GMPR2_HUMAN
ID GMPR2_HUMAN Reviewed; 348 AA.
AC Q9P2T1; D3DS66; Q567T0; Q6IAJ8; Q86T14;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=GMP reductase 2 {ECO:0000255|HAMAP-Rule:MF_03195};
DE Short=GMPR 2 {ECO:0000255|HAMAP-Rule:MF_03195};
DE EC=1.7.1.7 {ECO:0000255|HAMAP-Rule:MF_03195};
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase 2 {ECO:0000255|HAMAP-Rule:MF_03195};
DE Short=Guanosine monophosphate reductase 2 {ECO:0000255|HAMAP-Rule:MF_03195};
GN Name=GMPR2 {ECO:0000255|HAMAP-Rule:MF_03195};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=12009299; DOI=10.1016/s1357-2725(02)00024-9;
RA Deng Y., Wang Z., Ying K., Gu S., Ji C., Huang Y., Gu X., Wang Y., Xu Y.,
RA Li Y., Xie Y., Mao Y.;
RT "NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression,
RT purification, and kinetic properties.";
RL Int. J. Biochem. Cell Biol. 34:1035-1050(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12669231; DOI=10.1007/s00432-002-0413-7;
RA Zhang J., Zhang W., Zou D., Chen G., Wan T., Zhang M., Cao X.;
RT "Cloning and functional characterization of GMPR2, a novel human guanosine
RT monophosphate reductase, which promotes the monocytic differentiation of
RT HL-60 leukemia cells.";
RL J. Cancer Res. Clin. Oncol. 129:76-83(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Okaze H., Hayashi A., Kozuma S., Saito T.;
RT "A novel protein related to guanosine monophosphate reductase.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Placenta, and T-cell;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-291, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH GMP, CATALYTIC
RP ACTIVITY, FUNCTION, ACTIVE SITE, SUBUNIT, AND MUTAGENESIS OF CYS-186.
RX PubMed=16359702; DOI=10.1016/j.jmb.2005.11.047;
RA Li J., Wei Z., Zheng M., Gu X., Deng Y., Qiu R., Chen F., Ji C., Gong W.,
RA Xie Y., Mao Y.;
RT "Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in
RT complex with GMP.";
RL J. Mol. Biol. 355:980-988(2006).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 10-341 IN COMPLEX WITH IMP AND
RP NADP, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, SUBUNIT, AND MUTAGENESIS
RP OF CYS-186; THR-188 AND GLU-289.
RX PubMed=22037469; DOI=10.1038/nchembio.693;
RA Patton G.C., Stenmark P., Gollapalli D.R., Sevastik R., Kursula P.,
RA Flodin S., Schuler H., Swales C.T., Eklund H., Himo F., Nordlund P.,
RA Hedstrom L.;
RT "Cofactor mobility determines reaction outcome in the IMPDH and GMPR (beta-
RT alpha)8 barrel enzymes.";
RL Nat. Chem. Biol. 7:950-958(2011).
CC -!- FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP
CC to IMP. It functions in the conversion of nucleobase, nucleoside and
CC nucleotide derivatives of G to A nucleotides, and in maintaining the
CC intracellular balance of A and G nucleotides (PubMed:12009299,
CC PubMed:12669231, PubMed:16359702, PubMed:22037469). Plays a role in
CC modulating cellular differentiation (PubMed:12669231).
CC {ECO:0000255|HAMAP-Rule:MF_03195, ECO:0000269|PubMed:12009299,
CC ECO:0000269|PubMed:12669231, ECO:0000269|PubMed:16359702,
CC ECO:0000269|PubMed:22037469}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:17185, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:58349; EC=1.7.1.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03195, ECO:0000269|PubMed:12009299,
CC ECO:0000269|PubMed:16359702, ECO:0000269|PubMed:22037469};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03195,
CC ECO:0000269|PubMed:16359702, ECO:0000269|PubMed:22037469}.
CC -!- INTERACTION:
CC Q9P2T1; P50222: MEOX2; NbExp=3; IntAct=EBI-2806548, EBI-748397;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9P2T1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2T1-2; Sequence=VSP_041459;
CC Name=3;
CC IsoId=Q9P2T1-3; Sequence=VSP_054585;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, kidney,
CC brain, liver, prostate, spleen, placenta, testis and ovary. Low
CC expression in colon, thymus and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:12009299, ECO:0000269|PubMed:12669231}.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03195}.
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DR EMBL; AF419346; AAN32701.1; -; mRNA.
DR EMBL; AF135159; AAG09132.1; -; mRNA.
DR EMBL; AB032903; BAA93080.1; -; mRNA.
DR EMBL; BX161436; CAD61908.1; -; mRNA.
DR EMBL; BX247993; CAD62327.1; -; mRNA.
