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 27-MAR-2024, entry version 173. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 9606-ENSP00000324343; -. DR PeptideAtlas; Q9UBR1; -. DR ProteomicsDB; 84035; -. DR Antibodypedia; 252; 102 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 AGR; HGNC:16297; -. 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; HWPFLRD; -. DR OrthoDB; 177430at2759; -. DR PhylomeDB; Q9UBR1; -. DR TreeFam; TF313402; -. DR BioCyc; MetaCyc:HS01953-MONOMER; -. DR BRENDA; 3.5.1.6; 2681. DR PathwayCommons; Q9UBR1; -. DR Reactome; R-HSA-73621; Pyrimidine catabolism. DR SABIO-RK; Q9UBR1; -. DR UniPathway; UPA00131; -. DR BioGRID-ORCS; 51733; 9 hits in 1149 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 165 other cell types or 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: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 CDD; cd07587; ML_beta-AS; 1. DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1. DR InterPro; IPR003010; C-N_Hydrolase. DR InterPro; IPR036526; C-N_Hydrolase_sf. DR PANTHER; PTHR43674:SF2; BETA-UREIDOPROPIONASE; 1. DR PANTHER; PTHR43674; NITRILASE C965.09-RELATED; 1. DR Pfam; PF00795; CN_hydrolase; 1. DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 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; uncertain significance; mildly FT reduced enzyme activity; no effect on formation of higher FT 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 //