ID C1A231_RHOE4 Unreviewed; 413 AA.
AC C1A231;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Probable N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|EMBL:BAH34666.1};
DE EC=3.5.1.25 {ECO:0000313|EMBL:BAH34666.1};
GN Name=nagA {ECO:0000313|EMBL:BAH34666.1};
GN OrderedLocusNames=RER_39580 {ECO:0000313|EMBL:BAH34666.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH34666.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH34666.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008957; BAH34666.1; -; Genomic_DNA.
DR RefSeq; WP_020908317.1; NC_012490.1.
DR AlphaFoldDB; C1A231; -.
DR KEGG; rer:RER_39580; -.
DR PATRIC; fig|234621.6.peg.4491; -.
DR eggNOG; COG1820; Bacteria.
DR HOGENOM; CLU_032482_1_2_11; -.
DR Proteomes; UP000002204; 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 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:BAH34666.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3}.
FT DOMAIN 64..391
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 294
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-1"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 236..237
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 332..334
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
SQ SEQUENCE 413 AA; 41917 MW; 65AB7C0375BE30D1 CRC64;
MSTSGSAAVG DPLVLRGTVI GSPIGKIHDG VVVADGEKIS WVGSAADYVA SAPVVVIPER
TDTVIMPGLI DVHSHGAAGA GFPNTDADGA SRAAAHHCEH GTTGMLASLV SAPRADLVRQ
ATMLADLVER GELLGIHLEG PFINGVRCGA QDPAAIVPGD PDLLEAVCDA ARGTVRSMTL
APETENFEEL LAIMRHRNIV PSFGHTDADA ATTSARIDAA VHGDWAGQIS ATHLFNGMPP
LHHRSPGPVA ACLAAAARGE MVVELIADGV HLAPETVSMV FDAVGPDQIA LVSDSMAAAG
MDDGDYQLGA LDVTVADGVA RLATTDGSSG AIAGGTARLL DVLRSTVLDG GVALEDAVAA
ATRSPARLLG LGDLIGSLAV GCRADIVVTD RQLRPGRVLL GGKAAGKEKS WKS
//
