HMCS2_MOUSE
ID HMCS2_MOUSE Reviewed; 508 AA.
AC P54869; Q64740; Q9DBK1; Q9DBM4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Hydroxymethylglutaryl-CoA synthase, mitochondrial;
DE Short=HMG-CoA synthase;
DE EC=2.3.3.10 {ECO:0000269|PubMed:24315375};
DE AltName: Full=3-hydroxy-3-methylglutaryl coenzyme A synthase;
DE Flags: Precursor;
GN Name=Hmgcs2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-508.
RC STRAIN=CHS; TISSUE=Liver;
RX PubMed=7851882; DOI=10.1006/geno.1994.1542;
RA Boukaftane Y., Duncan A., Wang S., Labuda D., Robert M.-F., Sarrazin J.,
RA Schappert K.T., Mitchell G.A.;
RT "Human mitochondrial HMG CoA synthase: liver cDNA and partial genomic
RT cloning, chromosome mapping to 1p12-p13, and possible role in vertebrate
RT evolution.";
RL Genomics 23:552-559(1994).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, SUCCINYLATION AT LYS-83; LYS-310; LYS-354 AND LYS-358,
RP MUTAGENESIS OF LYS-83 AND LYS-310, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CATALYTIC ACTIVITY.
RX PubMed=24315375; DOI=10.1016/j.cmet.2013.11.013;
RA Rardin M.J., He W., Nishida Y., Newman J.C., Carrico C., Danielson S.R.,
RA Guo A., Gut P., Sahu A.K., Li B., Uppala R., Fitch M., Riiff T., Zhu L.,
RA Zhou J., Mulhern D., Stevens R.D., Ilkayeva O.R., Newgard C.B.,
RA Jacobson M.P., Hellerstein M., Goetzman E.S., Gibson B.W., Verdin E.;
RT "SIRT5 regulates the mitochondrial lysine succinylome and metabolic
RT networks.";
RL Cell Metab. 18:920-933(2013).
RN [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-52; LYS-83; LYS-118; LYS-221;
RP LYS-256; LYS-310; LYS-327; LYS-333; LYS-342; LYS-350; LYS-354; LYS-358;
RP LYS-447 AND LYS-473, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83; LYS-118; LYS-243; LYS-256;
RP LYS-306; LYS-310; LYS-327; LYS-342; LYS-350; LYS-354; LYS-358; LYS-427;
RP LYS-437; LYS-447 AND LYS-473, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Catalyzes the first irreversible step in ketogenesis,
CC condensing acetyl-CoA to acetoacetyl-CoA to form HMG-CoA, which is
CC converted by HMG-CoA reductase (HMGCR) into mevalonate.
CC {ECO:0000269|PubMed:24315375}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-
CC methylglutaryl-CoA + CoA + H(+); Xref=Rhea:RHEA:10188,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.10;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10116,
CC ECO:0000269|PubMed:24315375};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10189;
CC Evidence={ECO:0000305|PubMed:24315375};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=460 uM for acetyl-CoA {ECO:0000269|PubMed:24315375};
CC Vmax=59 nmol/min/mg enzyme with acetyl-CoA as a substrate
CC {ECO:0000269|PubMed:24315375};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P54868}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P22791}.
CC -!- TISSUE SPECIFICITY: Liver and kidney.
CC -!- PTM: Acetylation of Lys-427 is observed in liver mitochondria from
CC fasted mice but not from fed mice.
CC -!- PTM: Succinylated. Desuccinylated by SIRT5. Succinylation, at least at
CC Lys-83 and Lys-310, inhibits the enzymatic activity.
CC {ECO:0000269|PubMed:24315375}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC family. {ECO:0000305}.
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DR EMBL; AK004865; BAB23626.1; -; mRNA.
DR EMBL; AK004902; BAB23657.1; -; mRNA.
DR EMBL; BC014714; AAH14714.1; -; mRNA.
DR EMBL; BC024744; AAH24744.1; -; mRNA.
DR EMBL; U12790; AAA92675.1; -; Genomic_DNA.
DR EMBL; U12791; AAA92676.1; -; Genomic_DNA.
DR CCDS; CCDS17662.1; -.
DR PIR; B55729; B55729.
DR RefSeq; NP_032282.2; NM_008256.4.
DR AlphaFoldDB; P54869; -.
DR SMR; P54869; -.
DR BioGRID; 200339; 1.
DR STRING; 10090.ENSMUSP00000088249; -.
DR iPTMnet; P54869; -.
DR PhosphoSitePlus; P54869; -.
DR SwissPalm; P54869; -.
DR REPRODUCTION-2DPAGE; P54869; -.
DR SWISS-2DPAGE; P54869; -.
DR jPOST; P54869; -.
DR MaxQB; P54869; -.
DR PaxDb; P54869; -.
DR PeptideAtlas; P54869; -.
DR PRIDE; P54869; -.
DR ProteomicsDB; 273365; -.
DR Antibodypedia; 33918; 204 antibodies from 26 providers.
DR DNASU; 15360; -.
DR Ensembl; ENSMUST00000090746; ENSMUSP00000088249; ENSMUSG00000027875.
