ID   A5FCT2_FLAJ1            Unreviewed;       374 AA.
AC   A5FCT2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   02-SEP-2026, entry version 98.
DE   SubName: Full=Candidate N-acetylglucosamine-6-phosphate deacetylase Carbohydrate esterase family 9 {ECO:0000313|EMBL:ABQ06984.1};
DE            EC=3.5.1.25 {ECO:0000313|EMBL:ABQ06984.1};
GN   OrderedLocusNames=Fjoh_3974 {ECO:0000313|EMBL:ABQ06984.1};
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / BCRC
OS   14874 / CCUG 350202 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga
OS   johnsonae).
OC   Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ06984.1, ECO:0000313|Proteomes:UP000006694};
RN   [1] {ECO:0000313|EMBL:ABQ06984.1, ECO:0000313|Proteomes:UP000006694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / BCRC 14874 / CCUG 350202 /
RC   NBRC 14942 / NCIMB 11054 / UW101 {ECO:0000313|Proteomes:UP000006694};
RX   PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
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; CP000685; ABQ06984.1; -; Genomic_DNA.
DR   RefSeq; WP_012025950.1; NC_009441.1.
DR   AlphaFoldDB; A5FCT2; -.
DR   STRING; 376686.Fjoh_3974; -.
DR   GeneID; 31766893; -.
DR   KEGG; fjo:Fjoh_3974; -.
DR   eggNOG; COG1820; Bacteria.
DR   HOGENOM; CLU_032482_2_2_10; -.
DR   OrthoDB; 9776488at2; -.
DR   Proteomes; UP000006694; Chromosome.
DR   GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006046; P:N-acetylglucosamine catabolic process; IEA:TreeGrafter.
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   Pfam; PF22643; NagA_N; 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:UP000006694}.
FT   DOMAIN          52..360
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   ACT_SITE        270
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-1"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         138
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         248
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   374 AA;  41270 MW;  CD709BB83AD92D1E CRC64;
     MKQAIVNAII HTGDEIIDNG VIIIENGTIL SVQKEIPNDI KTIDLQGKHI GAGFIDIQIN
     GGEKHYFSQT PNEETIQDIY NSSLKYGTTH VLPCLISSSK ETILQGIEAA RNYIKKHNNG
     VIGMHLEGPF LNPLKRGAHS IDQVRKPTNA ELEEIIKHGK DVIKVITIAP ECFTDEQLNM
     LLESGITISA GHSTMGYKEA QHYFSKGINL VTHLFNAMTQ FGHREPGLVG AVFENEKVYA
     PIILDGAHCD YAAAKVAYKL KQEKFFLISD ATFLGRKVEN FKWDNFDAHL ENGFYRNEDG
     NLAGATISML EAVQNAYNHL NVSADEALKM ATSRVAAAIG LENKIGKIKT GFPASFVKFN
     DNLSEIETLN FPAV
//