ID M5J6V9_9LACO Unreviewed; 379 AA.
AC M5J6V9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|EMBL:EKW99740.1};
GN ORFNames=D271_01358 {ECO:0000313|EMBL:EKW99740.1};
OS Ligilactobacillus saerimneri 30a.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1227363 {ECO:0000313|EMBL:EKW99740.1, ECO:0000313|Proteomes:UP000011912};
RN [1] {ECO:0000313|EMBL:EKW99740.1, ECO:0000313|Proteomes:UP000011912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30a {ECO:0000313|EMBL:EKW99740.1,
RC ECO:0000313|Proteomes:UP000011912};
RX PubMed=23405290;
RA Romano A., Trip H., Campbell-Sills H., Bouchez O., Sherman D.,
RA Lolkema J.S., Lucas P.M.;
RT "Genome Sequence of Lactobacillus saerimneri 30a (Formerly Lactobacillus
RT sp. Strain 30a), a Reference Lactic Acid Bacterium Strain Producing
RT Biogenic Amines.";
RL Genome Announc. 1:E00097-E00012(2013).
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}.
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:EKW99740.1}.
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DR EMBL; ANAG01000003; EKW99740.1; -; Genomic_DNA.
DR RefSeq; WP_009551446.1; NZ_ANAG01000003.1.
DR AlphaFoldDB; M5J6V9; -.
DR STRING; 1227363.D271_01358; -.
DR GeneID; 80986182; -.
DR PATRIC; fig|1227363.6.peg.265; -.
DR Proteomes; UP000011912; 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:UP000011912}.
FT DOMAIN 52..365
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 271
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-1"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 195
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 304..306
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
SQ SEQUENCE 379 AA; 41098 MW; 03CCE3927ED2A77E CRC64;
MAKVFKNVTI ATGTEIITDG YIRFDDRVRA VGPMSDFHNE AGDEVTYAHG KVIVPGFIDV
HCHGGYGYDT MDADPEKIDK MVRATAYHEG VTSFFCTTIT QSNENIARAM VGVKQAAKKN
KVIQGIHLEG PFIDAEVKGA QPEKYITQPD AALLDQWNDL AGGLVKIISF APENDGAREL
EDYCIDHGIV PSVGHSMATR QDLLTSKVSH TCHLYNAQSP LSHREPGVAG HTLLQDEMYA
ELIMDGYHIC PDMLQLAYSI KGPEKIELIT DSMRKKGLGD GVSELGGQKV FVEGIHATLA
DGTIAGSVLP FITAFQNAMK FTTAGLYEAV LMSSVNQARE FGLTSKGGLQ VGKDADLNVL
DADYNLLATY SYGELVTAE
//
