ID A0A0L7R617_9HYME Unreviewed; 408 AA.
AC A0A0L7R617;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000256|ARBA:ARBA00018029, ECO:0000256|PIRNR:PIRNR038994};
DE EC=3.5.1.25 {ECO:0000256|ARBA:ARBA00011899, ECO:0000256|PIRNR:PIRNR038994};
GN ORFNames=WH47_07384 {ECO:0000313|EMBL:KOC66315.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC66315.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC66315.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC66315.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001570,
CC ECO:0000256|PIRNR:PIRNR038994};
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}.
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DR EMBL; KQ414648; KOC66315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7R617; -.
DR STRING; 597456.A0A0L7R617; -.
DR Proteomes; UP000053825; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
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:SF14; 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:UP000053825}.
FT DOMAIN 60..401
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 296
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-1"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 237..238
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 330..332
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
SQ SEQUENCE 408 AA; 44773 MW; 5621F901063929D3 CRC64;
MSQENQQILK QFYNCCILRD GKILKEDLWV RDGKVVNSEK IFYVEKVKPN VRIDCKEALI
SPGYIDLQIN GGFGIDFTHN VDNVQEGINK VAKKLLEFGV TSFCPTLVTS PNETYLKIMP
NIKKTKGGKH GASVLGIHLE GPFISPNKKG AHAENHIKQF EKASLFNIGF KSLIDMYGTL
ENVCLVTLAP ELPNALNVIA ELCKRGIKVS LGHSIANQHE GEEAVKSGAS FITHLFNAML
PFHHRDPGLV GLLTSDQIPP GRIVHYGIIA DGIHTHPAAL RIAHRTHPEG LVLVTDALSA
LGLEEGVHQL GQLKIEMRMG RAYIAGTETL CGSTAEMSKC VRYFKEATVC STVEALEAAT
LHPAKTLGIE KKKGVLNYGA DADFVLLDEN LELLSTWISG ECVYLNVR
//
