ID ENO1_YEAST Reviewed; 437 AA. AC P00924; D6VV34; P99013; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 27-MAR-2024, entry version 240. DE RecName: Full=Enolase 1; DE EC=4.2.1.11; DE AltName: Full=2-phospho-D-glycerate hydro-lyase 1; DE AltName: Full=2-phosphoglycerate dehydratase 1; GN Name=ENO1; Synonyms=ENOA, HSP48; OrderedLocusNames=YGR254W; GN ORFNames=G9160; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6256394; DOI=10.1016/s0021-9258(19)69976-x; RA Holland M.J., Holland J.P., Thill G.P., Jackson K.A.; RT "The primary structures of two yeast enolase genes. Homology between the 5' RT noncoding flanking regions of yeast enolase and glyceraldehyde-3-phosphate RT dehydrogenase genes."; RL J. Biol. Chem. 256:1385-1395(1981). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9133741; RX DOI=10.1002/(sici)1097-0061(19970330)13:4<369::aid-yea81>3.0.co;2-v; RA Mazzoni C., Ruzzi M., Rinaldi T., Solinas F., Montebove F., Frontali L.; RT "Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome VII RT reveals the presence of three new open reading frames and of a tRNAThr RT gene."; RL Yeast 13:369-372(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP PROTEIN SEQUENCE OF 2-437. RX PubMed=7005235; DOI=10.1016/s0021-9258(19)69975-8; RA Chin C.C.Q., Brewer J.M., Wold F.; RT "The amino acid sequence of yeast enolase."; RL J. Biol. Chem. 256:1377-1384(1981). RN [6] RP PROTEIN SEQUENCE OF 2-12. RC STRAIN=ATCC 26786 / X2180-1A; RA Sanchez J.-C., Golaz O., Schaller D., Morch F., Frutiger S., Hughes G.J., RA Appel R.D., Deshusses J., Hochstrasser D.F.; RL Submitted (AUG-1995) to UniProtKB. RN [7] RP PROTEIN SEQUENCE OF 30-47. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7895733; DOI=10.1002/elps.11501501210; RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., RA Volpe T., Warner J.R., McLaughlin C.S.; RT "Protein identifications for a Saccharomyces cerevisiae protein database."; RL Electrophoresis 15:1466-1486(1994). RN [8] RP PROTEIN SEQUENCE OF 69-79. RC STRAIN=ATCC 38531 / Y41; RX PubMed=7737086; DOI=10.1002/elps.1150160124; RA Norbeck J., Blomberg A.; RT "Gene linkage of two-dimensional polyacrylamide gel electrophoresis RT resolved proteins from isogene families in Saccharomyces cerevisiae by RT microsequencing of in-gel trypsin generated peptides."; RL Electrophoresis 16:149-156(1995). RN [9] RP MUTAGENESIS OF LYS-346, AND ACTIVE SITE. RX PubMed=8634301; DOI=10.1021/bi952186y; RA Poyner R.R., Laughlin L.T., Sowa G.A., Reed G.H.; RT "Toward identification of acid/base catalysts in the active site of RT enolase: comparison of the properties of K345A, E168Q, and E211Q RT variants."; RL Biochemistry 35:1692-1699(1996). RN [10] RP MUTAGENESIS OF HIS-160. RX PubMed=11027610; DOI=10.1006/bbrc.2000.3618; RA Brewer J.M., Holland M.J., Lebioda L.; RT "The H159A mutant of yeast enolase 1 has significant activity."; RL Biochem. Biophys. Res. Commun. 276:1199-1202(2000). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=11502169; DOI=10.1021/bi010277r; RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., RA Schmitter J.-M.; RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular RT complex."; RL Biochemistry 40:9758-9769(2001). RN [12] RP MUTAGENESIS OF HIS-160 AND ASN-208. RX PubMed=13678299; DOI=10.1023/a:1025390123761; RA Brewer J.M., Glover C.V., Holland M.J., Lebioda L.; RT "Enzymatic function of loop movement in enolase: preparation and some RT properties of H159N, H159A, H159F, and N207A enolases."; RL J. Protein Chem. 22:353-361(2003). RN [13] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [15] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-358, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS). RX PubMed=3374614; DOI=10.1038/333683a0; RA Lebioda L., Stec B.; RT "Crystal structure of enolase indicates that enolase and pyruvate kinase RT evolved from a common ancestor."; RL Nature 333:683-686(1988). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS). RX PubMed=2645275; DOI=10.2210/pdb2enl/pdb; RA Lebioda L., Stec B., Brewer J.M.; RT "The structure of yeast enolase at 2.25-A resolution. An 8-fold beta + RT alpha-barrel with a novel beta beta alpha alpha (beta alpha)6 topology."; RL J. Biol. Chem. 264:3685-3693(1989). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS). RX PubMed=2405163; DOI=10.1016/0022-2836(90)90023-f; RA Stec B., Lebioda L.; RT "Refined structure of yeast apo-enolase at 2.25-A resolution."; RL J. Mol. Biol. 211:235-248(1990). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND RP MAGNESIUM IONS, AND COFACTOR. RX PubMed=8605183; DOI=10.1021/bi952859c; RA Larsen T.M., Wedekind J.E., Rayment I., Reed G.H.; RT "A carboxylate oxygen of the substrate bridges the magnesium ions at the RT active site of enolase: structure of the yeast enzyme complexed with the RT equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8-A RT resolution."; RL Biochemistry 35:4349-4358(1996). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE. RX PubMed=9376357; DOI=10.1021/bi9712450; RA Zhang E., Brewer J.M., Minor W., Carreira L.A., Lebioda L.; RT "Mechanism of enolase: the crystal structure of asymmetric dimer enolase-2- RT phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0-A resolution."; RL Biochemistry 36:12526-12534(1997). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-40 IN COMPLEX WITH RP MAGNESIUM IONS AND SUBSTRATE ANALOG. RX PubMed=12054465; DOI=10.1016/s0003-9861(02)00024-3; RA Poyner R.R., Larsen T.M., Wong S.-W., Reed G.H.; RT "Functional and structural changes due to a serine to alanine mutation in RT the active-site flap of enolase."; RL Arch. Biochem. Biophys. 401:155-163(2002). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT GLN-212 AND MUTANT GLN-169, RP MUTAGENESIS OF GLU-212 AND LYS-346, AND ACTIVE SITE. RX PubMed=12846578; DOI=10.1021/bi0346345; RA Sims P.A., Larsen T.M., Poyner R.R., Cleland W.W., Reed G.H.; RT "Reverse protonation is the key to general acid-base catalysis in RT enolase."; RL Biochemistry 42:8298-8306(2003). CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, CC ChEBI:CHEBI:58702; EC=4.2.1.11; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:8605183}; CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer. CC {ECO:0000269|PubMed:8605183}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 4/5. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12054465, CC ECO:0000269|PubMed:8605183, ECO:0000269|PubMed:9376357}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11502169}. CC -!- MISCELLANEOUS: Present with 76700 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}. 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; J01322; AAA88712.1; -; Genomic_DNA. DR EMBL; X99228; CAA67616.1; -; Genomic_DNA. DR EMBL; Z73039; CAA97283.1; -; Genomic_DNA. DR EMBL; BK006941; DAA08345.1; -; Genomic_DNA. DR PIR; S64586; NOBY. DR RefSeq; NP_011770.3; NM_001181383.3. DR PDB; 1EBG; X-ray; 2.10 A; A/B=2-437. DR PDB; 1EBH; X-ray; 1.90 A; A/B=2-437. DR PDB; 1ELS; X-ray; 2.40 A; A=2-437. DR PDB; 1L8P; X-ray; 2.10 A; A/B/C/D=2-437. DR PDB; 1NEL; X-ray; 2.60 A; A=2-437. DR PDB; 1ONE; X-ray; 1.80 A; A/B=2-437. DR PDB; 1P43; X-ray; 1.80 A; A/B=2-437. DR PDB; 1P48; X-ray; 2.00 A; A/B=2-437. DR PDB; 2AL1; X-ray; 1.50 A; A/B=2-437. DR PDB; 2AL2; X-ray; 1.85 A; A/B=2-437. DR PDB; 2ONE; X-ray; 2.00 A; A/B=2-437. DR PDB; 2XGZ; X-ray; 1.80 A; A/B=2-437. DR PDB; 2XH0; X-ray; 1.70 A; A/B/C/D=2-437. DR PDB; 2XH2; X-ray; 1.80 A; A/B/C/D=2-437. DR PDB; 2XH4; X-ray; 1.70 A; A/B/C/D=2-437. DR PDB; 2XH7; X-ray; 1.80 A; A/B=2-437. DR PDB; 3ENL; X-ray; 2.25 A; A=2-437. DR PDB; 4ENL; X-ray; 1.90 A; A=2-437. DR PDB; 5ENL; X-ray; 2.20 A; A=2-437. DR PDB; 6ENL; X-ray; 2.20 A; A=2-437. DR PDB; 7ENL; X-ray; 2.20 A; A=2-437. DR PDBsum; 1EBG; -. DR PDBsum; 1EBH; -. DR PDBsum; 1ELS; -. DR PDBsum; 1L8P; -. DR PDBsum; 1NEL; -. DR PDBsum; 1ONE; -. DR PDBsum; 1P43; -. DR PDBsum; 1P48; -. DR PDBsum; 2AL1; -. DR PDBsum; 2AL2; -. DR PDBsum; 2ONE; -. DR PDBsum; 2XGZ; -. DR PDBsum; 2XH0; -. DR PDBsum; 2XH2; -. DR PDBsum; 2XH4; -. DR PDBsum; 2XH7; -. DR PDBsum; 3ENL; -. DR PDBsum; 4ENL; -. DR PDBsum; 5ENL; -. DR PDBsum; 6ENL; -. DR PDBsum; 7ENL; -. DR AlphaFoldDB; P00924; -. DR SMR; P00924; -. DR BioGRID; 33505; 207. DR DIP; DIP-5561N; -. DR IntAct; P00924; 82. DR MINT; P00924; -. DR STRING; 4932.YGR254W; -. DR