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Database: UniProt
Entry: A0A1I4FJI8_9FIRM
LinkDB: A0A1I4FJI8_9FIRM
Original site: A0A1I4FJI8_9FIRM 
ID   A0A1I4FJI8_9FIRM        Unreviewed;       387 AA.
AC   A0A1I4FJI8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=N-acetylgalactosamine 6-phosphate deacetylase {ECO:0000313|EMBL:SFL18084.1};
GN   ORFNames=SAMN02983006_00392 {ECO:0000313|EMBL:SFL18084.1};
OS   Halanaerobium salsuginis.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=29563 {ECO:0000313|EMBL:SFL18084.1, ECO:0000313|Proteomes:UP000199006};
RN   [1] {ECO:0000313|EMBL:SFL18084.1, ECO:0000313|Proteomes:UP000199006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51327 {ECO:0000313|EMBL:SFL18084.1,
RC   ECO:0000313|Proteomes:UP000199006};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOTI01000003; SFL18084.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4FJI8; -.
DR   STRING; 29563.SAMN02983006_00392; -.
DR   OrthoDB; 9776488at2; -.
DR   Proteomes; UP000199006; 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:UP000199006}.
FT   DOMAIN          54..383
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   ACT_SITE        277
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-1"
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         199
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         220
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         223..224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         310..312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
SQ   SEQUENCE   387 AA;  42078 MW;  76DE7C2D24590229 CRC64;
     MKYYLKSEQI FLENRILKNA YLLIEDEIIK DIFSCSENKS LNKNLKIIDL GSKIIAPGLI
     DLHIHGAVGK DVMDADYESL NSISQFLAKN GVTSFLATTL TSPLSKIKSA LQNVKLGIEK
     GVDGAKILGI YLEGPYLTPE HNGAHPVEFM REINLQEIDE LIDLSGNNIM VVALAPEKDL
     ASQITEYLTE KGIKVTIAHT NASYEETKKT INCGANIATH TFNGMTGLHH RAPGAVGAIL
     SSAEVYSELI ADKIHVHPAV IKILYKVKNN KLMLISDCIR AGGLADGNYK LGELDIKVHD
     SIARTETGSL AGSTLKIREA ILNIKDSAEL SLFDSLKLAT LTPAAAIGLA EEIGSIEIGK
     KADLIAIDKK MNVYLTIING KIIYNNL
//
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