ID A0A0Q8P000_9ACTN Unreviewed; 395 AA.
AC A0A0Q8P000;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|EMBL:KRB67100.1};
GN ORFNames=ASE03_01670 {ECO:0000313|EMBL:KRB67100.1};
OS Kitasatospora sp. Root187.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1736486 {ECO:0000313|EMBL:KRB67100.1, ECO:0000313|Proteomes:UP000051829};
RN [1] {ECO:0000313|EMBL:KRB67100.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB67100.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB67100.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB67100.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR038994-3};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000256|PIRSR:PIRSR038994-3};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC NagA family. {ECO:0000256|ARBA:ARBA00010716,
CC ECO:0000256|PIRNR:PIRNR038994}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRB67100.1}.
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DR EMBL; LMHX01000023; KRB67100.1; -; Genomic_DNA.
DR RefSeq; WP_057227796.1; NZ_LMHX01000023.1.
DR AlphaFoldDB; A0A0Q8P000; -.
DR STRING; 1736486.ASE03_01670; -.
DR Proteomes; UP000051829; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:InterPro.
DR CDD; cd00854; NagA; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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 NCBIfam; TIGR00221; nagA; 1.
DR PANTHER; PTHR11113; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR PANTHER; PTHR11113:SF16; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF038994; NagA; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PIRNR:PIRNR038994}; Hydrolase {ECO:0000256|PIRNR:PIRNR038994};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000051829}.
FT DOMAIN 55..382
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 275
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-1"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 220..221
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 309..311
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
SQ SEQUENCE 395 AA; 40443 MW; 9B9482777102B1DD CRC64;
MTADRSALSG ARLVLPGGVV ENGRLAIEGS RIAGLGAAAS TPEGSPGDVD LTGYTVVPGF
VDLHVHGGGG ASYASGIAEE ALTVARTHLA HGTTTTIAST VTGEIDELCH QAAVLSELVE
DGVLAGVHFE GPFISHNRCG AHRPDLLRDP DPVLVRKLVD AARGTAKMFT LAPELTGGLE
SVRMLADLGV IAAVGHTDSD YAKTLEAVEA GATVATHLFN AMPGIQHRAP GPIVALLEDE
RVTVELINDG VHLHPSVLDL AYGTAGAERV ALITDAMGAA GMGDGLYPLG PLQVRVENGV
ARLVEGGSIA GSTLTLDVAF KRSVTINGLS LNQAVTSLST VPARLLGLAD SIGSLEAGKN
ADLVVLDSET FDLVAVMRRG EWIVGADRLA KAHAA
//
