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

 IMDH2_HUMAN             Reviewed;         514 AA.
P12268; Q6LEF3;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 2.
10-OCT-2018, entry version 218.
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}; Synonyms=IMPD2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
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 [MRNA].
TISSUE=Spleen;
PubMed=1969416;
Natsumeda Y., Ohno S., Kawasaki H., Konno Y., Weber G., Suzuki K.;
"Two distinct cDNAs for human IMP dehydrogenase.";
J. Biol. Chem. 265:5292-5295(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
PubMed=7999076; DOI=10.1006/bbrc.1994.2698;
Glesne D.A., Huberman E.;
"Cloning and sequence of the human type II IMP dehydrogenase gene.";
Biochem. Biophys. Res. Commun. 205:537-544(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7896827; DOI=10.1074/jbc.270.12.6808;
Zimmermann A.G., Spychala J., Mitchell B.S.;
"Characterization of the human inosine-5'-monophosphate dehydrogenase
type II gene.";
J. Biol. Chem. 270:6808-6814(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=B-cell, Colon, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-514.
PubMed=8098009; DOI=10.1006/geno.1993.1177;
Glesne D.A., Collart F.R., Varkony T., Drabkin H., Huberman E.;
"Chromosomal localization and structure of the human type II IMP
dehydrogenase gene.";
Genomics 16:274-277(1993).
[7]
PROTEIN SEQUENCE OF 2-11, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
ACTIVITY REGULATION.
PubMed=7903306;
Carr S.F., Papp E., Wu J.C., Natsumeda Y.;
"Characterization of human type I and type II IMP dehydrogenases.";
J. Biol. Chem. 268:27286-27290(1993).
[8]
PROTEIN SEQUENCE OF N-TERMINUS, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=7763314; DOI=10.1016/0006-2952(95)00026-V;
Hager P.W., Collart F.R., Huberman E., Mitchell B.S.;
"Recombinant human inosine monophosphate dehydrogenase type I and type
II proteins. Purification and characterization of inhibitor binding.";
Biochem. Pharmacol. 49:1323-1329(1995).
[9]
SUBCELLULAR LOCATION, AND NUCLEIC ACID-BINDING.
PubMed=14766016; DOI=10.1042/BJ20031585;
McLean J.E., Hamaguchi N., Belenky P., Mortimer S.E., Stanton M.,
Hedstrom L.;
"Inosine 5'-monophosphate dehydrogenase binds nucleic acids in vitro
and in vivo.";
Biochem. J. 379:243-251(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-400, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
POLYMORPHISM, AND VARIANT PHE-263.
PubMed=17496727; DOI=10.1097/FPC.0b013e328012b8cf;
Wang J., Zeevi A., Webber S., Girnita D.M., Addonizio L., Selby R.,
Hutchinson I.V., Burckart G.J.;
"A novel variant L263F in human inosine 5'-monophosphate dehydrogenase
2 is associated with diminished enzyme activity.";
Pharmacogenet. Genomics 17:283-290(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-511, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-416, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122; SER-160 AND
SER-416, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[21]
ACETYLATION, AND INTERACTION WITH CLOCK.
PubMed=28985504; DOI=10.1016/j.molcel.2017.09.008;
Lin R., Mo Y., Zha H., Qu Z., Xie P., Zhu Z.J., Xu Y., Xiong Y.,
Guan K.L.;
"CLOCK acetylates ASS1 to drive circadian rhythm of ureagenesis.";
Mol. Cell 68:198-209(2017).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-195; LYS-208 AND LYS-438,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[23]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), AND ACTIVE SITE.
PubMed=10097070; DOI=10.1073/pnas.96.7.3531;
Colby T.D., Vanderveen K., Strickler M.D., Markham G.D.,
Goldstein B.M.;
"Crystal structure of human type II inosine monophosphate
dehydrogenase: implications for ligand binding and drug design.";
Proc. Natl. Acad. Sci. U.S.A. 96:3531-3536(1999).
[24]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH INHIBITOR AND
POTASSIUM.
Risal D., Strickler M.D., Goldstein B.M.;
"Crystal structure of human inosine monophosphate dehydrogenase type
II complexed with the MPA/NAD analog C2-MAD.";
Submitted (DEC-2002) to the PDB data bank.
[25]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH NAD(+).
Risal D., Strickler M.D., Goldstein B.M.;
"The conformation of NAD bound to human inosine monophosphate
Dehydrogenase Type II.";
Submitted (DEC-2002) to the PDB data bank.
-!- 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.
