NAGB_ECOLI
ID NAGB_ECOLI Reviewed; 266 AA.
AC P0A759; O68603; P09375;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glucosamine-6-phosphate deaminase;
DE EC=3.5.99.6 {ECO:0000269|PubMed:1734962};
DE AltName: Full=GlcN6P deaminase;
DE Short=GNPDA;
DE AltName: Full=Glucosamine-6-phosphate isomerase;
GN Name=nagB; Synonyms=glmD; OrderedLocusNames=b0678, JW0664;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3284790; DOI=10.1016/0378-1119(88)90558-6;
RA Rogers M.J., Ohgi T., Plumbridge J., Soell D.;
RT "Nucleotide sequences of the Escherichia coli nagE and nagB genes: the
RT structural genes for the N-acetylglucosamine transport protein of the
RT bacterial phosphoenolpyruvate: sugar phosphotransferase system and for
RT glucosamine-6-phosphate deaminase.";
RL Gene 62:197-207(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2190615; DOI=10.1139/o90-017;
RA Peri K.G., Goldie H., Waygood E.B.;
RT "Cloning and characterization of the N-acetylglucosamine operon of
RT Escherichia coli.";
RL Biochem. Cell Biol. 68:123-137(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=2821923; DOI=10.1016/0003-9861(87)90326-2;
RA Altamirano M.M., Mulliert G., Calcagno M.;
RT "Sulfhydryl groups of glucosamine-6-phosphate isomerase deaminase from
RT Escherichia coli.";
RL Arch. Biochem. Biophys. 258:95-100(1987).
RN [7]
RP MUTAGENESIS OF CYS-118 AND CYS-239, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=1734962; DOI=10.1021/bi00119a026;
RA Altamirano M.M., Plumbridge J.A., Calcagno M.L.;
RT "Identification of two cysteine residues forming a pair of vicinal thiols
RT in glucosamine-6-phosphate deaminase from Escherichia coli and a study of
RT their functional role by site-directed mutagenesis.";
RL Biochemistry 31:1153-1158(1992).
RN [8]
RP DISULFIDE BONDS.
RX PubMed=8240271; DOI=10.1042/bj2950645;
RA Altamirano M.M., Plumbridge J.A., Barba H.A., Calcagno M.L.;
RT "Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of
RT dimers structure with three intersubunit disulphides.";
RL Biochem. J. 295:645-648(1993).
RN [9]
RP ACTIVE SITES, AND MUTAGENESIS OF ASP-141; HIS-143 AND GLU-148.
RX PubMed=11513596; DOI=10.1021/bi0105835;
RA Montero-Moran G.M., Lara-Gonzalez S., Alvarez-Anorve L.I., Plumbridge J.A.,
RA Calcagno M.L.;
RT "On the multiple functional roles of the active site histidine in catalysis
RT and allosteric regulation of Escherichia coli glucosamine 6-phosphate
RT deaminase.";
RL Biochemistry 40:10187-10196(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH
RP THE INHIBITOR 2-AMINO-2-DEOXY-D-GLUCITOL-6-PHOSPHATE.
RX PubMed=8747459; DOI=10.1016/s0969-2126(01)00270-2;
RA Oliva G., Fontes M.R.M., Garratt R.C., Altamirano M.M., Calcagno M.L.,
RA Horjales E.;
RT "Structure and catalytic mechanism of glucosamine 6-phosphate deaminase
RT from Escherichia coli at 2.1-A resolution.";
RL Structure 3:1323-1332(1995).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=10378272; DOI=10.1016/s0969-2126(99)80069-0;
RA Horjales E., Altamirano M.M., Calcagno M.L., Garratt R.C., Oliva G.;
RT "The allosteric transition of glucosamine-6-phosphate deaminase: the
RT structure of the T state at 2.3-A resolution.";
RL Structure 7:527-537(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH
RP FRUCTOSE-6-PHOSPHATE AND N-ACETYLGLUCOSAMINE-6-PHOSPHATE.
RX PubMed=11752775; DOI=10.1107/s0907444901016699;
RA Rudino-Pinera E., Morales-Arrieta S., Rojas-Trejo S.P., Horjales E.;
RT "Structural flexibility, an essential component of the allosteric
RT activation in Escherichia coli glucosamine-6-phosphate deaminase.";
RL Acta Crystallogr. D 58:10-20(2002).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF MUTANT ALA-174.