Allergome; 786; Sac c Enolase. DR MoonDB; P00924; Curated. DR MoonProt; P00924; -. DR CarbonylDB; P00924; -. DR iPTMnet; P00924; -. DR MetOSite; P00924; -. DR MaxQB; P00924; -. DR PaxDb; 4932-YGR254W; -. DR PeptideAtlas; P00924; -. DR TopDownProteomics; P00924; -. DR EnsemblFungi; YGR254W_mRNA; YGR254W; YGR254W. DR GeneID; 853169; -. DR KEGG; sce:YGR254W; -. DR AGR; SGD:S000003486; -. DR SGD; S000003486; ENO1. DR VEuPathDB; FungiDB:YGR254W; -. DR eggNOG; KOG2670; Eukaryota. DR GeneTree; ENSGT00950000182805; -. DR HOGENOM; CLU_031223_0_0_1; -. DR InParanoid; P00924; -. DR OMA; RCMMSHR; -. DR OrthoDB; 1093250at2759; -. DR BioCyc; YEAST:YGR254W-MONOMER; -. DR BRENDA; 4.2.1.11; 984. DR Reactome; R-SCE-70171; Glycolysis. DR Reactome; R-SCE-70263; Gluconeogenesis. DR SABIO-RK; P00924; -. DR UniPathway; UPA00109; UER00187. DR BioGRID-ORCS; 853169; 6 hits in 10 CRISPR screens. DR EvolutionaryTrace; P00924; -. DR PRO; PR:P00924; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; P00924; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005829; C:cytosol; HDA:SGD. DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; IDA:SGD. DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IDA:SGD. DR GO; GO:0005886; C:plasma membrane; HDA:SGD. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:1904408; F:melatonin binding; IDA:SGD. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IMP:SGD. DR GO; GO:0006096; P:glycolytic process; IMP:SGD. DR GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IDA:SGD. DR CDD; cd03313; enolase; 1. DR Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1. DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1. DR HAMAP; MF_00318; Enolase; 1. DR InterPro; IPR000941; Enolase. DR InterPro; IPR036849; Enolase-like_C_sf. DR InterPro; IPR029017; Enolase-like_N. DR InterPro; IPR020810; Enolase_C. DR InterPro; IPR020809; Enolase_CS. DR InterPro; IPR020811; Enolase_N. DR NCBIfam; TIGR01060; eno; 1. DR PANTHER; PTHR11902; ENOLASE; 1. DR PANTHER; PTHR11902:SF1; ENOLASE; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PIRSF; PIRSF001400; Enolase; 1. DR PRINTS; PR00148; ENOLASE. DR SFLD; SFLDS00001; Enolase; 1. DR SFLD; SFLDF00002; enolase; 1. DR SMART; SM01192; Enolase_C; 1. DR SMART; SM01193; Enolase_N; 1. DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1. DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1. DR PROSITE; PS00164; ENOLASE; 1. DR COMPLUYEAST-2DPAGE; P00924; -. DR SWISS-2DPAGE; P00924; -. DR UCD-2DPAGE; P00924; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Glycolysis; KW Isopeptide bond; Lyase; Magnesium; Metal-binding; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:7005235, ECO:0000269|Ref.6" FT CHAIN 2..437 FT /note="Enolase 1" FT /id="PRO_0000134062" FT ACT_SITE 212 FT /note="Proton donor" FT /evidence="ECO:0000269|PubMed:12846578" FT ACT_SITE 346 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:12846578, FT ECO:0000269|PubMed:8634301" FT BINDING 160 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:8605183, FT ECO:0000269|PubMed:9376357" FT BINDING 169 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:8605183, FT ECO:0000269|PubMed:9376357" FT BINDING 247 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:8605183" FT BINDING 296 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:8605183" FT BINDING 296 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:8605183, FT ECO:0000269|PubMed:9376357" FT BINDING 321 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:8605183" FT BINDING 321 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:8605183, FT ECO:0000269|PubMed:9376357" FT BINDING 373..376 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12054465, FT ECO:0000269|PubMed:8605183, ECO:0000269|PubMed:9376357" FT BINDING 397 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:8605183, FT ECO:0000269|PubMed:9376357" FT MOD_RES 119 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358" FT MOD_RES 138 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00925" FT MOD_RES 188 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00925" FT MOD_RES 313 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P00925" FT