ID   NAGB_LACLS              Reviewed;         235 AA.
AC   Q02Y08;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=LACR_1667;
OS   Lactococcus lactis subsp. cremoris (strain SK11).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=272622;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK11;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000425; ABJ73164.1; -; Genomic_DNA.
DR   RefSeq; WP_011676603.1; NC_008527.1.
DR   AlphaFoldDB; Q02Y08; -.
DR   SMR; Q02Y08; -.
DR   EnsemblBacteria; ABJ73164; ABJ73164; LACR_1667.
DR   KEGG; llc:LACR_1667; -.
DR   HOGENOM; CLU_049611_1_0_9; -.
DR   OMA; FNEPCSS; -.
DR   UniPathway; UPA00629; UER00684.
DR   Proteomes; UP000000240; 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   PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase.
FT   CHAIN           1..235
FT                   /note="Glucosamine-6-phosphate deaminase"
FT                   /id="PRO_1000066996"
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   235 AA;  25689 MW;  7C4BEA288F4CE1DA CRC64;
     MKVIVVKNQL EGGKIGLDLL KESINNGAKT LGLATGSTPV EFYNQIVNSD LDFTNMVSVN
     LDEYVGLDGS NEQSYRYFMT KHLFGEKPFK ENFLPNGKAT DLEAEAKHYD QIIEENPIDW
     QILGIGQNGH IGFNEPGTPA EITTHVVDLQ ESTIKANARF FESEADVPRK AISMGLASIM
     KSKNIVLMAY GKEKAEAIKG MVEGEVTTEL PASILQNHAN VTVIADEAAV SLLSK