NAGA_DANRE
ID NAGA_DANRE Reviewed; 404 AA.
AC Q6P0U0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000250|UniProtKB:Q9Y303};
DE Short=GlcNAc 6-P deacetylase {ECO:0000250|UniProtKB:Q9Y303};
DE EC=3.5.1.25 {ECO:0000250|UniProtKB:Q9Y303};
DE AltName: Full=Amidohydrolase domain-containing protein 2 {ECO:0000250|UniProtKB:Q9Y303};
GN Name=amdhd2; ORFNames=zgc:77775;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes the N-glycolyl group from N-glycolylglucosamine 6-
CC phosphate (GlcNGc-6-P) in the N-glycolylneuraminic acid (Neu5Gc)
CC degradation pathway. {ECO:0000250|UniProtKB:Q9Y303}.
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:Q9Y303};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P0AF18};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000250|UniProtKB:P0AF18};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC {ECO:0000250|UniProtKB:Q9Y303}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC NagA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC065449; AAH65449.1; -; mRNA.
DR RefSeq; NP_991244.1; NM_205681.1.
DR RefSeq; XP_005163800.1; XM_005163743.3.
DR RefSeq; XP_005163801.1; XM_005163744.3.
DR AlphaFoldDB; Q6P0U0; -.
DR SMR; Q6P0U0; -.
DR STRING; 7955.ENSDARP00000011842; -.
DR PaxDb; Q6P0U0; -.
DR Ensembl; ENSDART00000159647; ENSDARP00000133871; ENSDARG00000100376.
DR GeneID; 402981; -.
DR KEGG; dre:402981; -.
DR CTD; 51005; -.
DR ZFIN; ZDB-GENE-040426-1871; amdhd2.
DR eggNOG; KOG3892; Eukaryota.
DR GeneTree; ENSGT00390000012605; -.
DR HOGENOM; CLU_032482_0_2_1; -.
DR InParanoid; Q6P0U0; -.
DR OMA; HAFNAMP; -.
DR OrthoDB; 1066877at2759; -.
DR PhylomeDB; Q6P0U0; -.
DR TreeFam; TF315036; -.
DR Reactome; R-DRE-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR UniPathway; UPA00629; -.
DR PRO; PR:Q6P0U0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000100376; Expressed in intestine and 34 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..404
FT /note="N-acetylglucosamine-6-phosphate deacetylase"
FT /id="PRO_0000315779"
FT ACT_SITE 294
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 143
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 154..155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 211
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 232
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 235..236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 269..272
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 328..330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
SQ SEQUENCE 404 AA; 43686 MW; BCF27EA3F4D1226F CRC64;
MPSNKSVSDA PITQFVNCRI LKNHKLQWED LWVREGKILN PEKLFFDEQG FADHRVDCEN
KIIAPGFIDV QLNGGYGIDF SQASSDIRGG VALVAKKILE HGVTSFCPTL VTSPPHIYHK
VIPELRVQDG GPEGAGVLGI HLEGPFISEE KRGAHPPKFL RTFQSGGVAD LMETYGQLEN
VAMVTLAPEL TNSAAAIHEL SSRGITVSVG HSMADLSQAE EAVQNGATFI THLFNAMLPF
HHRDPGIVGL LTSDRIPPGR TVYYGMIADG IHTHPAALRI AHRAHPAGLV LVTDAVTAMG
LPPGRHTLGQ QQIDIQGLHA YVAGTTTLSG SIATMDMCVR HFREASGCTV EAALEAASLH
PAQLLGISHR KGTLEFGADA DFIVLDDMLT VRETYIAGQQ VWRK