MOD_RES 324 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P00925" FT CROSSLNK 60 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P00925" FT CROSSLNK 243 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P00925" FT CROSSLNK 358 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT MUTAGEN 40 FT /note="S->A: Reduces activity by 99.9%." FT MUTAGEN 160 FT /note="H->A,F,N: Reduces activity by 99%." FT /evidence="ECO:0000269|PubMed:11027610, FT ECO:0000269|PubMed:13678299" FT MUTAGEN 169 FT /note="E->Q: Reduces kcat over 100000-fold." FT MUTAGEN 208 FT /note="N->A: Reduces activity by 44%." FT /evidence="ECO:0000269|PubMed:13678299" FT MUTAGEN 212 FT /note="E->Q: Reduces kcat over 100000-fold." FT /evidence="ECO:0000269|PubMed:12846578" FT MUTAGEN 346 FT /note="K->A: Reduces kcat over 100000-fold. Abolishes of FT the proton exchange reaction that initiates the enzymatic FT reaction." FT /evidence="ECO:0000269|PubMed:12846578, FT ECO:0000269|PubMed:8634301" FT CONFLICT 242 FT /note="I -> V (in Ref. 1; AAA88712)" FT /evidence="ECO:0000305" FT STRAND 5..12 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 18..26 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 29..34 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:1EBH" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 63..71 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 73..80 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 87..98 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 100..102 FT /evidence="ECO:0007829|PDB:1EBH" FT TURN 104..106 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 108..125 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 130..138 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 152..156 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 158..160 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 161..164 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 169..173 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 180..202 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 204..207 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 213..215 FT /evidence="ECO:0007829|PDB:1P48" FT HELIX 222..236 FT /evidence="ECO:0007829|PDB:2AL1" FT TURN 239..241 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 243..247 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 250..253 FT /evidence="ECO:0007829|PDB:2AL1" FT TURN 261..264 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 270..272 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 276..289 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 292..296 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 304..311 FT /evidence="ECO:0007829|PDB:2AL1" FT TURN 312..314 FT /evidence="ECO:0007829|PDB:2AL2" FT STRAND 316..321 FT /evidence="ECO:0007829|PDB:2AL1" FT TURN 322..326 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 328..336 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 341..345 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 347..350 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 353..365 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 369..373 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 383..390 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 394..397 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 404..420 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 421..423 FT /evidence="ECO:0007829|PDB:2AL1" FT STRAND 424..426 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 428..430 FT /evidence="ECO:0007829|PDB:2AL1" FT HELIX 434..436 FT /evidence="ECO:0007829|PDB:2AL1" SQ SEQUENCE 437 AA; 46816 MW; 69F45214DBD375BE CRC64; MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGVHEALEMR DGDKSKWMGK GVLHAVKNVN DVIAPAFVKA NIDVKDQKAV DDFLISLDGT ANKSKLGANA ILGVSLAASR AAAAEKNVPL YKHLADLSKS KTSPYVLPVP FLNVLNGGSH AGGALALQEF MIAPTGAKTF AEALRIGSEV YHNLKSLTKK RYGASAGNVG DEGGVAPNIQ TAEEALDLIV DAIKAAGHDG KIKIGLDCAS SEFFKDGKYD LDFKNPNSDK SKWLTGPQLA DLYHSLMKRY PIVSIEDPFA EDDWEAWSHF FKTAGIQIVA DDLTVTNPKR IATAIEKKAA DALLLKVNQI GTLSESIKAA QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA PARSERLAKL NQLLRIEEEL GDNAVFAGEN FHHGDKL //