NAGB_STRMU
ID NAGB_STRMU Reviewed; 233 AA.
AC Q8DV70;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=SMU_636;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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: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 -!- 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; AE014133; AAN58370.1; -; Genomic_DNA.
DR RefSeq; NP_721064.1; NC_004350.2.
DR RefSeq; WP_002261905.1; NC_004350.2.
DR PDB; 2RI0; X-ray; 1.60 A; A/B=1-233.
DR PDB; 2RI1; X-ray; 2.03 A; A/B=1-233.
DR PDBsum; 2RI0; -.
DR PDBsum; 2RI1; -.
DR AlphaFoldDB; Q8DV70; -.
DR SMR; Q8DV70; -.
DR STRING; 210007.SMU_636; -.
DR PRIDE; Q8DV70; -.
DR EnsemblBacteria; AAN58370; AAN58370; SMU_636.
DR KEGG; smu:SMU_636; -.
DR PATRIC; fig|210007.7.peg.562; -.
DR eggNOG; COG0363; Bacteria.
DR HOGENOM; CLU_049611_1_0_9; -.
DR OMA; FNEPCSS; -.
DR PhylomeDB; Q8DV70; -.
DR UniPathway; UPA00629; UER00684.
DR EvolutionaryTrace; Q8DV70; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006040; P:amino sugar metabolic process; IDA:CACAO.
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; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR11280; PTHR11280; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Hydrolase; Reference proteome.
FT CHAIN 1..233
FT /note="Glucosamine-6-phosphate deaminase"
FT /id="PRO_0000160176"
FT ACT_SITE 62
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 128
FT /note="For ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 130
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 135
FT /note="For ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT STRAND 1..8
FT /evidence="ECO:0007829|PDB:2RI0"
FT HELIX 9..25
FT /evidence="ECO:0007829|PDB:2RI0"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:2RI0"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:2RI0"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:2RI0"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:2RI0"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:2RI0"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:2RI0"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:2RI0"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:2RI0"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:2RI0"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:2RI0"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2RI0"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:2RI0"
FT HELIX 176..180
FT /evidence="ECO:0007829|PDB:2RI0"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:2RI0"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:2RI0"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:2RI0"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:2RI0"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:2RI0"
FT TURN 227..232
FT /evidence="ECO:0007829|PDB:2RI0"
SQ SEQUENCE 233 AA; 25473 MW; B6546EE48C922900 CRC64;
MKTIKVKNKT EGSKVAFRML EEEITFGAKT LGLATGSTPL ELYKEIRESH LDFSDMVSIN
LDEYVGLSAD DKQSYAYFMK QNLFAAKPFK KSYLPNGLAA DLAKETEYYD QILAQYPIDL
QILGIGRNAH IGFNEPGTAF SSQTHLVDLT PSTIAANSRF FEKAEDVPKQ AISMGLASIM
SAKMILLMAF GEEKAEAVAA MVKGPVTEEI PASILQTHPK VILIVDEKAG AGI
