BUP1_HUMAN
ID BUP1_HUMAN Reviewed; 384 AA.
AC Q9UBR1; A3KMF8; Q9UIR3;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Beta-ureidopropionase;
DE EC=3.5.1.6 {ECO:0000269|PubMed:10415095, ECO:0000269|PubMed:10542323, ECO:0000269|PubMed:11508704, ECO:0000269|PubMed:22525402, ECO:0000269|PubMed:24526388, ECO:0000269|PubMed:29976570};
DE AltName: Full=BUP-1 {ECO:0000303|PubMed:10542323};
DE AltName: Full=Beta-alanine synthase;
DE AltName: Full=N-carbamoyl-beta-alanine amidohydrolase;
GN Name=UPB1; Synonyms=BUP1;
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 [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=10542323; DOI=10.1016/s0167-4781(99)00182-7;
RA Vreken P., van Kuilenburg A.B.P., Hamajima N., Meinsma R., van Lenthe H.,
RA Goehlich-Ratmann G., Assmann B.E., Wevers R.A., van Gennip A.H.;
RT "cDNA cloning, genomic structure and chromosomal localization of the human
RT BUP-1 gene encoding beta-ureidopropionase.";
RL Biochim. Biophys. Acta 1447:251-257(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP ZINC-BINDING.
RC TISSUE=Liver;
RX PubMed=11508704; DOI=10.3177/jnsv.47.132;
RA Sakamoto T., Sakata S.F., Matsuda K., Horikawa Y., Tamaki N.;
RT "Expression and properties of human liver beta-ureidopropionase.";
RL J. Nutr. Sci. Vitaminol. 47:132-138(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=10415095; DOI=10.1006/abio.1999.4181;
RA Van Kuilenburg A.B., Van Lenthe H., Van Gennip A.H.;
RT "A radiochemical assay for beta-ureidopropionase using radiolabeled N-
RT carbamyl-beta-alanine obtained via hydrolysis of [2-(14)C]5, 6-
RT dihydrouracil.";
RL Anal. Biochem. 272:250-253(1999).
RN [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF MUTANT CYS-299, FUNCTION,
RP CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBUNIT, LACK OF ZINC BINDING, ACTIVE SITE, AND MUTAGENESIS OF
RP ARG-130; LYS-132; SER-208; CYS-233 AND THR-299.
RX PubMed=29976570; DOI=10.1042/bcj20180222;
RA Maurer D., Lohkamp B., Krumpel M., Widersten M., Dobritzsch D.;
RT "Crystal structure and pH-dependent allosteric regulation of human beta-
RT ureidopropionase, an enzyme involved in anticancer drug metabolism.";
RL Biochem. J. 475:2395-2416(2018).
RN [9]
RP VARIANT UPB1D GLU-85, AND CHARACTERIZATION OF VARIANT UPB1D GLU-85.
RX PubMed=15385443; DOI=10.1093/hmg/ddh303;
RA van Kuilenburg A.B.P., Meinsma R., Beke E., Assmann B., Ribes A.,
RA Lorente I., Busch R., Mayatepek E., Abeling N.G.G.M., van Cruchten A.,
RA Stroomer A.E.M., van Lenthe H., Zoetekouw L., Kulik W., Hoffmann G.F.,
RA Voit T., Wevers R.A., Rutsch F., van Gennip A.H.;
RT "Beta-ureidopropionase deficiency: an inborn error of pyrimidine
RT degradation associated with neurological abnormalities.";
RL Hum. Mol. Genet. 13:2793-2801(2004).
RN [10]
RP VARIANTS UPB1D SER-13; ARG-235; TRP-236; ARG-264; GLN-326 AND MET-359,
RP CHARACTERIZATION OF VARIANTS UPB1D SER-13; ARG-235; ARG-264; GLN-326;
RP TRP-326 AND MET-359, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND
RP TISSUE SPECIFICITY.
RX PubMed=22525402; DOI=10.1016/j.bbadis.2012.04.001;
RA van Kuilenburg A.B., Dobritzsch D., Meijer J., Krumpel M., Selim L.A.,
RA Rashed M.S., Assmann B., Meinsma R., Lohkamp B., Ito T., Abeling N.G.,
RA Saito K., Eto K., Smitka M., Engvall M., Zhang C., Xu W., Zoetekouw L.,
RA Hennekam R.C.;
RT "Beta-ureidopropionase deficiency: phenotype, genotype and protein
RT structural consequences in 16 patients.";
RL Biochim. Biophys. Acta 1822:1096-1108(2012).
