NAGB_MYCPU
ID NAGB_MYCPU Reviewed; 256 AA.
AC Q98QJ9;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=MYPU_3620;
OS Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=272635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAB CTIP;
RX PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT pulmonis.";
RL Nucleic Acids Res. 29:2145-2153(2001).
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; AL445564; CAC13535.1; -; Genomic_DNA.
DR PIR; B90557; B90557.
DR RefSeq; WP_010925166.1; NC_002771.1.
DR AlphaFoldDB; Q98QJ9; -.
DR SMR; Q98QJ9; -.
DR STRING; 272635.MYPU_3620; -.
DR EnsemblBacteria; CAC13535; CAC13535; CAC13535.
DR KEGG; mpu:MYPU_3620; -.
DR eggNOG; COG0363; Bacteria.
DR HOGENOM; CLU_049611_1_1_14; -.
DR OMA; NSYRYYM; -.
DR OrthoDB; 1828393at2; -.
DR BioCyc; MPUL272635:G1GT6-370-MON; -.
DR UniPathway; UPA00629; UER00684.
DR Proteomes; UP000000528; 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 Carbohydrate metabolism; Hydrolase; Reference proteome.
FT CHAIN 1..256
FT /note="Glucosamine-6-phosphate deaminase"
FT /id="PRO_0000160156"
FT ACT_SITE 68
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 256 AA; 29281 MW; 409C382461F498CB CRC64;
MREIYIFKDL QDLHKFSAKQ IIDQIKIKKD STLGFATGKT PLKTYQLLVK DHQENKTSWK
DITSFNLDEF VDIDPSHPES FIKQMKSNLF DHLDINEQKI NIPKSNSSNP DQEALNYENK
IRKNNGIDLQ FISIGVNGHI AYNEPGTPKD SLTHVSNLTK ETILDLIAKN KFSSIDEVPK
KAITMGVKTI LNQCKKIMMV SFGKEKAQVT KQMLEDKPNE NVTASFLQEH PNCIYILDKE
AASLLNEETL KKAKWI
