ID   NAGB_BACTN              Reviewed;         270 AA.
AC   Q8A094;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Glucosamine-6-phosphate deaminase;
DE            EC=3.5.99.6;
DE   AltName: Full=GlcN6P deaminase;
DE            Short=GNPDA;
DE   AltName: Full=Glucosamine-6-phosphate isomerase;
GN   Name=nagB; OrderedLocusNames=BT_4127;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
CC   -!- FUNCTION: Catalyzes the reversible isomerization-deamination of
CC       glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P)
CC       and ammonium ion. {ECO:0000250}.
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   -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine 6-
CC       phosphate (GlcNAc6P). {ECO:0000250}.
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC       fructose 6-phosphate from N-acetylneuraminate: step 5/5.
CC   -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC       isomerase family. NagB subfamily. {ECO:0000305}.
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DR   EMBL; AE015928; AAO79232.1; -; Genomic_DNA.
DR   RefSeq; NP_813038.1; NC_004663.1.
DR   RefSeq; WP_008761009.1; NZ_UYXG01000005.1.
DR   AlphaFoldDB; Q8A094; -.
DR   SMR; Q8A094; -.
DR   STRING; 226186.BT_4127; -.
DR   PaxDb; Q8A094; -.
DR   PRIDE; Q8A094; -.
DR   EnsemblBacteria; AAO79232; AAO79232; BT_4127.
DR   GeneID; 60925302; -.
DR   KEGG; bth:BT_4127; -.
DR   PATRIC; fig|226186.12.peg.4194; -.
DR   eggNOG; COG0363; Bacteria.
DR   HOGENOM; CLU_049611_0_1_10; -.
DR   InParanoid; Q8A094; -.
DR   OMA; FNEPCSS; -.
DR   UniPathway; UPA00629; UER00684.
DR   Proteomes; UP000001414; 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   Allosteric enzyme; Carbohydrate metabolism; Hydrolase; Reference proteome.
FT   CHAIN           1..270
FT                   /note="Glucosamine-6-phosphate deaminase"
FT                   /id="PRO_0000160135"
FT   ACT_SITE        72
FT                   /note="Proton acceptor; for enolization step"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        141
FT                   /note="For ring-opening step"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        143
FT                   /note="Proton acceptor; for ring-opening step"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        148
FT                   /note="For ring-opening step"
FT                   /evidence="ECO:0000250"
FT   SITE            151
FT                   /note="Part of the allosteric site"
FT                   /evidence="ECO:0000250"
FT   SITE            158
FT                   /note="Part of the allosteric site"
FT                   /evidence="ECO:0000250"
FT   SITE            160
FT                   /note="Part of the allosteric site"
FT                   /evidence="ECO:0000250"
FT   SITE            161
FT                   /note="Part of the allosteric site"
FT                   /evidence="ECO:0000250"
FT   SITE            254
FT                   /note="Part of the allosteric site"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   270 AA;  29939 MW;  509B4CCD75B95265 CRC64;
     MRLIIQPDYQ SVSQWAAHYV AAKIKAANPT PEKPFVLGCP TGSSPLGMYK ALIDLNKKGI
     VSFQNVVTFN MDEYVGLPKE HPESYYSFMW NNFFSHIDIK KENTNILNGN APDLDAECAR
     YEEKIKSYGG IDLFMGGIGP DGHIAFNEPG SSLTSRTRQK TLTTDTIIAN SRFFDNDINK
     VPKTALTVGV GTVLSAKEVM IIVNGHNKAR ALYHAVEGSI TQMWTISALQ MHEKGIIVCD
     DAATEELKVG TYRYFKDIEA GHLDPESLIK