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GNPI_DROPS
ID   GNPI_DROPS              Reviewed;         274 AA.
AC   Q29NT9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Glucosamine-6-phosphate isomerase;
DE            EC=3.5.99.6;
DE   AltName: Full=Glucosamine-6-phosphate deaminase;
DE            Short=GNPDA;
DE            Short=GlcN6P deaminase;
GN   Name=Gnpda1; ORFNames=GA19983;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
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   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC       isomerase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL34555.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH379058; EAL34555.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001357485.1; XM_001357449.3.
DR   AlphaFoldDB; Q29NT9; -.
DR   SMR; Q29NT9; -.
DR   STRING; 7237.FBpp0279490; -.
DR   EnsemblMetazoa; FBtr0281052; FBpp0279490; FBgn0079979.
DR   GeneID; 4817879; -.
DR   KEGG; dpo:Dpse_GA19983; -.
DR   eggNOG; KOG3148; Eukaryota.
DR   HOGENOM; CLU_049611_0_1_1; -.
DR   InParanoid; Q29NT9; -.
DR   OMA; FNEPCSS; -.
DR   PhylomeDB; Q29NT9; -.
DR   Proteomes; UP000001819; Chromosome 4.
DR   Bgee; FBgn0079979; Expressed in male reproductive system and 2 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB.
DR   GO; GO:0006043; P:glucosamine catabolic process; ISS:UniProtKB.
DR   GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:InterPro.
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;
KW   Carbohydrate metabolism; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..274
FT                   /note="Glucosamine-6-phosphate isomerase"
FT                   /id="PRO_0000328092"
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"
SQ   SEQUENCE   274 AA;  30927 MW;  BD14E1CF079F6E67 CRC64;
     MRLVILETSQ SVGKWAAKYV MKRINDFQPG PNRYFVLGLP TGSTPLGMYK ELIEFHKQGK
     VSFQYVKTFN MDEYVGLPRD HQESYHFFMW HNFFKHIDIE PQNVHILNGN APDLVAECNK
     FEEQIKEAGG VELFIGGIGP DGHIAFNEPG SSLVSRTRVK TLAQDTLEAN ARFFDNDMSK
     VPKQALTVGV GTVMDSKEVM ILITGAHKAF ALYKAIEEGV NHMWTVSAFQ QHANTLMICD
     EDATLELRVK TVKYFKGILR DIDEGAATQD GYKN
 
 
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