RN [11]
RP VARIANTS UPB1D SER-13; LYS-271; THR-286 AND GLN-326, CHARACTERIZATION OF
RP VARIANTS UPB1D SER-13; LYS-271; THR-286 AND GLN-326, FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, AND SUBUNIT.
RX PubMed=24526388; DOI=10.1007/s10545-014-9682-y;
RA Nakajima Y., Meijer J., Dobritzsch D., Ito T., Meinsma R., Abeling N.G.,
RA Roelofsen J., Zoetekouw L., Watanabe Y., Tashiro K., Lee T., Takeshima Y.,
RA Mitsubuchi H., Yoneyama A., Ohta K., Eto K., Saito K., Kuhara T.,
RA van Kuilenburg A.B.;
RT "Clinical, biochemical and molecular analysis of 13 Japanese patients with
RT beta-ureidopropionase deficiency demonstrates high prevalence of the c.977G
RT > A (p.R326Q) mutation [corrected].";
RL J. Inherit. Metab. Dis. 37:801-812(2014).
CC -!- FUNCTION: Catalyzes a late step in pyrimidine degradation
CC (PubMed:22525402, PubMed:24526388). Converts N-carbamoyl-beta-alanine
CC (3-ureidopropanoate) into beta-alanine, ammonia and carbon dioxide
CC (PubMed:10542323, PubMed:11508704, PubMed:10415095, PubMed:29976570,
CC PubMed:22525402, PubMed:24526388). Likewise, converts N-carbamoyl-beta-
CC aminoisobutyrate (3-ureidoisobutyrate) into beta-aminoisobutyrate,
CC ammonia and carbon dioxide (Probable). {ECO:0000269|PubMed:10415095,
CC ECO:0000269|PubMed:10542323, ECO:0000269|PubMed:11508704,
CC ECO:0000269|PubMed:22525402, ECO:0000269|PubMed:24526388,
CC ECO:0000269|PubMed:29976570, ECO:0000305|PubMed:22525402,
CC ECO:0000305|PubMed:24526388}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(carbamoylamino)propanoate + 2 H(+) + H2O = beta-alanine +
CC CO2 + NH4(+); Xref=Rhea:RHEA:11184, ChEBI:CHEBI:11892,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57966; EC=3.5.1.6;
CC Evidence={ECO:0000269|PubMed:10415095, ECO:0000269|PubMed:10542323,
CC ECO:0000269|PubMed:11508704, ECO:0000269|PubMed:22525402,
CC ECO:0000269|PubMed:24526388, ECO:0000269|PubMed:29976570};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11185;
CC Evidence={ECO:0000269|PubMed:10415095, ECO:0000269|PubMed:10542323,
CC ECO:0000269|PubMed:11508704, ECO:0000269|PubMed:22525402,
CC ECO:0000269|PubMed:24526388, ECO:0000269|PubMed:29976570};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(carbamoylamino)-2-methylpropanoate + 2 H(+) + H2O = (R)-3-
CC amino-2-methylpropanoate + CO2 + NH4(+); Xref=Rhea:RHEA:37339,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57731, ChEBI:CHEBI:74414; EC=3.5.1.6;
CC Evidence={ECO:0000305|PubMed:22525402, ECO:0000305|PubMed:24526388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37340;
CC Evidence={ECO:0000305|PubMed:22525402, ECO:0000305|PubMed:24526388};
CC -!- ACTIVITY REGULATION: Strongly inhibited by 50 mM Zn(2+). Not inhibited
CC by EDTA. Competitively inhibited by beta-alanine, 5-aminolevulinic acid
CC (ALA), beta-aminoisobutyrate and 4-ureidobutyrate.
CC {ECO:0000269|PubMed:29976570}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.5 uM for N-carbamoyl-beta-alanine
CC {ECO:0000269|PubMed:10415095};
CC KM=48 uM for N-carbamoyl-beta-alanine {ECO:0000269|PubMed:29976570};
CC Note=kcat is 0.47 sec(-1) with N-carbamoyl-beta-alanine as substrate.
