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Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205) (Protein raspberry)

 IMDH_DROME              Reviewed;         537 AA.
Q07152; Q26455; Q8SXM5; Q9W2R8;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
18-JUL-2018, entry version 169.
RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03156};
Short=IMP dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03156};
Short=IMPD {ECO:0000255|HAMAP-Rule:MF_03156};
Short=IMPDH {ECO:0000255|HAMAP-Rule:MF_03156};
EC=1.1.1.205 {ECO:0000255|HAMAP-Rule:MF_03156};
AltName: Full=Protein raspberry;
Name=ras; ORFNames=CG1799;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE.
STRAIN=Oregon-R; TISSUE=Embryo;
Nash D., Hu S.;
"Drosophila inosine monophosphate dehydrogenase is encoded at the
raspberry locus.";
(In) Proceedings of the 35th meeting of the Canadian Federation of
Biological Societies, pp.72-72, Victoria (1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=Oregon-R; TISSUE=Embryo;
PubMed=7911114;
Nash D., Hu S., Leonard N.J., Tiong S.Y., Fillips D.;
"The raspberry locus of Drosophila melanogaster includes an inosine
monophosphate dehydrogenase like coding sequence.";
Genome 37:333-344(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Canton-S;
PubMed=7904480;
Sifri C.D., Wilson K., Smolik S., Forte M.A., Ullman B.;
"Cloning and sequence analysis of a Drosophila melanogaster cDNA
encoding IMP dehydrogenase.";
Biochim. Biophys. Acta 1217:103-106(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=7476879; DOI=10.1007/BF02191716;
Slee R., Bownes M.;
"The raspberry locus encodes Drosophila inosine monophosphate
dehydrogenase.";
Mol. Gen. Genet. 248:755-766(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[6]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP)
to xanthosine 5'-phosphate (XMP), the first committed and rate-
limiting step in the de novo synthesis of guanine nucleotides, and
therefore plays an important role in the regulation of cell
growth. {ECO:0000255|HAMAP-Rule:MF_03156,
ECO:0000269|PubMed:7476879, ECO:0000269|PubMed:7911114}.
-!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O =
xanthosine 5'-phosphate + NADH. {ECO:0000255|HAMAP-Rule:MF_03156}.
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000255|HAMAP-Rule:MF_03156};
-!- ENZYME REGULATION: Mycophenolic acid (MPA) is a non-competitive
inhibitor that prevents formation of the closed enzyme
conformation by binding to the same site as the amobile flap. In
contrast, mizoribine monophosphate (MZP) is a competitive
inhibitor that induces the closed conformation. MPA is a potent
inhibitor of mammalian IMPDHs but a poor inhibitor of the
bacterial enzymes. MZP is a more potent inhibitor of bacterial
IMPDH. {ECO:0000255|HAMAP-Rule:MF_03156}.
-!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway;
XMP from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_03156}.
-!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03156}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156}.
-!- TISSUE SPECIFICITY: Enriched in adult ovary and testis.
{ECO:0000269|PubMed:7476879}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
{ECO:0000269|PubMed:7476879}.
-!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP-
Rule:MF_03156}.
-!- SEQUENCE CAUTION:
Sequence=AAL90291.1; Type=Frameshift; Positions=49, 56; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; L14847; AAA21831.1; -; Genomic_DNA.
EMBL; L22608; AAA16839.1; -; mRNA.
EMBL; S80430; AAB35628.1; -; mRNA.
EMBL; AE014298; AAF46621.3; -; Genomic_DNA.
EMBL; AE014298; AAF46622.1; -; Genomic_DNA.
EMBL; AY089553; AAL90291.1; ALT_FRAME; mRNA.
PIR; S41064; S41064.
PIR; S59508; S59508.
RefSeq; NP_001259427.1; NM_001272498.2.
RefSeq; NP_524646.5; NM_079907.7.
RefSeq; NP_727441.1; NM_167240.3.
RefSeq; NP_727442.1; NM_167241.3.
UniGene; Dm.6459; -.
ProteinModelPortal; Q07152; -.
SMR; Q07152; -.
BioGrid; 68684; 11.
DIP; DIP-21552N; -.
IntAct; Q07152; 5.
STRING; 7227.FBpp0304573; -.
iPTMnet; Q07152; -.
PaxDb; Q07152; -.
PRIDE; Q07152; -.
EnsemblMetazoa; FBtr0071494; FBpp0071423; FBgn0003204.
EnsemblMetazoa; FBtr0071495; FBpp0071424; FBgn0003204.
EnsemblMetazoa; FBtr0332294; FBpp0304573; FBgn0003204.
EnsemblMetazoa; FBtr0343043; FBpp0309791; FBgn0003204.
GeneID; 43873; -.
KEGG; dme:Dmel_CG1799; -.
CTD; 19412; -.
FlyBase; FBgn0003204; ras.
eggNOG; KOG2550; Eukaryota.
eggNOG; COG0516; LUCA.
eggNOG; COG0517; LUCA.
GeneTree; ENSGT00530000062923; -.
InParanoid; Q07152; -.
KO; K00088; -.
OMA; GIGIVHK; -.
OrthoDB; EOG091G0EAV; -.
PhylomeDB; Q07152; -.
Reactome; R-DME-6798695; Neutrophil degranulation.
Reactome; R-DME-73817; Purine ribonucleoside monophosphate biosynthesis.
UniPathway; UPA00601; UER00295.
ChiTaRS; ras; fly.