RX PubMed=12051945; DOI=10.1016/s0022-2836(02)00096-7;
RA Bustos-Jaimes I., Sosa-Peinado A., Rudino-Pinera E., Horjales E.,
RA Calcagno M.L.;
RT "On the role of the conformational flexibility of the active-site lid on
RT the allosteric kinetics of glucosamine-6-phosphate deaminase.";
RL J. Mol. Biol. 319:183-189(2002).
CC -!- FUNCTION: Catalyzes the reversible isomerization-deamination of
CC glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P)
CC and ammonium ion. {ECO:0000269|PubMed:1734962,
CC ECO:0000269|PubMed:2821923}.
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:0000269|PubMed:1734962, ECO:0000269|PubMed:2821923};
CC -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine 6-
CC phosphate (GlcNAc6P). Competitively inhibited by 2-amino-2-deoxy-D-
CC glucitol-6-phosphate (GlcN-ol-6P).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for GlcN6P {ECO:0000269|PubMed:2821923};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 5/5.
CC -!- SUBUNIT: Homohexamer; trimer of disulfide-linked dimers.
CC {ECO:0000269|PubMed:8240271}.
CC -!- MISCELLANEOUS: Disulfide bonds seem not to be essential for the
CC stability of the oligomer under physiological conditions.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. NagB subfamily. {ECO:0000305}.
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DR EMBL; M19284; AAA24191.1; -; Genomic_DNA.
DR EMBL; AF052007; AAC09324.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73772.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35321.1; -; Genomic_DNA.
DR PIR; A29895; MUECNG.
DR RefSeq; NP_415204.1; NC_000913.3.
DR RefSeq; WP_001237072.1; NZ_STEB01000044.1.
DR PDB; 1CD5; X-ray; 2.30 A; A=1-266.
DR PDB; 1DEA; X-ray; 2.10 A; A/B=1-266.
DR PDB; 1FQO; X-ray; 2.20 A; A/B=1-266.
DR PDB; 1FRZ; X-ray; 2.20 A; A/B=1-266.
DR PDB; 1FS5; X-ray; 1.73 A; A/B=1-266.
DR PDB; 1FS6; X-ray; 2.20 A; A=1-266.
DR PDB; 1FSF; X-ray; 1.90 A; A=1-266.
DR PDB; 1HOR; X-ray; 2.40 A; A/B=1-266.
DR PDB; 1HOT; X-ray; 2.40 A; A/B=1-266.
DR PDB; 1JT9; X-ray; 2.06 A; A=1-266.
DR PDB; 2WU1; X-ray; 2.20 A; A/B=1-266.
DR PDBsum; 1CD5; -.
DR PDBsum; 1DEA; -.
DR PDBsum; 1FQO; -.
DR PDBsum; 1FRZ; -.
DR PDBsum; 1FS5; -.
DR PDBsum; 1FS6; -.
DR PDBsum; 1FSF; -.
DR PDBsum; 1HOR; -.
DR PDBsum; 1HOT; -.
DR PDBsum; 1JT9; -.
DR PDBsum; 2WU1; -.
DR AlphaFoldDB; P0A759; -.
DR SMR; P0A759; -.
DR BioGRID; 4261792; 32.
DR DIP; DIP-35992N; -.
DR IntAct; P0A759; 11.
DR STRING; 511145.b0678; -.
DR DrugBank; DB02445; 2-Deoxy-2-Amino Glucitol-6-Phosphate.
DR DrugBank; DB03951; N-acetyl-D-glucosamine-6-phosphate.
DR jPOST; P0A759; -.
DR PaxDb; P0A759; -.
DR PRIDE; P0A759; -.
DR EnsemblBacteria; AAC73772; AAC73772; b0678.
DR EnsemblBacteria; BAA35321; BAA35321; BAA35321.
DR GeneID; 67416285; -.
DR GeneID; 945290; -.
DR KEGG; ecj:JW0664; -.
DR KEGG; eco:b0678; -.
