GenomeNet

Database: UniProt/SWISS-PROT
Entry: SEPIA_DROME
LinkDB: SEPIA_DROME
Original site: SEPIA_DROME 
ID   SEPIA_DROME             Reviewed;         243 AA.
AC   Q9VSL3; D1KS67; D1KS72;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JAN-2019, entry version 166.
DE   RecName: Full=Pyrimidodiazepine synthase {ECO:0000305};
DE            EC=1.5.4.1 {ECO:0000269|PubMed:16712527};
DE   AltName: Full=Protein sepia {ECO:0000303|PubMed:16712527};
GN   Name=se {ECO:0000312|FlyBase:FBgn0086348};
GN   ORFNames=CG6781 {ECO:0000312|FlyBase:FBgn0086348};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000312, ECO:0000312|EMBL:AAF50405.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-200.
RX   PubMed=19608790; DOI=10.1093/jhered/esp043;
RA   Walters K.B., Grant P., Johnson D.L.;
RT   "Evolution of the GST omega gene family in 12 Drosophila species.";
RL   J. Hered. 100:742-753(2009).
RN   [5]
RP   FUNCTION.
RX   PubMed=6438092;
RA   Wiederrecht G.J., Brown G.M.;
RT   "Purification and properties of the enzymes from Drosophila
RT   melanogaster that catalyze the conversion of dihydroneopterin
RT   triphosphate to the pyrimidodiazepine precursor of the drosopterins.";
RL   J. Biol. Chem. 259:14121-14127(1984).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBUNIT, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16712527; DOI=10.1042/BJ20060424;
RA   Kim J., Suh H., Kim S., Kim K., Ahn C., Yim J.;
RT   "Identification and characteristics of the structural gene for the
RT   Drosophila eye color mutant sepia, encoding PDA synthase, a member of
RT   the omega class glutathione S-transferases.";
RL   Biochem. J. 398:451-460(2006).
CC   -!- FUNCTION: Mediates the conversion of 2-amino-4-oxo-6-pyruvoyl-
CC       5,6,7,8-tetrahydropteridine (6-PTP; also named 6-
CC       pyruvoyltetrahydropterin) to 2-amino-6-acetyl-3,7,8,9-tetrahydro-
CC       3H-pyrimido(4,5-b)[1,4]diazepin-4-one (pyrimidodiazepine or PDA),
CC       a key intermediate in red eye pigment drosopterin biosynthesis.
CC       {ECO:0000269|PubMed:16712527, ECO:0000269|PubMed:6438092}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-amino-6-acetyl-3,7,8,9-tetrahydro-3H-pyrimido[4,5-
CC         b][1,4]diazepin-4-one + glutathione disulfide + H2O = 6-
CC         pyruvoyl-5,6,7,8-tetrahydropterin + 2 glutathione;
CC         Xref=Rhea:RHEA:10720, ChEBI:CHEBI:15377, ChEBI:CHEBI:27714,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:136564;
CC         EC=1.5.4.1; Evidence={ECO:0000269|PubMed:16712527};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16712527}.
CC   -!- DEVELOPMENTAL STAGE: Appears only at the late pupal stage;
CC       expressed at high level. Also expressed in the early adult (0-2
CC       days old) at lower level. Expressed exclusively in the adult head.
CC       {ECO:0000269|PubMed:16712527}.
CC   -!- DISRUPTION PHENOTYPE: Sepia eye color, due to defects in 2-amino-
CC       6-acetyl-3,7,8,9-tetrahydro-3H-pyrimido(4,5-b)[1,4]diazepin-4-one
CC       (pyrimidodiazepine or PDA) synthesis, a key intermediate in red
CC       eye pigment drosopterin biosynthesis.
CC       {ECO:0000269|PubMed:16712527}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACZ02425.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=ACZ02430.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AE014296; AAF50405.1; -; Genomic_DNA.
DR   EMBL; AY070667; AAL48138.1; -; mRNA.
DR   EMBL; GQ351317; ACZ02425.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; GQ351318; ACZ02430.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_648235.1; NM_139978.4.
DR   UniGene; Dm.6327; -.
DR   ProteinModelPortal; Q9VSL3; -.
DR   SMR; Q9VSL3; -.
DR   BioGrid; 64383; 1.
DR   IntAct; Q9VSL3; 1.
DR   STRING; 7227.FBpp0076349; -.
DR   PaxDb; Q9VSL3; -.
DR   PRIDE; Q9VSL3; -.
DR   EnsemblMetazoa; FBtr0076623; FBpp0076349; FBgn0086348.
DR   GeneID; 38973; -.
DR   KEGG; dme:Dmel_CG6781; -.
DR   UCSC; CG6781-RA; d. melanogaster.
DR   CTD; 38973; -.
DR   FlyBase; FBgn0086348; se.
DR   eggNOG; KOG0406; Eukaryota.
DR   eggNOG; ENOG410XSIX; LUCA.
DR   GeneTree; ENSGT00940000163896; -.
DR   InParanoid; Q9VSL3; -.
DR   KO; K00310; -.
DR   OMA; EHPLKLY; -.
DR   OrthoDB; 1225872at2759; -.
DR   PhylomeDB; Q9VSL3; -.
DR   BioCyc; MetaCyc:MONOMER-18458; -.
DR   Reactome; R-DME-156581; Methylation.
DR   Reactome; R-DME-156590; Glutathione conjugation.
DR   Reactome; R-DME-196836; Vitamin C (ascorbate) metabolism.
DR   GenomeRNAi; 38973; -.
DR   PRO; PR:Q9VSL3; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0086348; Expressed in 4 organ(s), highest expression level in head.
DR   Genevisible; Q9VSL3; DM.
DR   GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR   GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IDA:FlyBase.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:FlyBase.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
DR   GO; GO:0004734; F:pyrimidodiazepine synthase activity; IDA:FlyBase.
DR   GO; GO:0016782; F:transferase activity, transferring sulfur-containing groups; IDA:FlyBase.
DR   GO; GO:0006726; P:eye pigment biosynthetic process; IGI:FlyBase.
DR   GO; GO:0006749; P:glutathione metabolic process; IDA:FlyBase.
DR   GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central.
DR   GO; GO:0006728; P:pteridine biosynthetic process; IDA:FlyBase.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR005442; GST_omega.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF13417; GST_N_3; 1.
DR   PRINTS; PR01625; GSTRNSFRASEO.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Oxidoreductase; Reference proteome.
FT   CHAIN         1    243       Pyrimidodiazepine synthase.
FT                                /FTId=PRO_0000430582.
FT   DOMAIN       20    102       GST N-terminal. {ECO:0000255}.
FT   DOMAIN      107    230       GST C-terminal. {ECO:0000255}.
FT   REGION       86     87       Glutathione binding.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   ACT_SITE     30     30       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   BINDING      57     57       Glutathione.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   BINDING      70     70       Glutathione; via amide nitrogen and
FT                                carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P78417}.
SQ   SEQUENCE   243 AA;  28413 MW;  A6B651F36487A5AE CRC64;
     MSNGRHLAKG SPMPDVPEDG ILRLYSMRFC PFAQRVHLVL DAKQIPYHSI YINLTDKPEW
     LLEKNPQGKV PALEIVREPG PPVLTESLLI CEYLDEQYPL RPLYPRDPLK KVQDKLLIER
     FRAVLGAFFK ASDGGDLEPF WSGLDIYERE LARRGTEFFG GEQTGILDYM IWPWCERLEL
     LKLQRGEDYN YDQSRFPQLT LWLERMKRDP AVMAFYMEAE VQAEFLRTRS LGRPNYNLLV
     KDA
//
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