ID R8VUN9_9CLOT Unreviewed; 382 AA.
AC R8VUN9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|EMBL:EOQ36199.1};
GN ORFNames=HMPREF1526_02231 {ECO:0000313|EMBL:EOQ36199.1};
OS Butyricicoccus pullicaecorum 1.2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Butyricicoccus.
OX NCBI_TaxID=1203606 {ECO:0000313|EMBL:EOQ36199.1, ECO:0000313|Proteomes:UP000013981};
RN [1] {ECO:0000313|EMBL:EOQ36199.1, ECO:0000313|Proteomes:UP000013981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1.2 {ECO:0000313|EMBL:EOQ36199.1,
RC ECO:0000313|Proteomes:UP000013981};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Van Immerseel F., Eeckhaut V.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Butyricicoccus pullicaecorum 1.2.";
RL Submitted (JAN-2013) 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}.
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:EOQ36199.1}.
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DR EMBL; AQOB01000008; EOQ36199.1; -; Genomic_DNA.
DR RefSeq; WP_016148354.1; NZ_KB976104.1.
DR AlphaFoldDB; R8VUN9; -.
DR PATRIC; fig|1203606.4.peg.2195; -.
DR eggNOG; COG1820; Bacteria.
DR HOGENOM; CLU_032482_2_1_9; -.
DR OrthoDB; 9776488at2; -.
DR Proteomes; UP000013981; 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:UP000013981}.
FT DOMAIN 45..377
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 269
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-1"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 214..215
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 305..307
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
SQ SEQUENCE 382 AA; 41687 MW; A1D456218E7F074A CRC64;
MILQSKKVWM ADRFVPAQIV VEDGKIAEIY PYGTKEADVD YGDQWVLPGF IDVHCHGAFG
FDTNDAEPEG LRKWLRGIVK EGVTSLLPTT ITQSEEVLTK ALENVANVVE EGYTGAEVLG
VHFEGPFLDM LYKGAQPEQH IKRPAVEQFK RYQEAAHGLI KYITMATEND EDFALTRYCT
ETGVVVSIGH SAATFDQAVM ACAHGARSMT HVYNGMSPFN HRQNGLVGAA YNIKSMYGEI
ICDGNHSTPA ALKQFFELKG PHYGMMVSDA LMAKGSPAGS KFLFGGNEIE IYPDGSAHLT
STKGLAGSTL CINKGLRLLI EEAMVPIETA INSCTKNPAE CLRVADRKGS IKVGLDADLV
VLDRDYEVVQ TYCAGKSMLD GE
//
