NAGB_PASMU
ID NAGB_PASMU Reviewed; 267 AA.
AC Q9CMF4;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=PM0875;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02959.1; -; Genomic_DNA.
DR RefSeq; WP_005716895.1; NC_002663.1.
DR PDB; 7LQM; X-ray; 2.30 A; A/B/C/D=1-267.
DR PDBsum; 7LQM; -.
DR AlphaFoldDB; Q9CMF4; -.
DR SMR; Q9CMF4; -.
DR STRING; 747.DR93_1716; -.
DR EnsemblBacteria; AAK02959; AAK02959; PM0875.
DR KEGG; pmu:PM0875; -.
DR HOGENOM; CLU_049611_0_1_6; -.
DR OMA; FNEPCSS; -.
DR UniPathway; UPA00629; UER00684.
DR Proteomes; UP000000809; 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 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Carbohydrate metabolism; Hydrolase;
KW Reference proteome.
FT CHAIN 1..267
FT /note="Glucosamine-6-phosphate deaminase"
FT /id="PRO_0000160158"
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"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 9..27
FT /evidence="ECO:0007829|PDB:7LQM"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:7LQM"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:7LQM"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:7LQM"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:7LQM"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:7LQM"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:7LQM"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:7LQM"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:7LQM"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:7LQM"
SQ SEQUENCE 267 AA; 30207 MW; 1C789922965AF49C CRC64;
MRLIPLHNVD QVAKWSARYI VDRINQFQPT EARPFVLGLP TGGTPLKTYE ALIELYKAGE
VSFKHVVTFN MDEYVGLPKE HPESYHSFMY KNFFDHVDIQ EKNINILNGN TEDHDAECQR
YEEKIKSYGK IHLFMGGVGV DGHIAFNEPA SSLSSRTRIK TLTEDTLIAN SRFFDNDVNK
VPKYALTIGV GTLLDAEEVM ILVTGYNKAQ ALQAAVEGSI NHLWTVTALQ MHRRAIIVCD
EPATQELKVK TVKYFTELEA SAIRSVK