CC {ECO:0000269|PubMed:29976570};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:29976570};
CC -!- PATHWAY: Amino-acid biosynthesis; beta-alanine biosynthesis.
CC {ECO:0000269|PubMed:10415095, ECO:0000269|PubMed:10542323,
CC ECO:0000269|PubMed:11508704, ECO:0000269|PubMed:22525402,
CC ECO:0000269|PubMed:24526388, ECO:0000269|PubMed:29976570}.
CC -!- SUBUNIT: Homodimer, homotetramer, homooctamer; can also form higher
CC homooligomers. {ECO:0000269|PubMed:22525402,
CC ECO:0000269|PubMed:24526388, ECO:0000269|PubMed:29976570}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:22525402}.
CC -!- DISEASE: Beta-ureidopropionase deficiency (UPB1D) [MIM:613161]: An
CC inborn error of metabolism due to a defect in pyrimidine degradation.
CC It is characterized by muscular hypotonia, dystonic movements,
CC scoliosis, microcephaly and severe developmental delay. Patients show
CC strongly elevated levels of N-carbamyl-beta-alanine and N-carbamyl-
CC beta-aminoisobutyric acid in plasma, cerebrospinal fluid and urine.
CC {ECO:0000269|PubMed:15385443, ECO:0000269|PubMed:22525402,
CC ECO:0000269|PubMed:24526388}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. BUP
CC family. {ECO:0000305}.
CC -!- CAUTION: The purified enzyme was shown to contain 0.5 zinc atoms per
CC subunit, and sequence analysis was used to predict the zinc binding
CC site (PubMed:11508704). The crystal structure indicates a lack of bound
CC zinc ions, and shows that the residues that were predicted to bind zinc
CC are too far apart in space to form a zinc binding site
CC (PubMed:29976570). {ECO:0000269|PubMed:11508704,
CC ECO:0000269|PubMed:29976570}.
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DR EMBL; AF163312; AAF06735.1; -; mRNA.
DR EMBL; AF169559; AAF06739.1; -; Genomic_DNA.
DR EMBL; AF169550; AAF06739.1; JOINED; Genomic_DNA.
DR EMBL; AF169551; AAF06739.1; JOINED; Genomic_DNA.
DR EMBL; AF169552; AAF06739.1; JOINED; Genomic_DNA.
DR EMBL; AF169553; AAF06739.1; JOINED; Genomic_DNA.
DR EMBL; AF169554; AAF06739.1; JOINED; Genomic_DNA.
DR EMBL; AF169555; AAF06739.1; JOINED; Genomic_DNA.
DR EMBL; AF169556; AAF06739.1; JOINED; Genomic_DNA.
DR EMBL; AF169557; AAF06739.1; JOINED; Genomic_DNA.
DR EMBL; AF169558; AAF06739.1; JOINED; Genomic_DNA.
DR EMBL; AB013885; BAA88634.1; -; mRNA.
DR EMBL; CR456375; CAG30261.1; -; mRNA.
DR EMBL; CH471095; EAW59663.1; -; Genomic_DNA.
DR EMBL; BC131703; AAI31704.1; -; mRNA.
DR CCDS; CCDS13827.1; -.
DR RefSeq; NP_057411.1; NM_016327.2.
DR PDB; 6FTQ; X-ray; 2.08 A; A=1-384.
DR PDBsum; 6FTQ; -.
DR AlphaFoldDB; Q9UBR1; -.
DR SMR; Q9UBR1; -.
DR BioGRID; 119703; 1.
DR STRING; 9606.ENSP00000324343; -.
DR ChEMBL; CHEMBL3430874; -.
DR iPTMnet; Q9UBR1; -.
DR PhosphoSitePlus; Q9UBR1; -.
DR BioMuta; UPB1; -.
DR DMDM; 17373540; -.
DR MassIVE; Q9UBR1; -.
DR MaxQB; Q9UBR1; -.
DR PaxDb; Q9UBR1; -.
DR PeptideAtlas; Q9UBR1; -.
DR PRIDE; Q9UBR1; -.
DR ProteomicsDB; 84035; -.
DR Antibodypedia; 252; 93 antibodies from 24 providers.
DR DNASU; 51733; -.
