ID   A1SS80_PSYIN            Unreviewed;       377 AA.
AC   A1SS80;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 99.
DE   RecName: Full=N-acetylgalactosamine-6-phosphate deacetylase {ECO:0000256|PIRNR:PIRNR038994};
DE            EC=3.5.1.25 {ECO:0000256|PIRNR:PIRNR038994};
DE   AltName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000256|PIRNR:PIRNR038994};
GN   OrderedLocusNames=Ping_0489 {ECO:0000313|EMBL:ABM02345.1};
OS   Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM02345.1, ECO:0000313|Proteomes:UP000000639};
RN   [1] {ECO:0000313|EMBL:ABM02345.1, ECO:0000313|Proteomes:UP000000639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37 {ECO:0000313|EMBL:ABM02345.1,
RC   ECO:0000313|Proteomes:UP000000639};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-
CC         phosphate + acetate; 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|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   -!- 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; CP000510; ABM02345.1; -; Genomic_DNA.
DR   RefSeq; WP_011768904.1; NC_008709.1.
DR   AlphaFoldDB; A1SS80; -.
DR   STRING; 357804.Ping_0489; -.
DR   KEGG; pin:Ping_0489; -.
DR   eggNOG; COG1820; Bacteria.
DR   HOGENOM; CLU_032482_2_2_6; -.
DR   OrthoDB; 9776488at2; -.
DR   Proteomes; UP000000639; Chromosome.
DR   GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006046; P:N-acetylglucosamine catabolic process; IEA:TreeGrafter.
DR   CDD; cd00854; NagA; 1.
DR   FunFam; 3.20.20.140:FF:000004; N-acetylglucosamine-6-phosphate deacetylase; 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   NCBIfam; NF008371; PRK11170.1; 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   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|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038994-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000639}.
FT   DOMAIN          51..372
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   ACT_SITE        269
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-1"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         216..217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         302..304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
SQ   SEQUENCE   377 AA;  40548 MW;  57330288317027DE CRC64;
     MYALTNCKIY TTDAVLLEHA VIVKNNKIDS VIPIAELSST IKKIDLLGAN LSPGFIDLQL
     NGCGGVMFNN EITEKTLAIM QSTNLKSGCT SYLPTLITSS DEDMRTALKV TRDYINKKPN
     EVLGLHLEGP YLSIERKGIH RSEYIRKADI SMLDLICQNA DIVSKVTIAP EKNSVEVIQR
     LSKAGIVVAI GHTNATYAQA AVAIDNGATF ATHLFNAMTP MTGREPGVIG AIYDKNIYAG
     IIVDGFHVAY ENVRISKKIM AEKLILVTDA TAPAGADIEQ FDFVGTTVYY KDGKCFAADG
     TLGGSALTMI EAIEKSVKFV GIELAEAVRM ATLYPARAMS IANKIGSIKS GNIANLAIFS
     SDYKVTGTVL NGVYKAS
//