-!- 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;
-!- 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. Subject to product inhibition by XMP and NADH. Also
inhibited by ADP. {ECO:0000255|HAMAP-Rule:MF_03156,
ECO:0000269|PubMed:7903306}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=9.3 uM for Inosine 5'-phosphate {ECO:0000269|PubMed:7763314,
ECO:0000269|PubMed:7903306};
KM=32 uM for NAD(+) {ECO:0000269|PubMed:7763314,
ECO:0000269|PubMed:7903306};
-!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway;
XMP from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_03156}.
-!- SUBUNIT: Homotetramer (PubMed:7903306, Ref.24, Ref.25). Interacts
with CLOCK; in a circadian manner (PubMed:28985504).
{ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|PubMed:28985504,
ECO:0000269|PubMed:7903306, ECO:0000269|Ref.24,
ECO:0000269|Ref.25}.
-!- INTERACTION:
Q96GX9:APIP; NbExp=3; IntAct=EBI-353389, EBI-359248;
Q9BU20:CPLANE2; NbExp=5; IntAct=EBI-353389, EBI-750332;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156,
ECO:0000269|PubMed:14766016}. Nucleus {ECO:0000255|HAMAP-
Rule:MF_03156, ECO:0000269|PubMed:14766016}.
-!- TISSUE SPECIFICITY: IMP type I is the main species in normal
leukocytes and type II predominates over type I in the tumor.
-!- INDUCTION: Selectively up-regulated in neoplastic and replicating
cells.
-!- PTM: The N-terminus is blocked.
-!- PTM: Acetylated by CLOCK in a circadian manner (PubMed:28985504).
{ECO:0000269|PubMed:28985504}.
-!- POLYMORPHISM: Genetic variants in the IMPDH2 gene are responsible
for the large inter-individual variability in enzyme activity and
may influence immunosuppressive efficacy and side effects in
transplant recipients receiving mycophenolic acid [MIM:617995].
{ECO:0000269|PubMed:17496727}.
-!- MISCELLANEOUS: Because IMPDH activity is tightly linked with cell
proliferation, it has been recognized as a target for cancer and
viral chemotherapy and as a target for immunosuppressive drugs.
The activities of the antitumor drug tiazofurin, the antiviral
drug ribavirin, and the immunosuppressive drugs mizoribine and
mycophenolic acid (MPA) are attributed to the inhibition of IMPDH.
In addition, bacterial and parasitic IMPDH's differ significantly
from mammalian enzymes, which makes it a suitable target for anti-
infective drugs.
-!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP-
Rule:MF_03156}.
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EMBL; J04208; AAA36112.1; -; mRNA.
EMBL; L33842; AAA67054.1; -; Genomic_DNA.
EMBL; L39210; AAB70699.1; -; Genomic_DNA.
EMBL; BC006124; AAH06124.1; -; mRNA.
EMBL; BC012840; AAH12840.1; -; mRNA.
EMBL; BC015567; AAH15567.1; -; mRNA.
EMBL; L08114; AAA36113.1; -; Genomic_DNA.
CCDS; CCDS2786.1; -.
PIR; I52303; A31997.
RefSeq; NP_000875.2; NM_000884.2.
UniGene; Hs.654400; -.
PDB; 1B3O; X-ray; 2.90 A; A/B=1-514.
PDB; 1NF7; X-ray; 2.65 A; A/B=1-514.
PDB; 1NFB; X-ray; 2.90 A; A/B=1-514.
PDBsum; 1B3O; -.
PDBsum; 1NF7; -.
PDBsum; 1NFB; -.
ProteinModelPortal; P12268; -.
SMR; P12268; -.
BioGrid; 109828; 101.
IntAct; P12268; 40.
MINT; P12268; -.
STRING; 9606.ENSP00000321584; -.
BindingDB; P12268; -.
ChEMBL; CHEMBL2002; -.
DrugBank; DB04566; Inosinic Acid.
DrugBank; DB01033; Mercaptopurine.
DrugBank; DB00688; Mycophenolate mofetil.
DrugBank; DB01024; Mycophenolic acid.
DrugBank; DB00157; NADH.
DrugBank; DB00811; Ribavirin.
DrugBank; DB03070; Selenazole-4-Carboxyamide-Adenine Dinucleotide.
DrugBank; DB06103; VX-148.
GuidetoPHARMACOLOGY; 2625; -.
iPTMnet; P12268; -.
PhosphoSitePlus; P12268; -.
SwissPalm; P12268; -.
BioMuta; IMPDH2; -.