DR Ensembl; ENST00000326010.10; ENSP00000324343.5; ENSG00000100024.15.
DR GeneID; 51733; -.
DR KEGG; hsa:51733; -.
DR MANE-Select; ENST00000326010.10; ENSP00000324343.5; NM_016327.3; NP_057411.1.
DR UCSC; uc003aaf.4; human.
DR CTD; 51733; -.
DR DisGeNET; 51733; -.
DR GeneCards; UPB1; -.
DR HGNC; HGNC:16297; UPB1.
DR HPA; ENSG00000100024; Tissue enriched (liver).
DR MalaCards; UPB1; -.
DR MIM; 606673; gene.
DR MIM; 613161; phenotype.
DR neXtProt; NX_Q9UBR1; -.
DR OpenTargets; ENSG00000100024; -.
DR Orphanet; 65287; Beta-ureidopropionase deficiency.
DR PharmGKB; PA418; -.
DR VEuPathDB; HostDB:ENSG00000100024; -.
DR eggNOG; KOG0808; Eukaryota.
DR GeneTree; ENSGT00390000004906; -.
DR HOGENOM; CLU_030130_4_1_1; -.
DR InParanoid; Q9UBR1; -.
DR OMA; AVKPNYS; -.
DR OrthoDB; 996578at2759; -.
DR PhylomeDB; Q9UBR1; -.
DR TreeFam; TF313402; -.
DR BioCyc; MetaCyc:HS01953-MON; -.
DR BRENDA; 3.5.1.6; 2681.
DR PathwayCommons; Q9UBR1; -.
DR Reactome; R-HSA-73621; Pyrimidine catabolism.
DR UniPathway; UPA00131; -.
DR BioGRID-ORCS; 51733; 9 hits in 1069 CRISPR screens.
DR ChiTaRS; UPB1; human.
DR GeneWiki; UPB1; -.
DR GenomeRNAi; 51733; -.
DR Pharos; Q9UBR1; Tbio.
DR PRO; PR:Q9UBR1; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9UBR1; protein.
DR Bgee; ENSG00000100024; Expressed in right lobe of liver and 164 other tissues.
DR ExpressionAtlas; Q9UBR1; baseline and differential.
DR Genevisible; Q9UBR1; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0003837; F:beta-ureidopropionase activity; IDA:UniProtKB.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0033396; P:beta-alanine biosynthetic process via 3-ureidopropionate; IDA:UniProtKB.
DR GO; GO:0006248; P:CMP catabolic process; IEA:Ensembl.
DR GO; GO:0006249; P:dCMP catabolic process; IEA:Ensembl.
DR GO; GO:0046079; P:dUMP catabolic process; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0046135; P:pyrimidine nucleoside catabolic process; IMP:UniProtKB.
DR GO; GO:0046050; P:UMP catabolic process; IEA:Ensembl.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disease variant; Hydrolase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..384
FT /note="Beta-ureidopropionase"
FT /id="PRO_0000204051"
FT DOMAIN 72..344
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 119
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 233
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054,
FT ECO:0000269|PubMed:29976570"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03248"
FT VARIANT 13
FT /note="L -> S (in UPB1D; strongly reduced activity; reduced
FT formation of higher oligomers; dbSNP:rs200688546)"
FT /evidence="ECO:0000269|PubMed:22525402,
FT ECO:0000269|PubMed:24526388"
FT /id="VAR_081207"
FT VARIANT 85
FT /note="A -> E (in UPB1D; complete loss of activity;
FT dbSNP:rs34035085)"
FT /evidence="ECO:0000269|PubMed:15385443"
FT /id="VAR_026752"
FT VARIANT 235
FT /note="G -> R (in UPB1D; complete loss of activity;
FT dbSNP:rs766196011)"
FT /evidence="ECO:0000269|PubMed:22525402"
FT /id="VAR_081208"
FT VARIANT 236
FT /note="R -> W (in UPB1D; complete loss of activity;
FT dbSNP:rs144135211)"
FT /evidence="ECO:0000269|PubMed:22525402"
FT /id="VAR_081209"
FT VARIANT 264
FT /note="S -> R (in UPB1D; complete loss of activity)"
FT /evidence="ECO:0000269|PubMed:22525402"
FT /id="VAR_081210"
FT VARIANT 271
FT /note="E -> K (in UPB1D; complete loss of activity;
FT abolishes formation of higher oligomers;
FT dbSNP:rs747454154)"
FT /evidence="ECO:0000269|PubMed:24526388"
FT /id="VAR_081211"
FT VARIANT 286
FT /note="I -> T (in UPB1D; unknown pathological significance;
FT mildly reduced enzyme activity; no effect on formation of
