ID NAGA_BOVIN Reviewed; 409 AA.
AC A7MBC0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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}.
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DR EMBL; BC151478; AAI51479.1; -; mRNA.
DR RefSeq; NP_001094574.1; NM_001101104.2.
DR AlphaFoldDB; A7MBC0; -.
DR SMR; A7MBC0; -.
DR STRING; 9913.ENSBTAP00000063678; -.
DR PaxDb; 9913-ENSBTAP00000001355; -.
DR Ensembl; ENSBTAT00000074115.1; ENSBTAP00000072880.1; ENSBTAG00000001022.6.
DR GeneID; 521401; -.
DR KEGG; bta:521401; -.
DR CTD; 51005; -.
DR VEuPathDB; HostDB:ENSBTAG00000001022; -.
DR eggNOG; KOG3892; Eukaryota.
DR GeneTree; ENSGT00390000012605; -.
DR HOGENOM; CLU_032482_0_2_1; -.
DR InParanoid; A7MBC0; -.
DR OMA; PCRKGAH; -.
DR TreeFam; TF315036; -.
DR Reactome; R-BTA-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR UniPathway; UPA00629; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000001022; Expressed in Ammon's horn and 103 other cell types or tissues.
DR ExpressionAtlas; A7MBC0; baseline.
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; 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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..409
FT /note="N-acetylglucosamine-6-phosphate deacetylase"
FT /id="PRO_0000315775"
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 409 AA; 43496 MW; F0B34ACF01011397 CRC64;
MRGGQGAARA PVIQFTNCRI LRGGALLRED LWVRGGRILD PEKLFFEERR VADEQRDCGG
CILAPGFIDV QINGGFGVDF SQASEDVGSG VALVARRILS HGVTSFCPTL VTSPLEVYHK
VLPQIPVKSG GPHGAGVLGV HLEGPFISRE KRGAHPEAHL RSFEADAFQD VLATYGGLDN
VRIVTLAPEL GHSQEVIRAL TALGICVSLG HSVADLGTAE EAVQSGATFI THLFNAMLPF
HHRDPGIVGL LTSDRLPAGR HIFYGMIADG IHTNPAALRI AHRAHPKGLV LVTDAVPALG
LGNGRHTLGQ QEVEVDGLTA YVAGTNTLSG SIAPMDTCVR HFLQATGCSV ESALEAASLH
PAQLLGLEKR KGTLDFGADA DFVVLDDSLH VRATYISGEL VWQVEEARP
//