DR PATRIC; fig|1411691.4.peg.1600; -.
DR EchoBASE; EB0627; -.
DR eggNOG; COG0363; Bacteria.
DR HOGENOM; CLU_049611_0_1_6; -.
DR InParanoid; P0A759; -.
DR OMA; FNEPCSS; -.
DR PhylomeDB; P0A759; -.
DR BioCyc; EcoCyc:GLUCOSAMINE-6-P-DEAMIN-MON; -.
DR BioCyc; MetaCyc:GLUCOSAMINE-6-P-DEAMIN-MON; -.
DR BRENDA; 3.5.99.6; 2026.
DR SABIO-RK; P0A759; -.
DR UniPathway; UPA00629; UER00684.
DR EvolutionaryTrace; P0A759; -.
DR PRO; PR:P0A759; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006043; P:glucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IMP:EcoCyc.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IMP:EcoCyc.
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; Disulfide bond;
KW Hydrolase; Reference proteome.
FT CHAIN 1..266
FT /note="Glucosamine-6-phosphate deaminase"
FT /id="PRO_0000160143"
FT ACT_SITE 72
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000269|PubMed:11513596"
FT ACT_SITE 141
FT /note="For ring-opening step"
FT /evidence="ECO:0000269|PubMed:11513596"
FT ACT_SITE 143
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000269|PubMed:11513596"
FT ACT_SITE 148
FT /note="For ring-opening step"
FT /evidence="ECO:0000269|PubMed:11513596"
FT SITE 151
FT /note="Part of the allosteric site"
FT SITE 158
FT /note="Part of the allosteric site"
FT SITE 160
FT /note="Part of the allosteric site"
FT SITE 161
FT /note="Part of the allosteric site"
FT SITE 254
FT /note="Part of the allosteric site"
FT DISULFID 219
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:8240271"
FT MUTAGEN 118
FT /note="C->S: 50% of wild-type activity, but 2-fold decrease
FT in substrate affinity."
FT /evidence="ECO:0000269|PubMed:1734962"
FT MUTAGEN 141
FT /note="D->N: Large decrease in activity."
FT /evidence="ECO:0000269|PubMed:11513596"
FT MUTAGEN 143
FT /note="H->Q: Loss of activity for the deamination reaction
FT but not for the reverse reaction; complete loss of the
FT homotropic cooperativity."
FT /evidence="ECO:0000269|PubMed:11513596"
FT MUTAGEN 148
FT /note="E->Q: Large decrease in activity."
FT /evidence="ECO:0000269|PubMed:11513596"
FT MUTAGEN 174
FT /note="F->A: Loss of activity in the absence of the
FT allosteric activator."
FT MUTAGEN 239
FT /note="C->S: 50% of wild-type activity, but 2-fold decrease
FT in substrate affinity; decrease in allosteric interaction
FT energy."
FT /evidence="ECO:0000269|PubMed:1734962"
FT CONFLICT 70
FT /note="N -> NM (in Ref. 2; AAC09324)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="Missing (in Ref. 2; AAC09324)"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 9..27
FT /evidence="ECO:0007829|PDB:1FS5"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1FS5"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:1FS5"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 114..128
FT /evidence="ECO:0007829|PDB:1FS5"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1FS5"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1FS5"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1FS5"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:1FS5"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:1FS5"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:1FS5"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1FS5"
FT HELIX 249..263
FT /evidence="ECO:0007829|PDB:1FS5"
SQ SEQUENCE 266 AA; 29774 MW; D1443A40E74AC08E CRC64;
MRLIPLTTAE QVGKWAARHI VNRINAFKPT ADRPFVLGLP TGGTPMTTYK ALVEMHKAGQ
VSFKHVVTFN MDEYVGLPKE HPESYYSFMH RNFFDHVDIP AENINLLNGN APDIDAECRQ
YEEKIRSYGK IHLFMGGVGN DGHIAFNEPA SSLASRTRIK TLTHDTRVAN SRFFDNDVNQ
VPKYALTVGV GTLLDAEEVM ILVLGSQKAL ALQAAVEGCV NHMWTISCLQ LHPKAIMVCD
EPSTMELKVK TLRYFNELEA ENIKGL
