ID   NAGB_LACAC              Reviewed;         239 AA.
AC   Q5FHT1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=LBA1948;
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV43743.1; -; Genomic_DNA.
DR   RefSeq; WP_003549469.1; NC_006814.3.
DR   RefSeq; YP_194774.1; NC_006814.3.
DR   AlphaFoldDB; Q5FHT1; -.
DR   SMR; Q5FHT1; -.
DR   STRING; 272621.LBA1948; -.
DR   EnsemblBacteria; AAV43743; AAV43743; LBA1948.
DR   GeneID; 56943495; -.
DR   KEGG; lac:LBA1948; -.
DR   PATRIC; fig|272621.13.peg.1852; -.
DR   eggNOG; COG0363; Bacteria.
DR   HOGENOM; CLU_049611_1_0_9; -.
DR   OMA; FNEPCSS; -.
DR   BioCyc; LACI272621:G1G49-1899-MON; -.
DR   UniPathway; UPA00629; UER00684.
DR   Proteomes; UP000006381; 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..239
FT                   /note="Glucosamine-6-phosphate deaminase"
FT                   /id="PRO_1000066990"
FT   ACT_SITE        62
FT                   /note="Proton acceptor; for enolization step"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT   ACT_SITE        128
FT                   /note="For ring-opening step"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT   ACT_SITE        130
FT                   /note="Proton acceptor; for ring-opening step"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT   ACT_SITE        135
FT                   /note="For ring-opening step"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
SQ   SEQUENCE   239 AA;  26756 MW;  A0AFC009864ED497 CRC64;
     MKVIVTENKI QGSAKAFEIF EKGIKNGAKV LGLATGSTPE ILYQNWVKSD LNCDDLTSIN
     LDEYVGLTPD NPQSYHYFMQ KHLFDKKTFK KTYIPDGMTK DVPAYCKEYD QIIKDNPIDI
     QLLGIGQNGH IAFNEPGTPF DIGTHEVKLT ENTIKANARF FDNEDEVPKS AICMGTANIM
     DSKKIVLMAF GEKKAKAIKE MIEGPITEEV PASILQKHPD VTVIVDTYAA QELDDKYKN