NAGB_ECO57
ID NAGB_ECO57 Reviewed; 266 AA.
AC P0A760; O68603; P09375;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Glucosamine-6-phosphate deaminase;
DE EC=3.5.99.6;
DE AltName: Full=GlcN6P deaminase;
DE Short=GNPDA;
DE AltName: Full=Glucosamine-6-phosphate isomerase;
GN Name=nagB; Synonyms=glmD; OrderedLocusNames=Z0825, ECs0708;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP INDUCTION.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=23634833; DOI=10.1186/1471-2180-13-94;
RA Hu Z., Patel I.R., Mukherjee A.;
RT "Genetic analysis of the roles of agaA, agaI, and agaS genes in the N-
RT acetyl-D-galactosamine and D-galactosamine catabolic pathways in
RT Escherichia coli strains O157:H7 and C.";
RL BMC Microbiol. 13:94-94(2013).
CC -!- FUNCTION: Catalyzes the reversible isomerization-deamination of
CC glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P)
CC and ammonium ion. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-
CC phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6;
CC -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine 6-
CC phosphate (GlcNAc6P). {ECO:0000250}.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 5/5.
CC -!- SUBUNIT: Homohexamer; trimer of disulfide-linked dimers. {ECO:0000250}.
CC -!- INDUCTION: Induced by growth on N-acetyl-D-glucosamine but not by
CC growth on N-acetyl-D-galactosamine. {ECO:0000269|PubMed:23634833}.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. NagB subfamily. {ECO:0000305}.
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DR EMBL; AE005174; AAG55000.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34131.1; -; Genomic_DNA.
DR PIR; D90717; D90717.
DR RefSeq; NP_308735.1; NC_002695.1.
DR RefSeq; WP_001237072.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A760; -.
DR SMR; P0A760; -.
DR STRING; 155864.EDL933_0746; -.
DR EnsemblBacteria; AAG55000; AAG55000; Z0825.
DR EnsemblBacteria; BAB34131; BAB34131; ECs_0708.
DR GeneID; 67416285; -.
DR GeneID; 917077; -.
DR KEGG; ece:Z0825; -.
DR KEGG; ecs:ECs_0708; -.
DR PATRIC; fig|386585.9.peg.820; -.
DR eggNOG; COG0363; Bacteria.
DR HOGENOM; CLU_049611_0_1_6; -.
DR OMA; FNEPCSS; -.
DR UniPathway; UPA00629; UER00684.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:UniProtKB-UniRule.
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 InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR11280; PTHR11280; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00502; nagB; 1.
DR PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme; Carbohydrate metabolism; Disulfide bond; Hydrolase;
KW Reference proteome.
FT CHAIN 1..266
FT /note="Glucosamine-6-phosphate deaminase"
FT /id="PRO_0000160145"
FT ACT_SITE 72
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000250"
FT ACT_SITE 141
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 143
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 148
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
FT SITE 151
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000250"
FT SITE 158
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000250"
FT SITE 160
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000250"
FT SITE 161
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000250"
FT SITE 254
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000250"
FT DISULFID 219
FT /note="Interchain"
FT /evidence="ECO:0000250"
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