FT higher oligomers; dbSNP:rs200034079)"
FT /evidence="ECO:0000269|PubMed:24526388"
FT /id="VAR_081212"
FT VARIANT 326
FT /note="R -> Q (in UPB1D; complete loss of activity;
FT abolishes formation of higher oligomers;
FT dbSNP:rs118163237)"
FT /evidence="ECO:0000269|PubMed:22525402,
FT ECO:0000269|PubMed:24526388"
FT /id="VAR_081213"
FT VARIANT 340
FT /note="A -> D (in dbSNP:rs34110964)"
FT /id="VAR_050280"
FT VARIANT 359
FT /note="T -> M (in UPB1D; complete loss of activity;
FT dbSNP:rs369879221)"
FT /evidence="ECO:0000269|PubMed:22525402"
FT /id="VAR_081214"
FT MUTAGEN 130
FT /note="R->I: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29976570"
FT MUTAGEN 132
FT /note="K->L: Loss of catalytic activity. Forms dimers, but
FT no higher oligomers."
FT /evidence="ECO:0000269|PubMed:29976570"
FT MUTAGEN 208
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29976570"
FT MUTAGEN 208
FT /note="S->C: Loss of catalytic activity. Forms dimers, but
FT no higher oligomers."
FT /evidence="ECO:0000269|PubMed:29976570"
FT MUTAGEN 208
FT /note="S->R: Loss of catalytic activity. Forms dimers, but
FT no higher oligomers."
FT /evidence="ECO:0000269|PubMed:29976570"
FT MUTAGEN 233
FT /note="C->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29976570"
FT MUTAGEN 299
FT /note="T->C: Loss of catalytic activity. Forms dimers, but
FT no higher oligomers."
FT /evidence="ECO:0000269|PubMed:29976570"
FT CONFLICT 263
FT /note="L -> LRSL (in Ref. 1; AAF06739)"
FT /evidence="ECO:0000305"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:6FTQ"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:6FTQ"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:6FTQ"
FT HELIX 89..109
FT /evidence="ECO:0007829|PDB:6FTQ"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:6FTQ"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:6FTQ"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:6FTQ"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:6FTQ"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:6FTQ"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:6FTQ"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:6FTQ"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:6FTQ"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:6FTQ"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:6FTQ"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:6FTQ"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:6FTQ"
FT HELIX 239..247
FT /evidence="ECO:0007829|PDB:6FTQ"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:6FTQ"
FT HELIX 262..279
FT /evidence="ECO:0007829|PDB:6FTQ"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:6FTQ"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:6FTQ"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:6FTQ"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6FTQ"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:6FTQ"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:6FTQ"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:6FTQ"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:6FTQ"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:6FTQ"
FT HELIX 362..373
FT /evidence="ECO:0007829|PDB:6FTQ"
SQ SEQUENCE 384 AA; 43166 MW; 62B81982D2D63CC3 CRC64;
MAGAEWKSLE ECLEKHLPLP DLQEVKRVLY GKELRKLDLP REAFEAASRE DFELQGYAFE
AAEEQLRRPR IVHVGLVQNR IPLPANAPVA EQVSALHRRI KAIVEVAAMC GVNIICFQEA
WTMPFAFCTR EKLPWTEFAE SAEDGPTTRF CQKLAKNHDM VVVSPILERD SEHGDVLWNT
AVVISNSGAV LGKTRKNHIP RVGDFNESTY YMEGNLGHPV FQTQFGRIAV NICYGRHHPL
NWLMYSINGA EIIFNPSATI GALSESLWPI EARNAAIANH CFTCAINRVG TEHFPNEFTS
GDGKKAHQDF GYFYGSSYVA APDSSRTPGL SRSRDGLLVA KLDLNLCQQV NDVWNFKMTG
RYEMYARELA EAVKSNYSPT IVKE
