(data stored in SCRATCH zone)

SWISSPROT: D6XVV4_BACIE

ID   D6XVV4_BACIE            Unreviewed;       383 AA.
AC   D6XVV4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   SubName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|EMBL:ADH97727.1};
DE            EC=3.5.1.25 {ECO:0000313|EMBL:ADH97727.1};
GN   OrderedLocusNames=Bsel_0179 {ECO:0000313|EMBL:ADH97727.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97727.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97727.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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
CC       superfamily. NagA family. {ECO:0000256|PIRNR:PIRNR038994}.
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DR   EMBL; CP001791; ADH97727.1; -; Genomic_DNA.
DR   RefSeq; WP_013171156.1; NC_014219.1.
DR   STRING; 439292.Bsel_0179; -.
DR   MEROPS; M38.983; -.
DR   EnsemblBacteria; ADH97727; ADH97727; Bsel_0179.
DR   KEGG; bse:Bsel_0179; -.
DR   eggNOG; COG1820; LUCA.
DR   HOGENOM; HOG000275009; -.
DR   KO; K01443; -.
DR   OMA; HAFNAMP; -.
DR   OrthoDB; 1026967at2; -.
DR   BioCyc; BSEL439292:G1GLR-203-MONOMER; -.
DR   Proteomes; UP000000271; 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; 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; D6XVV4.
DR   SWISS-2DPAGE; D6XVV4.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR038994};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR038994,
KW   ECO:0000313|EMBL:ADH97727.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN       55    381       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   REGION      222    223       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR038994-2}.
FT   REGION      310    312       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR038994-2}.
FT   ACT_SITE    277    277       Proton donor/acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR038994-1}.
FT   METAL       132    132       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR038994-3}.
FT   METAL       198    198       Divalent metal cation; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR038994-3}.
FT   METAL       219    219       Divalent metal cation; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR038994-3}.
FT   BINDING     143    143       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR038994-2}.
FT   BINDING     230    230       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR038994-2}.
FT   BINDING     254    254       Substrate; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR038994-2}.
SQ   SEQUENCE   383 AA;  39904 MW;  06C6735B6066F343 CRC64;
     MKNKIYIQGG TVYNADGAPI RQPLITVNSG IIEQITEGGE PPEGADVLRL DGDDVILPGF
     IDIHIHGSHG ADVMDATPEA LATISRSITN EGVTSFLATT ITAPAASIEE ALQQVASSEG
     TDGARCLGVH LEGPFINAKQ AGAQPVGAIL DPDAGQFKHW QALSGNQIRI ATIAPERPGG
     AELVQALADS GVIGSIGHSD ASSADVRAAE QDGLRHATHL FNGMRGLHHR EAGVVGGVML
     SDNLKAELIL DHVHVSPDAA RVAYQALGAN RLMLITDAMR GKGLGDGVFD LGGQEVTIEG
     KEARLKNGAL AGSVLTMDEA VRNARSTFNA SWHDIARMTS YNQAESLGLT GTKGTIQTGA
     DADLTVMSRT GFIKHTIIGG EKP
//

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