(data stored in SCRATCH zone)

SWISSPROT: Q145Z4_PARXL

ID   Q145Z4_PARXL            Unreviewed;       367 AA.
AC   Q145Z4;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 78.
DE   SubName: Full=N-acetylglucosamine 6-phosphate deacetylase {ECO:0000313|EMBL:ABE28845.1};
DE            EC=3.5.1.25 {ECO:0000313|EMBL:ABE28845.1};
GN   ORFNames=Bxe_A4155 {ECO:0000313|EMBL:ABE28845.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28845.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28845.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28845.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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
CC       superfamily. NagA family. {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; CP000270; ABE28845.1; -; Genomic_DNA.
DR   RefSeq; WP_011486678.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4155; -.
DR   EnsemblBacteria; ABE28845; ABE28845; Bxe_A4155.
DR   GeneID; 4002325; -.
DR   KEGG; bxb:DR64_1832; -.
DR   KEGG; bxe:Bxe_A4155; -.
DR   PATRIC; fig|266265.5.peg.325; -.
DR   eggNOG; ENOG4105CE4; Bacteria.
DR   eggNOG; COG1820; LUCA.
DR   HOGENOM; HOG000275009; -.
DR   KO; K01443; -.
DR   OMA; YMKNPRL; -.
DR   OrthoDB; 1026967at2; -.
DR   BioCyc; BXEN266265:BXE_RS01530-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
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; 2.30.40.10; -; 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:SF1; PTHR11113:SF1; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   PIRSF; PIRSF038994; NagA; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR00221; nagA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q145Z4.
DR   SWISS-2DPAGE; Q145Z4.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR038994};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR038994,
KW   ECO:0000313|EMBL:ABE28845.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN       41    349       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   REGION      207    208       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR038994-2}.
FT   REGION      292    294       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR038994-2}.
FT   ACT_SITE    259    259       Proton donor/acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR038994-1}.
FT   METAL       120    120       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR038994-3}.
FT   METAL       183    183       Divalent metal cation; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR038994-3}.
FT   METAL       204    204       Divalent metal cation; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR038994-3}.
FT   BINDING     131    131       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR038994-2}.
FT   BINDING     215    215       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR038994-2}.
FT   BINDING     238    238       Substrate; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR038994-2}.
SQ   SEQUENCE   367 AA;  38825 MW;  5E6F38F28C275BB0 CRC64;
     MLTGNILTTD GWIHGTLEYE NGRITALAGD RVDPSTNDAP YILPGFIDLH VHGGGGADVM
     EGDRAIETIT RTHARYGTTS LLATTMTAPR DELMSVVAGL GHNARIRTPG GARVLGVHLE
     GPYINPGKLG AQPDAAVSAV MDEVLKYLSI APIRVVTLAP EIAGHMEIIS EMAARGVRVQ
     LGHSLGTYDD AVAALKHGAC GFTHLFNAMS PLHHRNPGLV GAALAHAEFA EIIPDLLHVH
     PGAIRAALRA IPRLYVVTDS TSATGMPDGE YRLGSQHVTK CLGGVRLADG TLAGSTLTMD
     QALRNLVSIG LPIADVSNRL SRYAADYLGI EDRGRIARGA WADVVVFDRE LALSATYVEG
     EAIVEYA
//

If you have problems or comments...

PBIL Back to PBIL home page