(data stored in SCRATCH zone)

SWISSPROT: D6XVV3_BACIE

ID   D6XVV3_BACIE            Unreviewed;       246 AA.
AC   D6XVV3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=Glucosamine-6-phosphate deaminase {ECO:0000256|HAMAP-Rule:MF_01241};
DE            EC=3.5.99.6 {ECO:0000256|HAMAP-Rule:MF_01241};
DE   AltName: Full=GlcN6P deaminase {ECO:0000256|HAMAP-Rule:MF_01241};
DE            Short=GNPDA {ECO:0000256|HAMAP-Rule:MF_01241};
DE   AltName: Full=Glucosamine-6-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01241};
GN   Name=nagB {ECO:0000256|HAMAP-Rule:MF_01241};
GN   OrderedLocusNames=Bsel_0178 {ECO:0000313|EMBL:ADH97726.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97726.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97726.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible isomerization-deamination of
CC       glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate
CC       (Fru6P) and ammonium ion. {ECO:0000256|HAMAP-Rule:MF_01241}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose
CC         6-phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989;
CC         EC=3.5.99.6; Evidence={ECO:0000256|HAMAP-Rule:MF_01241,
CC         ECO:0000256|SAAS:SAAS01119605};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation;
CC       D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
CC       {ECO:0000256|HAMAP-Rule:MF_01241}.
CC   -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC       isomerase family. NagB subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01241}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01241}.
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DR   EMBL; CP001791; ADH97726.1; -; Genomic_DNA.
DR   RefSeq; WP_013171155.1; NC_014219.1.
DR   STRING; 439292.Bsel_0178; -.
DR   EnsemblBacteria; ADH97726; ADH97726; Bsel_0178.
DR   KEGG; bse:Bsel_0178; -.
DR   eggNOG; COG0363; LUCA.
DR   HOGENOM; HOG000064978; -.
DR   KO; K02564; -.
DR   OMA; PLHSMKE; -.
DR   OrthoDB; 1828393at2; -.
DR   BioCyc; BSEL439292:G1GLR-202-MONOMER; -.
DR   UniPathway; UPA00629; UER00684.
DR   Proteomes; UP000000271; Chromosome.
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;
DR   PRODOM; D6XVV3.
DR   SWISS-2DPAGE; D6XVV3.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01241,
KW   ECO:0000256|SAAS:SAAS01083540};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01241,
KW   ECO:0000256|SAAS:SAAS01083547};
KW   Isomerase {ECO:0000313|EMBL:ADH97726.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN       12    228       Glucosamine_iso. {ECO:0000259|Pfam:
FT                                PF01182}.
FT   ACT_SITE     69     69       Proton acceptor; for enolization step.
FT                                {ECO:0000256|HAMAP-Rule:MF_01241}.
FT   ACT_SITE    137    137       For ring-opening step.
FT                                {ECO:0000256|HAMAP-Rule:MF_01241}.
FT   ACT_SITE    139    139       Proton acceptor; for ring-opening step.
FT                                {ECO:0000256|HAMAP-Rule:MF_01241}.
FT   ACT_SITE    144    144       For ring-opening step.
FT                                {ECO:0000256|HAMAP-Rule:MF_01241}.
SQ   SEQUENCE   246 AA;  27191 MW;  F961229683D4E79E CRC64;
     MTITIQTVDD YHAMSEQAAE YFYDAIKENP DIHIGLATGG TPSGMYEALI QKIQDSALPL
     GAIQTFNLDE YIGLSQDDPN SYYTFMKDTL FAPLKLSRNQ TYVPDGNTSD HEMECRRYEA
     LIDEHGIDLQ LLGVGENGHI GFNEPGTPFD SVTHVIELND TTREANARYF NSPDEVPTHA
     ITMGIRSILK AKKIVLLASG TNKAEAISAL FRDTITEDWP ITALKEHPDV TVIVDKAAAG
     QIPDEK
//

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