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Database: UniProt
Entry: A0A1K1PJU7_9BACL
LinkDB: A0A1K1PJU7_9BACL
Original site: A0A1K1PJU7_9BACL 
ID   A0A1K1PJU7_9BACL        Unreviewed;       396 AA.
AC   A0A1K1PJU7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|EMBL:SFW47707.1};
GN   ORFNames=SAMN02799630_03485 {ECO:0000313|EMBL:SFW47707.1};
OS   Paenibacillus sp. UNCCL117.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1502764 {ECO:0000313|EMBL:SFW47707.1, ECO:0000313|Proteomes:UP000182480};
RN   [1] {ECO:0000313|EMBL:SFW47707.1, ECO:0000313|Proteomes:UP000182480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UNCCL117 {ECO:0000313|EMBL:SFW47707.1,
RC   ECO:0000313|Proteomes:UP000182480};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FPIU01000012; SFW47707.1; -; Genomic_DNA.
DR   RefSeq; WP_072332133.1; NZ_FPIU01000012.1.
DR   AlphaFoldDB; A0A1K1PJU7; -.
DR   STRING; 1502764.SAMN02799630_03485; -.
DR   OrthoDB; 9776488at2; -.
DR   Proteomes; UP000182480; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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:SF16; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR038994};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182480}.
FT   DOMAIN          64..384
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   ACT_SITE        286
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-1"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         228
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         231..232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         316..318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
SQ   SEQUENCE   396 AA;  42084 MW;  CEBAD313E532430B CRC64;
     MATGKALYRN ARVYTPGGPI KDGYVLVGTD GVIEAVGQMP GGEEEEKDTI LKLAGEVDCG
     GMLLVPGFID IHVHGGGGFD VLSGLPEELD GMSRFHAEHG TTAFLATTAT VEHKRLLHAL
     SQAGASVGQT SGAELCGIHL EGPFICKARR GAQSLEAIRL PDPEIMETYL EAASGNIRLV
     TLAPEVEGGL EAVRYLISQG ITVSAGHTDA TYEQMRRAVE AGVSQTTHHF NGMRPMHHRE
     PGAAGAGLLL DELTTELICD GVHVHPAAVK LLFDVKRPER VCLITDALFC AGLPDGSYGD
     IVVRGGENML ADGSSLAGSS LTMLQALRNA LKYTGRTLEE LLPSLTSVPA RQAGLQRHKG
     ELKAGKHADF LLLDAELQLQ ATFVRGQLVY RRRTAG
//
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