NAGB_BORBU
ID NAGB_BORBU Reviewed; 268 AA.
AC O30564;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 126.
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=BB_0152;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sh-2-82;
RA Whitehouse C.A., Austin F.E.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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; AF011226; AAB65253.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66538.1; -; Genomic_DNA.
DR PIR; H70118; H70118.
DR RefSeq; NP_212286.1; NC_001318.1.
DR RefSeq; WP_002556751.1; NC_001318.1.
DR PDB; 3HN6; X-ray; 2.20 A; A/B/C/D/E/F=1-268.
DR PDBsum; 3HN6; -.
DR AlphaFoldDB; O30564; -.
DR SMR; O30564; -.
DR STRING; 224326.BB_0152; -.
DR PRIDE; O30564; -.
DR EnsemblBacteria; AAC66538; AAC66538; BB_0152.
DR GeneID; 56568068; -.
DR KEGG; bbu:BB_0152; -.
DR PATRIC; fig|224326.49.peg.549; -.
DR HOGENOM; CLU_049611_0_1_12; -.
DR OMA; FNEPCSS; -.
DR UniPathway; UPA00629; UER00684.
DR EvolutionaryTrace; O30564; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
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 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Carbohydrate metabolism; Hydrolase;
KW Reference proteome.
FT CHAIN 1..268
FT /note="Glucosamine-6-phosphate deaminase"
FT /id="PRO_0000160137"
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"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:3HN6"
FT HELIX 9..27
FT /evidence="ECO:0007829|PDB:3HN6"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3HN6"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:3HN6"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:3HN6"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:3HN6"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3HN6"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3HN6"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:3HN6"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:3HN6"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:3HN6"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:3HN6"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3HN6"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3HN6"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:3HN6"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:3HN6"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:3HN6"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:3HN6"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:3HN6"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:3HN6"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:3HN6"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:3HN6"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:3HN6"
FT HELIX 249..263
FT /evidence="ECO:0007829|PDB:3HN6"
SQ SEQUENCE 268 AA; 30358 MW; 9807089FCCC4BD75 CRC64;
MRLIIRPTYE DISKWAANHV AQKINEFSPT KENPFILGLP TGSSPIGMYK NLIELNKNKK
ISFQNVITFN MDEYIGIEEN HPESYHSFMW NNFFSHIDIK KENINILNGN ASNLKKECEE
YEKKIKSFGG IMLFVGGIGP DGHIAFNEPG SSLTSRTRIK TLTQDTIIAN SRFFEGDVNK
VPKNALTVGI GTIMDSQEVL IIVNGHNKAR ALKHAIEKGV NHMWTISALQ LHKNAIIVSD
KNATYELKVG TVEYFNDIER KNFNNDLK
