NAGB_KLEP3
ID NAGB_KLEP3 Reviewed; 266 AA.
AC B5XZG9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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}; OrderedLocusNames=KPK_3874;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
CC -!- FUNCTION: Catalyzes the reversible isomerization-deamination of
CC glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P)
CC and ammonium ion. {ECO:0000255|HAMAP-Rule:MF_01241}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01241};
CC -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine 6-
CC phosphate (GlcNAc6P). {ECO:0000255|HAMAP-Rule:MF_01241}.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 5/5.
CC {ECO:0000255|HAMAP-Rule:MF_01241}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01241}.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. NagB subfamily. {ECO:0000255|HAMAP-Rule:MF_01241}.
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; CP000964; ACI10519.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XZG9; -.
DR SMR; B5XZG9; -.
DR EnsemblBacteria; ACI10519; ACI10519; KPK_3874.
DR KEGG; kpe:KPK_3874; -.
DR HOGENOM; CLU_049611_0_1_6; -.
DR OMA; FNEPCSS; -.
DR OrthoDB; 1828393at2; -.
DR UniPathway; UPA00629; UER00684.
DR Proteomes; UP000001734; 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 3: Inferred from homology;
KW Allosteric enzyme; Carbohydrate metabolism; Hydrolase.
FT CHAIN 1..266
FT /note="Glucosamine-6-phosphate deaminase"
FT /id="PRO_1000139779"
FT ACT_SITE 72
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 141
FT /note="For ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 143
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 148
FT /note="For ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 151
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 158
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 160
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 161
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 254
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
SQ SEQUENCE 266 AA; 29670 MW; 7C149785E43954B2 CRC64;
MRLIPLVTAE QVGKWAARHI VNRINAFKPT ADRPFVLGLP TGGTPLTAYK ALVEMHKAGQ
VSFKHVVTFN MDEYVGLPKE HPESYHSFMH RNFFDHVDIP AENINLLNGN APDIDAECRR
YEEKIRSYGK IHLFMGGVGN DGHIAFNEPA SSLASRTRIK TLTHDTRVAN SRFFDGDVDL
VPKYALTVGV GTLLDAEEVM ILVLGHQKAL ALQAAVEGNV NHMWTITCLQ LHPKAVIVCD
EPSTMELKVK TLKYFNELEA ENIKGL