DMDM; 124419; -.
REPRODUCTION-2DPAGE; IPI00291510; -.
REPRODUCTION-2DPAGE; P12268; -.
UCD-2DPAGE; P12268; -.
EPD; P12268; -.
MaxQB; P12268; -.
PaxDb; P12268; -.
PeptideAtlas; P12268; -.
PRIDE; P12268; -.
ProteomicsDB; 52839; -.
TopDownProteomics; P12268; -.
DNASU; 3615; -.
Ensembl; ENST00000326739; ENSP00000321584; ENSG00000178035.
GeneID; 3615; -.
KEGG; hsa:3615; -.
UCSC; uc003cvt.4; human.
CTD; 3615; -.
DisGeNET; 3615; -.
EuPathDB; HostDB:ENSG00000178035.11; -.
GeneCards; IMPDH2; -.
HGNC; HGNC:6053; IMPDH2.
HPA; CAB020717; -.
HPA; HPA001400; -.
MIM; 146691; gene.
MIM; 617995; phenotype.
neXtProt; NX_P12268; -.
OpenTargets; ENSG00000178035; -.
PharmGKB; PA29863; -.
eggNOG; KOG2550; Eukaryota.
eggNOG; COG0516; LUCA.
eggNOG; COG0517; LUCA.
GeneTree; ENSGT00530000062923; -.
HOGENOM; HOG000165752; -.
HOVERGEN; HBG052122; -.
KO; K00088; -.
OMA; NLGSQNR; -.
OrthoDB; EOG091G0EAV; -.
PhylomeDB; P12268; -.
TreeFam; TF300378; -.
BioCyc; MetaCyc:HS11242-MONOMER; -.
BRENDA; 1.1.1.205; 2681.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-73817; Purine ribonucleoside monophosphate biosynthesis.
SABIO-RK; P12268; -.
UniPathway; UPA00601; UER00295.
ChiTaRS; IMPDH2; human.
EvolutionaryTrace; P12268; -.
GeneWiki; IMPDH2; -.
GenomeRNAi; 3615; -.
PRO; PR:P12268; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000178035; Expressed in 234 organ(s), highest expression level in right ovary.
CleanEx; HS_IMPDH2; -.
ExpressionAtlas; P12268; baseline and differential.
Genevisible; P12268; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005778; C:peroxisomal membrane; HDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003938; F:IMP dehydrogenase activity; EXP:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0000166; F:nucleotide binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; IDA:UniProtKB.
GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0006183; P:GTP biosynthetic process; IBA:GO_Central.
GO; GO:0046651; P:lymphocyte proliferation; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; TAS:Reactome.
GO; GO:0060041; P:retina development in camera-type eye; 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; DNA-binding; GMP biosynthesis;
Isopeptide bond; Metal-binding; NAD; Nucleus; Oxidoreductase;
Phosphoprotein; Polymorphism; Potassium; Purine biosynthesis;
Reference proteome; Repeat; RNA-binding; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000255|HAMAP-
Rule:MF_03156,
ECO:0000269|PubMed:7903306}.
CHAIN 2 514 Inosine-5'-monophosphate dehydrogenase 2.
/FTId=PRO_0000093673.
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.
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. {ECO:0000255|HAMAP-
Rule:MF_03156}.
ACT_SITE 331 331 Thioimidate intermediate.
{ECO:0000255|HAMAP-Rule:MF_03156,
ECO:0000269|PubMed:10097070}.
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,
ECO:0000269|Ref.24}.
METAL 328 328 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03156,
ECO:0000269|Ref.24}.
METAL 331 331 Potassium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_03156,
ECO:0000269|Ref.24}.
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 329 329 IMP. {ECO:0000255|HAMAP-Rule:MF_03156}.
BINDING 441 441 IMP. {ECO:0000255|HAMAP-Rule:MF_03156}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 160 160 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 400 400 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 416 416 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 511 511 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 195 195 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 208 208 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 438 438 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 263 263 L -> F (functional polymorphism; results
in 10-fold decrease of enzymatic
activity; dbSNP:rs121434586).
{ECO:0000269|PubMed:17496727}.
/FTId=VAR_070542.
CONFLICT 190 191 AG -> RS (in Ref. 1; AAA36112).
{ECO:0000305}.
STRAND 17 19 {ECO:0000244|PDB:1B3O}.
HELIX 20 24 {ECO:0000244|PDB:1NF7}.
STRAND 25 27 {ECO:0000244|PDB:1NF7}.
HELIX 32 34 {ECO:0000244|PDB:1NF7}.