DR EMBL; CR457156; CAG33437.1; -; mRNA.
DR EMBL; AL096870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66051.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66053.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66054.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66056.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66057.1; -; Genomic_DNA.
DR EMBL; BC008021; AAH08021.2; -; mRNA.
DR EMBL; BC009832; AAH09832.1; -; mRNA.
DR EMBL; BC093039; AAH93039.1; -; mRNA.
DR CCDS; CCDS41935.1; -. [Q9P2T1-1]
DR CCDS; CCDS45087.1; -. [Q9P2T1-2]
DR CCDS; CCDS61419.1; -. [Q9P2T1-3]
DR RefSeq; NP_001002000.1; NM_001002000.2. [Q9P2T1-1]
DR RefSeq; NP_001002001.1; NM_001002001.2. [Q9P2T1-1]
DR RefSeq; NP_001002002.1; NM_001002002.2. [Q9P2T1-1]
DR RefSeq; NP_001269950.1; NM_001283021.1.
DR RefSeq; NP_001269951.1; NM_001283022.1.
DR RefSeq; NP_001269952.1; NM_001283023.1. [Q9P2T1-3]
DR RefSeq; NP_057660.2; NM_016576.4. [Q9P2T1-2]
DR PDB; 2A7R; X-ray; 3.00 A; A/B/C/D=1-348.
DR PDB; 2BZN; X-ray; 2.15 A; A/B/C/D/E/F/G/H=10-341.
DR PDB; 2C6Q; X-ray; 1.70 A; A/B/C/D/E/F/G/H=10-341.
DR PDBsum; 2A7R; -.
DR PDBsum; 2BZN; -.
DR PDBsum; 2C6Q; -.
DR AlphaFoldDB; Q9P2T1; -.
DR SMR; Q9P2T1; -.
DR BioGRID; 119443; 13.
DR ComplexPortal; CPX-2154; Guanosine monophosphate reductase 2.
DR IntAct; Q9P2T1; 3.
DR MINT; Q9P2T1; -.
DR BindingDB; Q9P2T1; -.
DR ChEMBL; CHEMBL4296017; -.
DR iPTMnet; Q9P2T1; -.
DR PhosphoSitePlus; Q9P2T1; -.
DR BioMuta; GMPR2; -.
DR DMDM; 25008511; -.
DR EPD; Q9P2T1; -.
DR jPOST; Q9P2T1; -.
DR MassIVE; Q9P2T1; -.
DR MaxQB; Q9P2T1; -.
DR PaxDb; Q9P2T1; -.
DR PeptideAtlas; Q9P2T1; -.
DR PRIDE; Q9P2T1; -.
DR ProteomicsDB; 69657; -.
DR ProteomicsDB; 83896; -. [Q9P2T1-1]
DR ProteomicsDB; 83897; -. [Q9P2T1-2]
DR Antibodypedia; 61; 116 antibodies from 18 providers.
DR DNASU; 51292; -.
DR Ensembl; ENST00000355299.8; ENSP00000347449.4; ENSG00000100938.19. [Q9P2T1-1]
DR Ensembl; ENST00000399440.7; ENSP00000382369.2; ENSG00000100938.19. [Q9P2T1-1]
DR Ensembl; ENST00000420554.6; ENSP00000392859.2; ENSG00000100938.19. [Q9P2T1-2]
DR Ensembl; ENST00000456667.7; ENSP00000405743.3; ENSG00000100938.19. [Q9P2T1-3]
DR Ensembl; ENST00000559836.5; ENSP00000453299.1; ENSG00000100938.19. [Q9P2T1-1]
DR Ensembl; ENST00000642276.1; ENSP00000496504.1; ENSG00000284752.3. [Q9P2T1-1]
DR Ensembl; ENST00000643803.1; ENSP00000495708.1; ENSG00000284752.3. [Q9P2T1-3]
DR Ensembl; ENST00000644066.1; ENSP00000494224.1; ENSG00000284752.3. [Q9P2T1-1]
DR Ensembl; ENST00000645781.1; ENSP00000496234.1; ENSG00000284752.3. [Q9P2T1-2]
DR Ensembl; ENST00000647320.3; ENSP00000495583.1; ENSG00000284752.3. [Q9P2T1-1]
DR GeneID; 51292; -.
DR KEGG; hsa:51292; -.
DR MANE-Select; ENST00000399440.7; ENSP00000382369.2; NM_001002002.3; NP_001002002.1.
DR UCSC; uc001wnr.5; human. [Q9P2T1-1]
DR CTD; 51292; -.
DR DisGeNET; 51292; -.
DR GeneCards; GMPR2; -.
DR HGNC; HGNC:4377; GMPR2.
DR HPA; ENSG00000100938; Low tissue specificity.
DR MIM; 610781; gene.
