(data stored in ACNUC7421 zone)

SWISSPROT: NAGB_ECODH

ID   NAGB_ECODH              Reviewed;         266 AA.
AC   B1X6L1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 59.
DE   RecName: Full=Glucosamine-6-phosphate deaminase {ECO:0000255|HAMAP-Rule:MF_01241};
DE            EC=3.5.99.6 {ECO:0000255|HAMAP-Rule:MF_01241};
DE   AltName: Full=GlcN6P deaminase {ECO:0000255|HAMAP-Rule:MF_01241};
DE            Short=GNPDA {ECO:0000255|HAMAP-Rule:MF_01241};
DE   AltName: Full=Glucosamine-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01241};
GN   Name=nagB {ECO:0000255|HAMAP-Rule:MF_01241};
GN   OrderedLocusNames=ECDH10B_0743;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Catalyzes the reversible isomerization-deamination of
CC       glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate
CC       (Fru6P) and ammonium ion. {ECO:0000255|HAMAP-Rule:MF_01241}.
CC   -!- CATALYTIC ACTIVITY: Alpha-D-glucosamine 6-phosphate + H(2)O = D-
CC       fructose 6-phosphate + NH(3). {ECO:0000255|HAMAP-Rule:MF_01241}.
CC   -!- ENZYME REGULATION: Allosterically activated by N-acetylglucosamine
CC       6-phosphate (GlcNAc6P). {ECO:0000255|HAMAP-Rule:MF_01241}.
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation;
CC       D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
CC       {ECO:0000255|HAMAP-Rule:MF_01241}.
CC   -!- SUBUNIT: Homohexamer; trimer of disulfide-linked dimers.
CC       {ECO:0000255|HAMAP-Rule:MF_01241}.
CC   -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC       isomerase family. NagB subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01241}.
DR   EMBL; CP000948; ACB01889.1; -; Genomic_DNA.
DR   RefSeq; WP_001237072.1; NC_010473.1.
DR   ProteinModelPortal; B1X6L1; -.
DR   SMR; B1X6L1; -.
DR   EnsemblBacteria; ACB01889; ACB01889; ECDH10B_0743.
DR   KEGG; ecd:ECDH10B_0743; -.
DR   eggNOG; ENOG4105CKA; Bacteria.
DR   eggNOG; COG0363; LUCA.
DR   HOGENOM; HOG000064979; -.
DR   KO; K02564; -.
DR   OMA; AFQQHAN; -.
DR   UniPathway; UPA00629; UER00684.
DR   GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:InterPro.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01399; GlcN6P_deaminase; 1.
DR   HAMAP; MF_01241; GlcN6P_deamin; 1.
DR   InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR   InterPro; IPR004547; Glucosamine6P_isomerase.
DR   InterPro; IPR018321; Glucosamine6P_isomerase_CS.
DR   PANTHER; PTHR11280; PTHR11280; 1.
DR   Pfam; PF01182; Glucosamine_iso; 1.
DR   TIGRFAMs; TIGR00502; nagB; 1.
DR   PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1X6L1.
DR   SWISS-2DPAGE; B1X6L1.
KW   Allosteric enzyme; Carbohydrate metabolism; Disulfide bond; Hydrolase.
FT   CHAIN         1    266       Glucosamine-6-phosphate deaminase.
FT                                /FTId=PRO_1000139772.
FT   ACT_SITE     72     72       Proton acceptor; for enolization step.
FT                                {ECO:0000255|HAMAP-Rule:MF_01241}.
FT   ACT_SITE    141    141       For ring-opening step.
FT                                {ECO:0000255|HAMAP-Rule:MF_01241}.
FT   ACT_SITE    143    143       Proton acceptor; for ring-opening step.
FT                                {ECO:0000255|HAMAP-Rule:MF_01241}.
FT   ACT_SITE    148    148       For ring-opening step.
FT                                {ECO:0000255|HAMAP-Rule:MF_01241}.
FT   SITE        151    151       Part of the allosteric site.
FT                                {ECO:0000255|HAMAP-Rule:MF_01241}.
FT   SITE        158    158       Part of the allosteric site.
FT                                {ECO:0000255|HAMAP-Rule:MF_01241}.
FT   SITE        160    160       Part of the allosteric site.
FT                                {ECO:0000255|HAMAP-Rule:MF_01241}.
FT   SITE        161    161       Part of the allosteric site.
FT                                {ECO:0000255|HAMAP-Rule:MF_01241}.
FT   SITE        254    254       Part of the allosteric site.
FT                                {ECO:0000255|HAMAP-Rule:MF_01241}.
FT   DISULFID    219    219       Interchain. {ECO:0000255|HAMAP-
FT                                Rule:MF_01241}.
SQ   SEQUENCE   266 AA;  29774 MW;  D1443A40E74AC08E CRC64;
     MRLIPLTTAE QVGKWAARHI VNRINAFKPT ADRPFVLGLP TGGTPMTTYK ALVEMHKAGQ
     VSFKHVVTFN MDEYVGLPKE HPESYYSFMH RNFFDHVDIP AENINLLNGN APDIDAECRQ
     YEEKIRSYGK IHLFMGGVGN DGHIAFNEPA SSLASRTRIK TLTHDTRVAN SRFFDNDVNQ
     VPKYALTVGV GTLLDAEEVM ILVLGSQKAL ALQAAVEGCV NHMWTISCLQ LHPKAIMVCD
     EPSTMELKVK TLRYFNELEA ENIKGL
//

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