AC   MF_01241;
DC   Protein; auto
TR   HAMAP; MF_01241; -; 1; level=0
XX
Names: GlcN6P_deamin
XX
ID   NAGB
DE   RecName: Full=Glucosamine-6-phosphate deaminase;
DE            EC=3.5.99.6;
DE   AltName: Full=GlcN6P deaminase;
DE            Short=GNPDA;
DE   AltName: Full=Glucosamine-6-phosphate isomerase;
GN   Name=nagB;
XX
CC   -!- FUNCTION: Catalyzes the reversible isomerization-deamination of
CC       glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P)
CC       and ammonium ion.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-
CC         phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6;
case <FTGroup:1>
CC   -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine 6-
CC       phosphate (GlcNAc6P).
end case
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC       fructose 6-phosphate from N-acetylneuraminate: step 5/5.
case <OC:Gammaproteobacteria> and <FT:10>
CC   -!- SUBUNIT: Homohexamer; trimer of disulfide-linked dimers.
end case
case <OC:Gammaproteobacteria> and not <FT:10>
CC   -!- SUBUNIT: Homohexamer.
end case
CC   -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC       isomerase family. NagB subfamily.
XX
DR   Pfam; PF01182; Glucosamine_iso; 1; trigger=no
DR   NCBIfam; TIGR00502; NagB; 1; trigger=no
DR   PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1; trigger=no
XX
KW   Carbohydrate metabolism
case <FT:10>
KW   Disulfide bond
end case
KW   Hydrolase
case <FTGroup:1>
KW   Allosteric enzyme
end case
XX
GO   GO:0004342; F:glucosamine-6-phosphate deaminase activity
GO   GO:0006044; P:N-acetylglucosamine metabolic process
XX
FT   From: NAGB_ECOLI (P0A759)
FT   ACT_SITE        72
FT                   /note="Proton acceptor; for enolization step"
FT   Condition: D
FT   ACT_SITE        141
FT                   /note="For ring-opening step"
FT   Condition: [DN]
FT   ACT_SITE        143
FT                   /note="Proton acceptor; for ring-opening step"
FT   Condition: H
FT   ACT_SITE        148
FT                   /note="For ring-opening step"
FT   Condition: E
FT   SITE            151
FT                   /note="Part of the allosteric site"
FT   Optional; Group: 1; Condition: S
FT   SITE            158
FT                   /note="Part of the allosteric site"
FT   Optional; Group: 1; Condition: R
FT   SITE            160
FT                   /note="Part of the allosteric site"
FT   Optional; Group: 1; Condition: K
FT   SITE            161
FT                   /note="Part of the allosteric site"
FT   Optional; Group: 1; Condition: T
FT   SITE            254
FT                   /note="Part of the allosteric site"
FT   Optional; Group: 1; Condition: Y
FT   DISULFID        219
FT                   /note="Interchain"
FT   Optional; Condition: C
XX
Size: 233-274;
Related: None;
Template: P0A759; P59686;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: <Unknown>
Duplicate: in BACSU, BACTN
Plasmid: None
Comments: Possible second divergent copy in BACTN, which is fused with an unknown
 C-terminal domain; sequence not included in alignment
XX
# Revision 1.26 2023/06/01
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