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

 G1LDZ9_AILME            Unreviewed;       533 AA.
G1LDZ9;
19-OCT-2011, integrated into UniProtKB/TrEMBL.
19-OCT-2011, sequence version 1.
12-SEP-2018, entry version 39.
RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928};
Short=IMP dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03156};
Short=IMPD {ECO:0000256|HAMAP-Rule:MF_03156};
Short=IMPDH {ECO:0000256|HAMAP-Rule:MF_03156};
EC=1.1.1.205 {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928};
Name=IMPDH1 {ECO:0000313|Ensembl:ENSAMEP00000005133};
Synonyms=IMPDH {ECO:0000256|HAMAP-Rule:MF_03156};
Ailuropoda melanoleuca (Giant panda).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae;
Ailuropoda.
NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000005133, ECO:0000313|Proteomes:UP000008912};
[1] {ECO:0000313|Ensembl:ENSAMEP00000005133}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=20010809; DOI=10.1038/nature08696;
Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q.,
Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H.,
Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z.,
Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X.,
Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W.,
Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q.,
Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H.,
Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z.,
Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G.,
Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W.,
Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N.,
Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N.,
Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y.,
Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X.,
Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H.,
Wang J., Wang J.;
"The sequence and de novo assembly of the giant panda genome.";
Nature 463:311-317(2010).
[2] {ECO:0000313|Ensembl:ENSAMEP00000005133}
IDENTIFICATION.
Ensembl;
Submitted (SEP-2011) to UniProtKB.
-!- 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. Could also have a single-stranded nucleic acid-binding
activity and could play a role in RNA and/or DNA metabolism. It
may also have a role in the development of malignancy and the
growth progression of some tumors. {ECO:0000256|HAMAP-
Rule:MF_03156}.
-!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O =
xanthosine 5'-phosphate + NADH. {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|RuleBase:RU003928}.
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000256|HAMAP-Rule:MF_03156};
-!- ACTIVITY 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:0000256|HAMAP-Rule:MF_03156}.
-!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway;
XMP from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|RuleBase:RU003928}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03156}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156}.
Nucleus {ECO:0000256|HAMAP-Rule:MF_03156}.
-!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000256|HAMAP-
Rule:MF_03156, ECO:0000256|RuleBase:RU003927}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03156}.
-----------------------------------------------------------------------
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EMBL; ACTA01001075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; ACTA01009075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; ACTA01185064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; ACTA01193062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
STRING; 9646.ENSAMEP00000005133; -.
Ensembl; ENSAMET00000005343; ENSAMEP00000005133; ENSAMEG00000004824.
eggNOG; ENOG410ISZP; Eukaryota.
eggNOG; COG0517; LUCA.
GeneTree; ENSGT00530000062923; -.
InParanoid; G1LDZ9; -.
OrthoDB; EOG091G0EAV; -.
TreeFam; TF300378; -.
UniPathway; UPA00601; UER00295.
Proteomes; UP000008912; Unassembled WGS sequence.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:Ensembl.
GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0046651; P:lymphocyte proliferation; IEA:Ensembl.
CDD; cd00381; IMPDH; 1.
Gene3D; 3.20.20.70; -; 2.
HAMAP; MF_01964; IMPDH; 1.
InterPro; IPR013785; Aldolase_TIM.
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.
3: Inferred from homology;
CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
Complete proteome {ECO:0000313|Proteomes:UP000008912};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156};
GMP biosynthesis {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|RuleBase:RU003928};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|RuleBase:RU003928};
NAD {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|PIRSR:PIRSR000130-3,
ECO:0000256|RuleBase:RU003928};
Nucleus {ECO:0000256|HAMAP-Rule:MF_03156};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|RuleBase:RU003927};
Potassium {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|PIRSR:PIRSR000130-4, ECO:0000256|RuleBase:RU003928};
Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|RuleBase:RU003928};
Reference proteome {ECO:0000313|Proteomes:UP000008912}.
DOMAIN 133 192 CBS. {ECO:0000259|PROSITE:PS51371}.
DOMAIN 198 256 CBS. {ECO:0000259|PROSITE:PS51371}.
NP_BIND 293 295 NAD. {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|PIRSR:PIRSR000130-3}.
NP_BIND 343 345 NAD. {ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|PIRSR:PIRSR000130-3}.
REGION 383 385 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_03156}.
REGION 406 407 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_03156}.
REGION 430 434 IMP binding. {ECO:0000256|HAMAP-
Rule:MF_03156}.
ACT_SITE 350 350 Thioimidate intermediate.
{ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|PIRSR:PIRSR000130-1}.
ACT_SITE 448 448 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_03156,
ECO:0000256|PIRSR:PIRSR000130-1}.
METAL 345 345 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|PIRSR:PIRSR000130-4}.
METAL 347 347 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|PIRSR:PIRSR000130-4}.
METAL 350 350 Potassium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03156,
ECO:0000256|PIRSR:PIRSR000130-4}.
METAL 515 515 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000256|HAMAP-Rule:MF_03156}.
BINDING 348 348 IMP. {ECO:0000256|HAMAP-Rule:MF_03156}.
BINDING 460 460 IMP. {ECO:0000256|HAMAP-Rule:MF_03156}.
SEQUENCE 533 AA; 57415 MW; 5F2D791DC11BFBB5 CRC64;
SRVLLAGVGV RMDASSELXX XXXXXXXGTG YVPEDGLTAQ QLFANADGLT YNDFLILPGF
IDFIADEVDL TSALTRKITL KTPLVSSPMD TVTEADMAIA MALMGGIGFI HHNCTPEFQA
NEVRKVKKFE QGFITDPVVL SPSHTVGDVL EAKIRHGFSG IPITETGTMG SKLVGIVTSR
DIDFLAEKDH TTLLSEVMTP RNELVVAPAG VTLKEANEIL QRSKKGKLPI VNDRDELVAI
IARTDLKKNR DYPLASKDSH KQLLCGAAVG TREDDKYRLD LLTQAGADVI VLDSSQGNSV
YQIAMVHYIK QKYPHLQVIG GNVVTAAQAK NLIDAGVDGL RVGMGCGSIC ITQEVMACGR
PQGTAVYKVA EYARRFGVPV IADGGIQTVG HVVKALALGA STVMMGSLLA ATTEAPGEYF
FSDGVRLKKY RGMGSLDAME KSSSSQKRYF SEGDKVKIAQ GVSGSIQDKG SIQKFVPYLI
AGIQHGCQDI GARSLSVLRS MMYSGELKFE KRTMSAQIEG GVHGLHSYEK RLY


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