DR neXtProt; NX_Q9P2T1; -.
DR OpenTargets; ENSG00000100938; -.
DR PharmGKB; PA28762; -.
DR VEuPathDB; HostDB:ENSG00000100938; -.
DR eggNOG; KOG2550; Eukaryota.
DR GeneTree; ENSGT00940000159574; -.
DR HOGENOM; CLU_022552_5_3_1; -.
DR InParanoid; Q9P2T1; -.
DR OrthoDB; 618077at2759; -.
DR PhylomeDB; Q9P2T1; -.
DR TreeFam; TF300378; -.
DR BRENDA; 1.7.1.7; 2681.
DR PathwayCommons; Q9P2T1; -.
DR Reactome; R-HSA-74217; Purine salvage.
DR SignaLink; Q9P2T1; -.
DR BioGRID-ORCS; 51292; 9 hits in 1076 CRISPR screens.
DR ChiTaRS; GMPR2; human.
DR EvolutionaryTrace; Q9P2T1; -.
DR GenomeRNAi; 51292; -.
DR Pharos; Q9P2T1; Tbio.
DR PRO; PR:Q9P2T1; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9P2T1; protein.
DR Bgee; ENSG00000100938; Expressed in right adrenal gland and 98 other tissues.
DR ExpressionAtlas; Q9P2T1; baseline and differential.
DR Genevisible; Q9P2T1; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR GO; GO:0003920; F:GMP reductase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046037; P:GMP metabolic process; IDA:UniProtKB.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00596; GMP_reduct_type1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005993; GMPR.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000235; GMP_reductase; 1.
DR TIGRFAMs; TIGR01305; GMP_reduct_1; 1.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Metal-binding; NADP;
KW Oxidoreductase; Potassium; Purine metabolism; Reference proteome.
FT CHAIN 1..348
FT /note="GMP reductase 2"
FT /id="PRO_0000093726"
FT ACT_SITE 186
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT ACT_SITE 188
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 26..27
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195,
FT ECO:0000269|PubMed:22037469"
FT BINDING 78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195,
FT ECO:0000269|PubMed:22037469"
FT BINDING 129..131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195,
FT ECO:0000269|PubMed:22037469"
FT BINDING 180..181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195,
FT ECO:0000269|PubMed:22037469"
FT BINDING 181
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 183
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 186
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 189
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 219..221
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 242..243
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 268..270
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 269
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195,
FT ECO:0000269|PubMed:22037469"
FT BINDING 285..286
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195,
FT ECO:0000269|PubMed:22037469"
FT BINDING 286..290
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 314..317
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195,
FT ECO:0000269|PubMed:22037469"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1
FT /note="M -> MTSCLPALRFIATPRLSAM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041459"
FT VAR_SEQ 70..97
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_054585"
FT VARIANT 242
FT /note="G -> D (in dbSNP:rs34354104)"
FT /id="VAR_049602"
FT MUTAGEN 186
FT /note="C->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:16359702,
FT ECO:0000269|PubMed:22037469"
FT MUTAGEN 188
FT /note="T->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22037469"
FT MUTAGEN 289
FT /note="E->Q: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22037469"
FT CONFLICT 91
FT /note="Q -> R (in Ref. 5; CAG33437)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="S -> G (in Ref. 5; CAG33437)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="S -> N (in Ref. 5; CAG33437)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2A7R"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:2C6Q"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:2C6Q"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2C6Q"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:2C6Q"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2C6Q"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:2C6Q"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:2C6Q"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:2C6Q"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:2C6Q"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:2C6Q"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:2C6Q"
FT HELIX 198..211
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:2C6Q"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:2C6Q"
FT TURN 243..247
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:2A7R"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2A7R"
FT HELIX 272..278
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2C6Q"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:2A7R"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:2A7R"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:2C6Q"
FT HELIX 301..319
FT /evidence="ECO:0007829|PDB:2C6Q"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:2C6Q"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:2C6Q"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:2C6Q"
SQ SEQUENCE 348 AA; 37874 MW; E7812A754C433E51 CRC64;
MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV DLTRSFSFRN SKQTYSGVPI IAANMDTVGT
FEMAKVLCKF SLFTAVHKHY SLVQWQEFAG QNPDCLEHLA ASSGTGSSDF EQLEQILEAI
PQVKYICLDV ANGYSEHFVE FVKDVRKRFP QHTIMAGNVV TGEMVEELIL SGADIIKVGI
GPGSVCTTRK KTGVGYPQLS AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM
LGGMLAGHSE SGGELIERDG KKYKLFYGMS SEMAMKKYAG GVAEYRASEG KTVEVPFKGD
VEHTIRDILG GIRSTCTYVG AAKLKELSRR TTFIRVTQQV NPIFSEAC
