NAGB_STAA8
ID NAGB_STAA8 Reviewed; 252 AA.
AC Q2G0K8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=SAOUHSC_00552;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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 -!- 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 -!- 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; CP000253; ABD29699.1; -; Genomic_DNA.
DR RefSeq; WP_000866415.1; NZ_LS483365.1.
DR RefSeq; YP_499124.1; NC_007795.1.
DR AlphaFoldDB; Q2G0K8; -.
DR SMR; Q2G0K8; -.
DR STRING; 1280.SAXN108_0626; -.
DR EnsemblBacteria; ABD29699; ABD29699; SAOUHSC_00552.
DR GeneID; 3920831; -.
DR KEGG; sao:SAOUHSC_00552; -.
DR PATRIC; fig|93061.5.peg.497; -.
DR eggNOG; COG0363; Bacteria.
DR HOGENOM; CLU_049611_1_1_9; -.
DR OMA; FNEPCSS; -.
DR UniPathway; UPA00629; UER00684.
DR PRO; PR:Q2G0K8; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006043; P:glucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
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 Carbohydrate metabolism; Hydrolase; Reference proteome.
FT CHAIN 1..252
FT /note="Glucosamine-6-phosphate deaminase"
FT /id="PRO_1000067024"
FT ACT_SITE 67
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 137
FT /note="For ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 139
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 144
FT /note="For ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
SQ SEQUENCE 252 AA; 28467 MW; C687542EE7E5AD35 CRC64;
MKVLNLGSKK QASFYVACEL YKEMAFNQHC KLGLATGGTM TDLYEQLVKL LNKNQLNVDN
VSTFNLDEYV GLTASHPQSY HYYMDDMLFK QYPYFNRKNI HIPNGDADDM NAEASKYNDV
LEQQGQRDIQ ILGIGENGHI GFNEPGTPFD SVTHIVDLTE STIKANSRYF KNEDDVPKQA
ISMGLANILQ AKRIILLAFG EKKRAAITHL LNQEISVDVP ATLLHKHPNV EIYLDDEACP
KNVAKIHVDE MD