DR Ensembl; ENSMUST00000120541; ENSMUSP00000113296; ENSMUSG00000027875.
DR GeneID; 15360; -.
DR KEGG; mmu:15360; -.
DR UCSC; uc008qpr.2; mouse.
DR CTD; 3158; -.
DR MGI; MGI:101939; Hmgcs2.
DR VEuPathDB; HostDB:ENSMUSG00000027875; -.
DR eggNOG; KOG1393; Eukaryota.
DR GeneTree; ENSGT00390000006096; -.
DR HOGENOM; CLU_008065_0_1_1; -.
DR InParanoid; P54869; -.
DR OMA; YFAFHAP; -.
DR OrthoDB; 495111at2759; -.
DR PhylomeDB; P54869; -.
DR TreeFam; TF105361; -.
DR BRENDA; 2.3.3.10; 3474.
DR Reactome; R-MMU-77111; Synthesis of Ketone Bodies.
DR SABIO-RK; P54869; -.
DR UniPathway; UPA00058; UER00102.
DR BioGRID-ORCS; 15360; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Hmgcs2; mouse.
DR PRO; PR:P54869; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P54869; protein.
DR Bgee; ENSMUSG00000027875; Expressed in right colon and 194 other tissues.
DR Genevisible; P54869; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0004421; F:hydroxymethylglutaryl-CoA synthase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; ISO:MGI.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
DR GO; GO:0046951; P:ketone body biosynthetic process; ISO:MGI.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0007494; P:midgut development; IEA:Ensembl.
DR GO; GO:0033555; P:multicellular organismal response to stress; IEA:Ensembl.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0033762; P:response to glucagon; IEA:Ensembl.
DR GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
DR GO; GO:0070543; P:response to linoleic acid; IEA:Ensembl.
DR GO; GO:0010038; P:response to metal ion; IEA:Ensembl.
DR GO; GO:0034284; P:response to monosaccharide; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0034696; P:response to prostaglandin F; IEA:Ensembl.
DR GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR GO; GO:0009266; P:response to temperature stimulus; IEA:Ensembl.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0034014; P:response to triglyceride; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR000590; HMG_CoA_synt_AS.
DR InterPro; IPR013746; HMG_CoA_synt_C_dom.
DR InterPro; IPR013528; HMG_CoA_synth_N.
DR InterPro; IPR010122; HMG_CoA_synthase_euk.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF08540; HMG_CoA_synt_C; 1.
DR Pfam; PF01154; HMG_CoA_synt_N; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01833; HMG-CoA-S_euk; 1.
DR PROSITE; PS01226; HMG_COA_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cholesterol biosynthesis; Cholesterol metabolism;
KW Lipid biosynthesis; Lipid metabolism; Mitochondrion; Phosphoprotein;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transferase; Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN 38..508
FT /note="Hydroxymethylglutaryl-CoA synthase, mitochondrial"
FT /id="PRO_0000013484"
FT ACT_SITE 132
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
FT ACT_SITE 166
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
FT ACT_SITE 301
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54868"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54868"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54868"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P54868"
FT MOD_RES 52
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 83
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 83
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24315375,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 118
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 118
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 221
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 243
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 256
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 256
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 306
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 310
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 310
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24315375,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 327
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 327
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 333
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 342
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 342
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 350
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 350
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 354
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 354
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24315375,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 358
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 358
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24315375,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 427
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939"
FT MOD_RES 437
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54868"
FT MOD_RES 447
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 447
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 473
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 473
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22791"
FT MUTAGEN 83
FT /note="K->E: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24315375"
FT MUTAGEN 310
FT /note="K->E: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24315375"
FT CONFLICT 29..31
FT /note="LSA -> EFR (in Ref. 3; AAA92675)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="L -> I (in Ref. 1; BAB23657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 56823 MW; 5A20ACE918FF4758 CRC64;
MQRLLAPARR VLQVKRAMQE TSLTPAHLLS AAQQRFSTIP PAPLAKTDTW PKDVGILALE
VYFPAQYVDQ TDLEKFNNVE AGKYTVGLGQ TRMGFCSVQE DINSLCLTVV QRLMERTKLP
WDAVGRLEVG TETIIDKSKA VKTVLMELFQ DSGNTDIEGI DTTNACYGGT ASLFNAANWM
ESSYWDGRYA LVVCGDIAVY PSGNARPTGG AGAVAMLIGP KAPLVLEQGL RGTHMENAYD
FYKPNLASEY PLVDGKLSIQ CYLRALDRCY AAYRKKIQNQ WKQAGNNQPF TLDDVQYMIF
HTPFCKMVQK SLARLMFNDF LSSSSDKQNN LYKGLEAFRG LKLEETYTNK DVDKALLKAS
LDMFNQKTKA SLYLSTNNGN MYTSSLYGCL ASLLSHHSAQ ELAGSRIGAF SYGSGLAASF
FSFRVSKDAS PGSPLEKLVS SVSDLPKRLD SRRRMSPEEF TEIMNQREQF YHKVNFSPPG
DTSNLFPGTW YLERVDEMHR RKYARCPV
