ID A0A2K5VKC9_MACFA Unreviewed; 372 AA.
AC A0A2K5VKC9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 24-JAN-2024, entry version 27.
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 Name=AMDHD2 {ECO:0000313|Ensembl:ENSMFAP00000025207.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000025207.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000025207.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000025207.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|PIRNR:PIRNR038994}.
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 -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC {ECO:0000256|ARBA:ARBA00004878}.
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 AlphaFoldDB; A0A2K5VKC9; -.
DR SMR; A0A2K5VKC9; -.
DR STRING; 9541.ENSMFAP00000025207; -.
DR Ensembl; ENSMFAT00000033355.2; ENSMFAP00000025207.2; ENSMFAG00000002099.2.
DR VEuPathDB; HostDB:ENSMFAG00000044125; -.
DR GeneTree; ENSGT00390000012605; -.
DR UniPathway; UPA00629; -.
DR Proteomes; UP000233100; Chromosome 20.
DR Bgee; ENSMFAG00000002099; Expressed in adult mammalian kidney and 13 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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 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; 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; 2.
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:UP000233100}.
FT DOMAIN 62..357
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 294
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-1"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
SQ SEQUENCE 372 AA; 39777 MW; A2F5B13268162E4F CRC64;
MRGGQGAAEA RVLQFTNCRI LRGGKLLRED LWVRGGRILD PEKLFFEERR VADERRDCGG
RILAPGFIDV QINGGFGVDF SQATEDVGSG VALVARRILS HGVTSFCPTL VTSPPEVYHK
VVPQIPVKSG GPHGAGVLGL HLEGPFISRE KRGAHPEAHL RSFEANAFQD LLATYGPLDN
VRIVTLAPEL GHSHEVIREL TTRGICVSLG HSVADLRAAE DAVWSGATFI THLFNAMLPF
HHRDPGIVGL LTSDRLPAGR CIFYGMIADG THTNPAALRI AHRAHPQGLV LVTDAIPALG
LGNGRHTLGQ QEVEVDGLTA YVAGCSVESA LEAASLHPAQ LLGLEKSKGT LDFGADAGEG
ASQGYWAAWP YL
//
