ID   NAGB_BORHD              Reviewed;         267 AA.
AC   B2RZL5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=BH0152;
OS   Borrelia hermsii (strain HS1 / DAH).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=314723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS1 / DAH;
RA   Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA   Schwan T.G.;
RT   "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT   comparative analysis of two agents of endemic N. America relapsing fever.";
RL   Submitted (DEC-2004) 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   -!- 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   -!- 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; CP000048; AAX16671.1; -; Genomic_DNA.
DR   RefSeq; WP_012421928.1; NC_010673.1.
DR   AlphaFoldDB; B2RZL5; -.
DR   SMR; B2RZL5; -.
DR   KEGG; bhr:BH0152; -.
DR   HOGENOM; CLU_049611_0_1_12; -.
DR   OMA; FNEPCSS; -.
DR   UniPathway; UPA00629; UER00684.
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.
FT   CHAIN           1..267
FT                   /note="Glucosamine-6-phosphate deaminase"
FT                   /id="PRO_1000139761"
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   267 AA;  30207 MW;  D8AC0B34CA818B72 CRC64;
     MRLIIRTNYN DISKWAANHV AMRIKEFSPT KEKPFILGLP TGSSPIGMYK NLIEMNKIGK
     ISFENVVTFN MDEYVGLDKN HPESYNSFMW NNFFSHIDIK KENVHMLNGN AINLTNECTE
     YENKIKSYGG IMLFVGGIGP DGHIAFNEPG SSLKSRTRLK TLTQDTIIAN SRFFENDINK
     VPKSALTVGV GTIMDSKEVM IIVNGHNKAR ALRHAIEKGV NHMWTISTLQ LHKNAIIVSD
     EAATYELKVG TVKYFNDIEK DNFNNDI