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Inosine-5'-monophosphate dehydrogenase 2 (IMP dehydrogenase 2) (IMPD 2) (IMPDH 2) (EC 1.1.1.205) (IMPDH-II)

 IMDH2_CRIGR             Reviewed;         514 AA.
P12269; G3IB73;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
27-SEP-2017, entry version 138.
RecName: Full=Inosine-5'-monophosphate dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_03156};
Short=IMP dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_03156};
Short=IMPD 2 {ECO:0000255|HAMAP-Rule:MF_03156};
Short=IMPDH 2 {ECO:0000255|HAMAP-Rule:MF_03156};
EC=1.1.1.205 {ECO:0000255|HAMAP-Rule:MF_03156};
AltName: Full=IMPDH-II;
Name=IMPDH2 {ECO:0000255|HAMAP-Rule:MF_03156};
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 336-370.
PubMed=2902093;
Collart F.R., Huberman E.;
"Cloning and sequence analysis of the human and Chinese hamster
inosine-5'-monophosphate dehydrogenase cDNAs.";
J. Biol. Chem. 263:15769-15772(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=21804562; DOI=10.1038/nbt.1932;
Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W.,
Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B.,
Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J.,
Quake S.R., Famili I., Palsson B.O., Wang J.;
"The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell
line.";
Nat. Biotechnol. 29:735-741(2011).
[3]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
THE INHIBITOR MYCOPHENOLIC ACID (MPA), AND MUTAGENESIS OF SER-275;
SER-276; SER-329; CYS-331; THR-333; ASP-364; GLN-368 AND GLN-441.
PubMed=8681386; DOI=10.1016/S0092-8674(00)81275-1;
Sintchak M.D., Fleming M.A., Futer O., Raybuck S.A., Chambers S.P.,
Caron P.R., Murcko M.A., Wilson K.P.;
"Structure and mechanism of inosine monophosphate dehydrogenase in
complex with the immunosuppressant mycophenolic acid.";
Cell 85:921-930(1996).
-!- 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:0000255|HAMAP-
Rule:MF_03156}.
-!- 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;
-!- 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,
ECO:0000269|PubMed:8681386}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156}.
Nucleus {ECO:0000255|HAMAP-Rule:MF_03156}.
-!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP-
Rule:MF_03156}.
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EMBL; J04209; AAA36993.1; -; mRNA.
EMBL; JH001800; EGW10487.1; -; Genomic_DNA.
RefSeq; NP_001233751.1; NM_001246822.1.
PDB; 1JR1; X-ray; 2.60 A; A/B=1-514.
PDBsum; 1JR1; -.
ProteinModelPortal; P12269; -.
SMR; P12269; -.
PRIDE; P12269; -.
GeneID; 100689398; -.
KEGG; cge:100689398; -.
CTD; 3615; -.
HOVERGEN; HBG052122; -.
InParanoid; P12269; -.
KO; K00088; -.
UniPathway; UPA00601; UER00295.
EvolutionaryTrace; P12269; -.
PRO; PR:P12269; -.
Proteomes; UP000001075; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl.
GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; ISS:UniProtKB.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
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.
1: Evidence at protein level;
3D-structure; Acetylation; CBS domain; Complete proteome; Cytoplasm;
Direct protein sequencing; GMP biosynthesis; Isopeptide bond;
Metal-binding; NAD; Nucleus; Oxidoreductase; Phosphoprotein;
Potassium; Purine biosynthesis; Reference proteome; Repeat;
Ubl conjugation.
CHAIN 1 514 Inosine-5'-monophosphate dehydrogenase 2.
/FTId=PRO_0000093672.
DOMAIN 114 173 CBS 1. {ECO:0000255|HAMAP-Rule:MF_03156}.
DOMAIN 179 237 CBS 2. {ECO:0000255|HAMAP-Rule:MF_03156}.
NP_BIND 274 276 NAD. {ECO:0000255|HAMAP-Rule:MF_03156}.
NP_BIND 324 326 NAD. {ECO:0000255|HAMAP-Rule:MF_03156}.
REGION 364 366 IMP binding.
REGION 387 388 IMP binding.
REGION 411 415 IMP binding.
ACT_SITE 331 331 Thioimidate intermediate.
ACT_SITE 429 429 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03156}.
METAL 326 326 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 328 328 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 331 331 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 500 500 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 501 501 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_03156}.
METAL 502 502 Potassium; via carbonyl oxygen; shared
with tetrameric partner.
{ECO:0000255|HAMAP-Rule:MF_03156}.
BINDING 276 276 Inhibitor.
BINDING 329 329 IMP.
BINDING 333 333 Inhibitor.
BINDING 441 441 IMP.
MOD_RES 122 122 Phosphoserine.
{ECO:0000250|UniProtKB:P12268}.
MOD_RES 160 160 Phosphoserine.
{ECO:0000250|UniProtKB:P12268}.
MOD_RES 400 400 Phosphotyrosine.
{ECO:0000250|UniProtKB:P12268}.
MOD_RES 416 416 Phosphoserine.
{ECO:0000250|UniProtKB:P12268}.
MOD_RES 511 511 N6-acetyllysine.
{ECO:0000250|UniProtKB:P12268}.
CROSSLNK 195 195 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P12268}.
CROSSLNK 208 208 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P12268}.