GenomeRNAi; 43873; -.
PRO; PR:Q07152; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0003204; -.
ExpressionAtlas; Q07152; baseline and differential.
Genevisible; Q07152; DM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0003938; F:IMP dehydrogenase activity; ISS:FlyBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006183; P:GTP biosynthetic process; IBA:GO_Central.
GO; GO:0006164; P:purine nucleotide biosynthetic process; ISS:FlyBase.
CDD; cd00381; IMPDH; 1.
HAMAP; MF_01964; IMPDH; 1.
InterPro; IPR000644; CBS_dom.
InterPro; IPR005990; IMP_DH.
InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
InterPro; IPR001093; IMP_DH_GMPRt.
Pfam; PF00571; CBS; 2.
Pfam; PF00478; IMPDH; 1.
PIRSF; PIRSF000130; IMPDH; 1.
SMART; SM00116; CBS; 2.
TIGRFAMs; TIGR01302; IMP_dehydrog; 1.
PROSITE; PS51371; CBS; 2.
PROSITE; PS00487; IMP_DH_GMP_RED; 1.
1: Evidence at protein level;
CBS domain; Complete proteome; Cytoplasm; GMP biosynthesis;
Metal-binding; NAD; Oxidoreductase; Phosphoprotein; Potassium;
Purine biosynthesis; Reference proteome; Repeat.
CHAIN 1 537 Inosine-5'-monophosphate dehydrogenase.
/FTId=PRO_0000093678.
DOMAIN 136 195 CBS 1. {ECO:0000255|HAMAP-Rule:MF_03156}.
DOMAIN 200 256 CBS 2. {ECO:0000255|HAMAP-Rule:MF_03156}.
NP_BIND 293 295 NAD. {ECO:0000255|HAMAP-Rule:MF_03156}.
NP_BIND 343 345 NAD. {ECO:0000255|HAMAP-Rule:MF_03156}.
REGION 383 385 IMP binding. {ECO:0000255|HAMAP-
Rule:MF_03156}.
REGION 406 407 IMP binding. {ECO:0000255|HAMAP-
Rule:MF_03156}.
REGION 430 434 IMP binding. {ECO:0000255|HAMAP-
Rule:MF_03156}.
ACT_SITE 350 350 Thioimidate intermediate.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 345 345 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 347 347 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 350 350 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 523 523 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 524 524 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_03156}.
BINDING 348 348 IMP. {ECO:0000255|HAMAP-Rule:MF_03156}.
BINDING 464 464 IMP. {ECO:0000255|HAMAP-Rule:MF_03156}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CONFLICT 38 38 D -> V (in Ref. 4; AAB35628).
{ECO:0000305}.
CONFLICT 53 53 T -> P (in Ref. 4; AAB35628).
{ECO:0000305}.
CONFLICT 99 102 EMAI -> RCH (in Ref. 4; AAB35628).
{ECO:0000305}.
CONFLICT 184 184 D -> A (in Ref. 4; AAB35628).
{ECO:0000305}.
CONFLICT 194 194 V -> S (in Ref. 4; AAB35628).
{ECO:0000305}.
CONFLICT 216 217 AN -> EH (in Ref. 4; AAB35628).
{ECO:0000305}.
CONFLICT 226 229 GKLP -> ATA (in Ref. 4; AAB35628).
{ECO:0000305}.
CONFLICT 244 244 T -> A (in Ref. 4; AAB35628).
{ECO:0000305}.
CONFLICT 261 262 KQ -> TR (in Ref. 4; AAB35628).
{ECO:0000305}.
CONFLICT 265 266 VG -> CP (in Ref. 4; AAB35628).
{ECO:0000305}.
CONFLICT 277 278 AR -> GCRA (in Ref. 4; AAB35628).
{ECO:0000305}.
CONFLICT 284 284 A -> R (in Ref. 4; AAB35628).
{ECO:0000305}.
CONFLICT 301 301 Y -> I (in Ref. 4; AAB35628).
{ECO:0000305}.
CONFLICT 387 388 QS -> HA (in Ref. 4; AAB35628).
{ECO:0000305}.
SEQUENCE 537 AA; 57829 MW; A5EAB41AEAA64EBD CRC64;
MESTTKVKVN GFVESTSSSA APAIQTKSTT GFDAELQDGL SCKELFQNGE GLTYNDFLIL
PGYIDFTAEE VDLSSPLTKS LTLRAPLVSS PMDTVTESEM AIAMALCGGI GIIHHNCTPE
YQALEVHKVK KYKHGFMRDP SVMSPTNTVG DVLEARRKNG FTGYPVTENG KLGGKLLGMV
TSRDIDFREN QPEVLLADIM TTELVTAPNG INLPTANAIL EKSKKGKLPI VNQAGELVAM
IARTDLKKAR SYPNASKDSN KQLLVGAAIG TRSEDKARLA LLVANGVDVI ILDSSQGNSV
YQVEMIKYIK ETYPELQVIG GNVVTRAQAK NLIDAGVDGL RVGMGSGSIC ITQEVMACGC
PQATAVYQVS TYARQFGVPV IADGGIQSIG HIVKAIALGA SAVMMGSLLA GTSEAPGEYF
FSDGVRLKKY RGMGSLEAME RGDAKGAAMS RYYHNEMDKM KVAQGVSGSI VDKGSVLRYL
PYLECGLQHS CQDIGANSIN KLRDMIYNGQ LRFMKRTHSA QLEGNVHGLF SYEKRLF


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