ID F2NAK1_CORGP Unreviewed; 383 AA.
AC F2NAK1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=N-acetylglucosamine 6-phosphate deacetylase {ECO:0000313|EMBL:AEB06528.1};
DE EC=3.5.1.25 {ECO:0000313|EMBL:AEB06528.1};
GN OrderedLocusNames=Corgl_0410 {ECO:0000313|EMBL:AEB06528.1};
OS Coriobacterium glomerans (strain ATCC 49209 / DSM 20642 / JCM 10262 / PW2).
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Coriobacterium.
OX NCBI_TaxID=700015 {ECO:0000313|EMBL:AEB06528.1, ECO:0000313|Proteomes:UP000006851};
RN [1] {ECO:0000313|Proteomes:UP000006851}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 49209 / DSM 20642 / JCM 10262 / PW2
RC {ECO:0000313|Proteomes:UP000006851};
RX PubMed=23961308; DOI=10.4056/sigs.3507020;
RA Stackebrandt E., Zeytun A., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Chang Y.J., Land M., Hauser L., Rohde M.,
RA Pukall R., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Coriobacterium glomerans type strain (PW2(T))
RT from the midgut of Pyrrhocoris apterus L. (red soldier bug).";
RL Stand. Genomic Sci. 8:15-25(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}.
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DR EMBL; CP002628; AEB06528.1; -; Genomic_DNA.
DR RefSeq; WP_013708271.1; NC_015389.1.
DR AlphaFoldDB; F2NAK1; -.
DR STRING; 700015.Corgl_0410; -.
DR KEGG; cgo:Corgl_0410; -.
DR eggNOG; COG1820; Bacteria.
DR HOGENOM; CLU_032482_2_1_11; -.
DR OrthoDB; 9776488at2; -.
DR Proteomes; UP000006851; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047419; F:N-acetylgalactosamine-6-phosphate deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IEA:UniProtKB-EC.
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|PIRNR:PIRNR038994, ECO:0000313|EMBL:AEB06528.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000006851}.
FT DOMAIN 50..379
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 273
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 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 217..218
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 307..309
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
SQ SEQUENCE 383 AA; 40981 MW; C0CE1A67DB482BEA CRC64;
MGRYAVLADR FYFPTHTLDG GYLLVEDGMF GEHVEKEPDC EILDRRGCHV APGFVDTHIH
GYGDCDVMDG TWDSVHTIAK RILENGVTSW LPTTLTATAE QLDAACHGVA DRIDENTGAR
IQGIFLEGPF FTEKHKGAQN PAYLSAPAIE KLKRWQSSAK GLVKKIAIAA EFPDSPAFIR
AAREMGVVVA LGHSDAGVSD ALHCLDAGAR VFVHTYNGMS PLHHREPGMV GAALYSGHRT
YSELICDGHH VNPIAASIVM QCKGHDHCVL ITDCMRAGGM PDGDYLLGEL PVVVAGGTAR
LKDAGSLAGS ILRLNDAVKH VVAWGIATPA QAIDMATRVA AEANEIGDVC GSIQAGRAAD
FVVLEPDLTL SETFLGGKSV YRR
//
