NAGA_LYSSH
ID NAGA_LYSSH Reviewed; 387 AA.
AC Q84F86;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000303|PubMed:12855720};
DE Short=GlcNAc 6-P deacetylase {ECO:0000250|UniProtKB:O34450};
DE EC=3.5.1.25 {ECO:0000250|UniProtKB:P0AF18};
GN Name=nagA;
OS Lysinibacillus sphaericus (Bacillus sphaericus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=2362;
RX PubMed=12855720; DOI=10.1099/mic.0.26231-0;
RA Alice A.F., Perez-Martinez G., Sanchez-Rivas C.;
RT "Phosphoenolpyruvate phosphotransferase system and N-acetylglucosamine
RT metabolism in Bacillus sphaericus.";
RL Microbiology 149:1687-1698(2003).
CC -!- FUNCTION: Involved in the first committed step in the biosynthesis of
CC amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group
CC of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-
CC phosphate and acetate. {ECO:0000269|PubMed:12855720}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-
CC glucosamine 6-phosphate; Xref=Rhea:RHEA:22936, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=3.5.1.25;
CC Evidence={ECO:0000250|UniProtKB:P0AF18};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:O34450};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000250|UniProtKB:O34450};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 4/5.
CC {ECO:0000305|PubMed:12855720}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O34450}.
CC -!- INDUCTION: By N-acetylglucosamine. {ECO:0000269|PubMed:12855720}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC NagA family. {ECO:0000305}.
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DR EMBL; AY211495; AAO43396.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84F86; -.
DR SMR; Q84F86; -.
DR STRING; 1421.A2J09_04990; -.
DR UniPathway; UPA00629; UER00683.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0047419; F:N-acetylgalactosamine-6-phosphate deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; ISS:UniProtKB.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00854; NagA; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR003764; GlcNAc_6-P_deAcase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11113:SF14; PTHR11113:SF14; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF038994; NagA; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR00221; nagA; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Hydrolase; Metal-binding.
FT CHAIN 1..387
FT /note="N-acetylglucosamine-6-phosphate deacetylase"
FT /id="PRO_0000170913"
FT ACT_SITE 277
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 62
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 64
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 132
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 132
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 143..144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 198
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 219
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 222..223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 251..254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 277
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 310..312
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O34450"
SQ SEQUENCE 387 AA; 42382 MW; A7814358BE311857 CRC64;
MFFLSLIIRN ITVVNASGRD EQMDVWMKDG KIAQIAQHIH AQGVDQLEGS GKFLLPGFID
MHIHGSAQMD TMDASDEGLH IHGPITIKEG TTSFLATTMT QSFDWFDRAQ RQCGNNFSPK
SDEAEVLGLH IEGPFVSKQR AGAQPLDYIV QPDMEVIKKW QALSGQKIKQ ITLAPEEPNG
MAAVQSLSES GVIVSIGHSD ATFEQMQEAV QLGASQGTHL YNQMRPFHHR DPGVVGGVLL
VDAIKAELIV DFIHMHEGAV EMAYRLKGAD GIILITDAMR AKGMPYGEYD LGGQLVHVTE
SGAHLSNGSL AGSILTMDQA VRNMRQITNC TLEELVKMSS YNAAQQLKLT NKGQLTEGYD
ADAVIVDEHL LLHQTIKAGR IRVQTNN
