SUBUNIT | Homohexamer; trimer of disulfide-linked dimers. |
end case | |
case <OC:Gammaproteobacteria> and not <FT:10> | |
SUBUNIT | Homohexamer. |
end case | |
SIMILARITY | Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. NagB subfamily. |
Keywords
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Carbohydrate metabolism | |
case <FT:10> | |
Disulfide bond | |
end case | |
Hydrolase | |
case <FTGroup:1> | |
Allosteric enzyme | |
end case |
Gene Ontology
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GO:0004342; Molecular function:glucosamine-6-phosphate deaminase activity |
GO:0019262; Biological process:N-acetylneuraminate catabolic process |
Cross-references
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Pfam | PF01182; Glucosamine_iso; 1; |
NCBIfam | TIGR00502; NagB; 1; |
PROSITE | PS01161; GLC_GALNAC_ISOMERASE; 1; |
Features
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From: NAGB_ECOLI (P0A759) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ACT_SITE | 72 | 72 | /note="Proton acceptor; for enolization step" | D | ||||||||
ACT_SITE | 141 | 141 | /note="For ring-opening step" | [DN] | ||||||||
ACT_SITE | 143 | 143 | /note="Proton acceptor; for ring-opening step" | H | ||||||||
ACT_SITE | 148 | 148 | /note="For ring-opening step" | E | ||||||||
SITE | 151 | 151 | /note="Part of the allosteric site" | S | 1 | |||||||
SITE | 158 | 158 | /note="Part of the allosteric site" | R | 1 | |||||||
SITE | 160 | 160 | /note="Part of the allosteric site" | K | 1 | |||||||
SITE | 161 | 161 | /note="Part of the allosteric site" | T | 1 | |||||||
SITE | 254 | 254 | /note="Part of the allosteric site" | Y | 1 | |||||||
DISULFID | 219 | 219 | /note="Interchain" | C |
Additional information
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Size range | 233-274 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: <Unknown> |
Comments | Possible second divergent copy in BACTN, which is fused with an unknown C-terminal domain; sequence not included in alignment |