ID A0A2B7WHY5_9EURO Unreviewed; 459 AA.
AC A0A2B7WHY5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000256|ARBA:ARBA00018029};
DE EC=3.5.1.25 {ECO:0000256|ARBA:ARBA00011899};
GN ORFNames=GX51_07985 {ECO:0000313|EMBL:PGG96090.1};
OS Blastomyces parvus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGG96090.1, ECO:0000313|Proteomes:UP000224080};
RN [1] {ECO:0000313|EMBL:PGG96090.1, ECO:0000313|Proteomes:UP000224080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH130 {ECO:0000313|EMBL:PGG96090.1,
RC ECO:0000313|Proteomes:UP000224080};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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 -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC NagA family. {ECO:0000256|ARBA:ARBA00010716}.
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:PGG96090.1}.
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DR EMBL; PDNC01000191; PGG96090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7WHY5; -.
DR STRING; 2060905.A0A2B7WHY5; -.
DR OrthoDB; 2874448at2759; -.
DR Proteomes; UP000224080; Unassembled WGS sequence.
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-EC.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 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 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000224080}.
FT DOMAIN 65..442
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT REGION 196..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 48754 MW; B1A5AA26220FA5C3 CRC64;
MPSIAQAPVS PRITKFTNCR LPLNGQLVEQ DLWVDSATGK ILQDQQAFYE FQLSPDQTVD
LGGRILAPGF IDVQINGARG FDFSVPQATR EEYDAGVRKA SQALVRMGVT SYLPSVTSQE
AAVYKKVLPS LGPSGASRRA EDGAESLGAH VEGPFLSPGK NGIHSSSVLL AATNGFQDLI
DCYGEENLLL PQDVSTPTTA SASASNSSAI STTTTNPSPT IKMITAAPEV GVMNSLIPAL
AAQNIIFSIG HSDATYEQAL DALAAGATMI THLFNAMRPF YHRHPGIFGL LGQQSTQATR
PFYGLIADGI HLHPTSIQIA YHAHPEGMVL VTDAMKLCGM PDGVYEWTNG ERIVKSGALL
TLEGSAEGKI AGSSATLIEC VNNFRRWAGT GVVEAVRAVT ETPARMLGVD AVKGVLTPGA
DADLVVLGED AEGTLSVDQV WKFGVRVFDR EKDGEREEL
//