ID Q98DC3_RHILO Unreviewed; 390 AA.
AC Q98DC3;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000256|ARBA:ARBA00011899};
DE EC=3.5.1.25 {ECO:0000256|ARBA:ARBA00011899};
GN OrderedLocusNames=mll4766 {ECO:0000313|EMBL:BAB51348.1};
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB51348.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB51348.1, ECO:0000313|Proteomes:UP000000552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC {ECO:0000313|Proteomes:UP000000552};
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-
CC glucosamine 6-phosphate; 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|ARBA:ARBA00001570};
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; BA000012; BAB51348.1; -; Genomic_DNA.
DR RefSeq; WP_010912690.1; NC_002678.2.
DR AlphaFoldDB; Q98DC3; -.
DR KEGG; mlo:mll4766; -.
DR PATRIC; fig|266835.9.peg.3764; -.
DR eggNOG; COG1820; Bacteria.
DR HOGENOM; CLU_032482_2_2_5; -.
DR Proteomes; UP000000552; Chromosome.
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: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}; Hydrolase {ECO:0000256|PIRNR:PIRNR038994};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3}.
FT DOMAIN 53..382
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 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 221..222
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 253
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 390 AA; 40090 MW; AC312A11F1A9F688 CRC64;
MSDRFALTGA RIFDGDDWHD DAALVVRDGL VEAIVPSGAI ARDVRAVDTG GGMLVPGFVD
IQVNGGGGVM LNDHPDVASI ETICRAHAPF GTTALLPTLI TDTPAITAAA IAAGEAAALQ
KVPSFLGLHL EGPHLSIARK GAHDPALIRP MTDADQVMLI AARPKLPVLL TTIAPESVDP
TRVAALAKAG IIVSLGHSDT GYATAKGFAE AGAAVVTHLF NAMSQIGNRE PGLVGAAIDI
GTLSAGLIAD GIHVHPAAIR IALDAKQGPG KIVLVTDAMA TIGTDMTSFT LNGRTIYRKD
GSLRLADGTL AGADLDMISA VRFMHNIVGV DLSEALRMAS LYPAQAIGQS HRLGRLANGT
VADIVALSDG LDIRSVWIGG DKVFEAGASR
//