STRAND 35 37 {ECO:0000244|PDB:1NF7}.
HELIX 46 48 {ECO:0000244|PDB:1NF7}.
STRAND 53 58 {ECO:0000244|PDB:1NF7}.
STRAND 60 67 {ECO:0000244|PDB:1NF7}.
TURN 71 73 {ECO:0000244|PDB:1NF7}.
HELIX 77 85 {ECO:0000244|PDB:1NF7}.
STRAND 89 91 {ECO:0000244|PDB:1B3O}.
HELIX 97 108 {ECO:0000244|PDB:1NF7}.
TURN 109 113 {ECO:0000244|PDB:1B3O}.
STRAND 123 125 {ECO:0000244|PDB:1B3O}.
STRAND 142 149 {ECO:0000244|PDB:1B3O}.
STRAND 152 158 {ECO:0000244|PDB:1B3O}.
HELIX 161 164 {ECO:0000244|PDB:1NF7}.
TURN 175 177 {ECO:0000244|PDB:1NF7}.
STRAND 183 185 {ECO:0000244|PDB:1NF7}.
HELIX 194 203 {ECO:0000244|PDB:1NF7}.
STRAND 209 212 {ECO:0000244|PDB:1B3O}.
STRAND 214 216 {ECO:0000244|PDB:1NF7}.
STRAND 220 222 {ECO:0000244|PDB:1NF7}.
STRAND 247 250 {ECO:0000244|PDB:1NF7}.
HELIX 256 265 {ECO:0000244|PDB:1NF7}.
STRAND 270 273 {ECO:0000244|PDB:1NF7}.
HELIX 281 293 {ECO:0000244|PDB:1NF7}.
STRAND 295 304 {ECO:0000244|PDB:1NF7}.
HELIX 307 316 {ECO:0000244|PDB:1NF7}.
STRAND 319 323 {ECO:0000244|PDB:1NF7}.
STRAND 328 331 {ECO:0000244|PDB:1NF7}.
HELIX 333 336 {ECO:0000244|PDB:1NF7}.
HELIX 343 354 {ECO:0000244|PDB:1NF7}.
HELIX 355 357 {ECO:0000244|PDB:1NF7}.
STRAND 361 365 {ECO:0000244|PDB:1NF7}.
HELIX 370 378 {ECO:0000244|PDB:1NF7}.
STRAND 382 387 {ECO:0000244|PDB:1NF7}.
HELIX 388 390 {ECO:0000244|PDB:1NF7}.
STRAND 396 398 {ECO:0000244|PDB:1NF7}.
STRAND 404 406 {ECO:0000244|PDB:1NF7}.
STRAND 409 412 {ECO:0000244|PDB:1NF7}.
TURN 417 419 {ECO:0000244|PDB:1NF7}.
STRAND 444 447 {ECO:0000244|PDB:1NF7}.
HELIX 453 471 {ECO:0000244|PDB:1NF7}.
HELIX 476 484 {ECO:0000244|PDB:1NF7}.
STRAND 490 492 {ECO:0000244|PDB:1NF7}.
HELIX 495 501 {ECO:0000244|PDB:1NF7}.
SEQUENCE 514 AA; 55805 MW; 876BEA0EC1DDBEE9 CRC64;
MADYLISGGT SYVPDDGLTA QQLFNCGDGL TYNDFLILPG YIDFTADQVD LTSALTKKIT
LKTPLVSSPM DTVTEAGMAI AMALTGGIGF IHHNCTPEFQ ANEVRKVKKY EQGFITDPVV
LSPKDRVRDV FEAKARHGFC GIPITDTGRM GSRLVGIISS RDIDFLKEEE HDCFLEEIMT
KREDLVVAPA GITLKEANEI LQRSKKGKLP IVNEDDELVA IIARTDLKKN RDYPLASKDA
KKQLLCGAAI GTHEDDKYRL DLLAQAGVDV VVLDSSQGNS IFQINMIKYI KDKYPNLQVI
GGNVVTAAQA KNLIDAGVDA LRVGMGSGSI CITQEVLACG RPQATAVYKV SEYARRFGVP
VIADGGIQNV GHIAKALALG ASTVMMGSLL AATTEAPGEY FFSDGIRLKK YRGMGSLDAM
DKHLSSQNRY FSEADKIKVA QGVSGAVQDK GSIHKFVPYL IAGIQHSCQD IGAKSLTQVR
AMMYSGELKF EKRTSSAQVE GGVHSLHSYE KRLF


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