CROSSLNK 438 438 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P12268}.
MUTAGEN 275 275 S->A: No effect.
{ECO:0000269|PubMed:8681386}.
MUTAGEN 276 276 S->A: Increases Ki for MPA 7-fold.
{ECO:0000269|PubMed:8681386}.
MUTAGEN 329 329 S->A: Reduces activity by 87%.
{ECO:0000269|PubMed:8681386}.
MUTAGEN 331 331 C->A: Loss of activity.
{ECO:0000269|PubMed:8681386}.
MUTAGEN 333 333 T->I: Increases Ki for MPA 300-fold.
{ECO:0000269|PubMed:8681386}.
MUTAGEN 364 364 D->A: Loss of activity.
{ECO:0000269|PubMed:8681386}.
MUTAGEN 368 368 Q->A: No effect.
{ECO:0000269|PubMed:8681386}.
MUTAGEN 441 441 Q->A: Reduces activity by over 95% and
increases Ki for MPA 25-fold.
{ECO:0000269|PubMed:8681386}.
HELIX 20 23 {ECO:0000244|PDB:1JR1}.
HELIX 32 34 {ECO:0000244|PDB:1JR1}.
STRAND 35 37 {ECO:0000244|PDB:1JR1}.
HELIX 46 48 {ECO:0000244|PDB:1JR1}.
STRAND 53 58 {ECO:0000244|PDB:1JR1}.
STRAND 60 63 {ECO:0000244|PDB:1JR1}.
STRAND 65 67 {ECO:0000244|PDB:1JR1}.
TURN 71 73 {ECO:0000244|PDB:1JR1}.
HELIX 76 85 {ECO:0000244|PDB:1JR1}.
STRAND 88 91 {ECO:0000244|PDB:1JR1}.
HELIX 97 108 {ECO:0000244|PDB:1JR1}.
STRAND 113 115 {ECO:0000244|PDB:1JR1}.
HELIX 194 200 {ECO:0000244|PDB:1JR1}.
STRAND 210 213 {ECO:0000244|PDB:1JR1}.
TURN 214 216 {ECO:0000244|PDB:1JR1}.
STRAND 217 222 {ECO:0000244|PDB:1JR1}.
HELIX 224 232 {ECO:0000244|PDB:1JR1}.
STRAND 247 250 {ECO:0000244|PDB:1JR1}.
HELIX 255 266 {ECO:0000244|PDB:1JR1}.
STRAND 270 273 {ECO:0000244|PDB:1JR1}.
HELIX 281 293 {ECO:0000244|PDB:1JR1}.
STRAND 298 304 {ECO:0000244|PDB:1JR1}.
HELIX 307 316 {ECO:0000244|PDB:1JR1}.
STRAND 319 323 {ECO:0000244|PDB:1JR1}.
HELIX 333 337 {ECO:0000244|PDB:1JR1}.
HELIX 343 354 {ECO:0000244|PDB:1JR1}.
HELIX 355 357 {ECO:0000244|PDB:1JR1}.
STRAND 361 365 {ECO:0000244|PDB:1JR1}.
HELIX 370 378 {ECO:0000244|PDB:1JR1}.
STRAND 382 387 {ECO:0000244|PDB:1JR1}.
TURN 388 392 {ECO:0000244|PDB:1JR1}.
STRAND 396 398 {ECO:0000244|PDB:1JR1}.
STRAND 401 405 {ECO:0000244|PDB:1JR1}.
STRAND 407 412 {ECO:0000244|PDB:1JR1}.
TURN 417 419 {ECO:0000244|PDB:1JR1}.
STRAND 444 448 {ECO:0000244|PDB:1JR1}.
HELIX 453 470 {ECO:0000244|PDB:1JR1}.
HELIX 476 485 {ECO:0000244|PDB:1JR1}.
STRAND 490 492 {ECO:0000244|PDB:1JR1}.
HELIX 495 501 {ECO:0000244|PDB:1JR1}.
SEQUENCE 514 AA; 55890 MW; 5FA0138FA41E8A02 CRC64;
MADYLISGGT SYVPDDGLTA QQLFNCGDGL TYNDFLILPG YIDFTADQVD LTSALTKKIT
LKTPLVSSPM DTVTEAGMAI AMALTGGIGF IHHNCTPEFQ ANEVRKVKKY EQGFITDPVV
LSPKDRVRDV FEAKARHGFC GIPITDTGRM GSRLVGIISS RDIDFLKEEE HDRFLEEIMT
KREDLVVAPA GITLKEANEI LQRSKKGKLP IVNENDELVA IIARTDLKKN RDYPLASKDA
KKQLLCGAAI GTHEDDKYRL DLLALAGVDV VVLDSSQGNS IFQINMIKYM KEKYPNLQVI
GGNVVTAAQA KNLIDAGVDA LRVGMGCGSI CITQEVLACG RPQATAVYKV SEYARRFGVP
VIADGGIQNV GHIAKALALG ASTVMMGSLL AATTEAPGEY FFSDGIRLKK YRGMGSLDAM
DKHLSSQNRY FSEADKIKVA QGVSGAVQDK GSIHKFVPYL IAGIQHSCQD IGAKSLTQVR
AMMYSGELKF EKRTSSAQVE GGVHSLHSYE KRLF


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