ID   NAGB_GLAP5              Reviewed;         264 AA.
AC   B8F877;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=HAPS_2072;
OS   Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Glaesserella.
OX   NCBI_TaxID=557723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH0165;
RX   PubMed=19074396; DOI=10.1128/jb.01682-08;
RA   Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA   Jin M., Jin Q., Chen H.;
RT   "Complete genome sequence of Haemophilus parasuis SH0165.";
RL   J. Bacteriol. 191:1359-1360(2009).
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   -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine 6-
CC       phosphate (GlcNAc6P). {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   -!- SUBUNIT: Homohexamer. {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; CP001321; ACL33529.1; -; Genomic_DNA.
DR   RefSeq; WP_010787210.1; NC_011852.1.
DR   AlphaFoldDB; B8F877; -.
DR   SMR; B8F877; -.
DR   STRING; 557723.HAPS_2072; -.
DR   EnsemblBacteria; ACL33529; ACL33529; HAPS_2072.
DR   GeneID; 66619517; -.
DR   KEGG; hap:HAPS_2072; -.
DR   PATRIC; fig|557723.8.peg.2057; -.
DR   HOGENOM; CLU_049611_0_1_6; -.
DR   OMA; FNEPCSS; -.
DR   UniPathway; UPA00629; UER00684.
DR   Proteomes; UP000006743; 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   Allosteric enzyme; Carbohydrate metabolism; Hydrolase; Reference proteome.
FT   CHAIN           1..264
FT                   /note="Glucosamine-6-phosphate deaminase"
FT                   /id="PRO_1000165020"
FT   ACT_SITE        72
FT                   /note="Proton acceptor; for enolization step"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT   ACT_SITE        141
FT                   /note="For ring-opening step"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT   ACT_SITE        143
FT                   /note="Proton acceptor; for ring-opening step"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT   ACT_SITE        148
FT                   /note="For ring-opening step"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT   SITE            151
FT                   /note="Part of the allosteric site"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT   SITE            158
FT                   /note="Part of the allosteric site"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT   SITE            160
FT                   /note="Part of the allosteric site"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT   SITE            161
FT                   /note="Part of the allosteric site"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT   SITE            254
FT                   /note="Part of the allosteric site"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
SQ   SEQUENCE   264 AA;  29752 MW;  7FF32B0652AF01A9 CRC64;
     MRLVPLDCAE QVSRWAARYI VDKINAFQPT AEKPFVLGLP TGGTPLQTYK ELIKLYQAGE
     VSFKHVVTFN MDEYVGLPPE HKESYHYFMF HNFFNHIDIP VENVNILNGM AEDVDAECER
     YEAKIRSYGK IHLFMGGVGV DGHIAFNEPA SSLSSRTRIK TLTEDTLIAN SRFFDNDVNK
     VPKFALTVGV GTLMDAEEVL ILVTGYNKAL ALQACVEGAV NHLWTISALQ LHRRAVVVCD
     EPATQELKVK TVKYFKQLEQ NIAR