ID   NAGB_CLOBL              Reviewed;         244 AA.
AC   A7GH51;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=CLI_2883;
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F;
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA   Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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; CP000728; ABS40107.1; -; Genomic_DNA.
DR   RefSeq; WP_003400051.1; NC_009699.1.
DR   AlphaFoldDB; A7GH51; -.
DR   SMR; A7GH51; -.
DR   EnsemblBacteria; ABS40107; ABS40107; CLI_2883.
DR   KEGG; cbf:CLI_2883; -.
DR   HOGENOM; CLU_049611_1_1_9; -.
DR   OMA; FNEPCSS; -.
DR   UniPathway; UPA00629; UER00684.
DR   Proteomes; UP000002410; 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.
FT   CHAIN           1..244
FT                   /note="Glucosamine-6-phosphate deaminase"
FT                   /id="PRO_1000066969"
FT   ACT_SITE        67
FT                   /note="Proton acceptor; for enolization step"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT   ACT_SITE        136
FT                   /note="For ring-opening step"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT   ACT_SITE        138
FT                   /note="Proton acceptor; for ring-opening step"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT   ACT_SITE        143
FT                   /note="For ring-opening step"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
SQ   SEQUENCE   244 AA;  27302 MW;  95CEC7142EED424F CRC64;
     MRIIVVDNYE EMSKKAAAMI ASQVILKPDS VLGLATGDTP IGMYKEIINI YKNEKMNFSK
     VKTFNLDEYY GLNRENPQSY YYYMMNNLFN HVNIDKNNIN IPNGMADNIE VECKEYERKI
     DKAGGIDLQI LGIGVNGHIG FNEPNISFES ETHLVNLNEK TIESNSRFFS SKEEVPTKAI
     SMGIKSIIHS KKIILLACGS AKSDAVSKAI NGKINPNIPA SILQLHRDVV VIIDKEAASK
     LKLK