NAGB_SALG2
ID NAGB_SALG2 Reviewed; 266 AA.
AC B5R824;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=SG0681;
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(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}.
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DR EMBL; AM933173; CAR36577.1; -; Genomic_DNA.
DR RefSeq; WP_001237059.1; NC_011274.1.
DR AlphaFoldDB; B5R824; -.
DR SMR; B5R824; -.
DR EnsemblBacteria; CAR36577; CAR36577; SG0681.
DR KEGG; seg:SG0681; -.
DR HOGENOM; CLU_049611_0_1_6; -.
DR OMA; FNEPCSS; -.
DR UniPathway; UPA00629; UER00684.
DR Proteomes; UP000008321; 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_1000139787"
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; 29632 MW; 24C779A7178AF1D7 CRC64;
MRLIPLSTAE QVGKWAARHI VNRINAFKPT ADRPFVLGLP TGGTPLTAYK ALVEMHKAGE
VSFKHVVTFN MDEYVGLPKE HPESYHSFMH RNFFDHVDIP AENINLLNGN APDIDAECRQ
YEEKIRSYGK IHLFMGGVGN DGHIAFNEPA SSLASRTRIK TLTHDTRVAN SRFFDGDVNQ
VPKYALTVGV GTLLDAEEVM ILVLGHQKAQ ALQAAVEGNV NHMWTISCLQ LHPKAVVVCD
EPSTMELKVK TLKYFNELEA ENIKGL
