AASS_HUMAN
ID AASS_HUMAN Reviewed; 926 AA.
AC Q9UDR5; O95462;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Alpha-aminoadipic semialdehyde synthase, mitochondrial {ECO:0000305|PubMed:10775527, ECO:0000305|PubMed:463877};
DE AltName: Full=LKR/SDH {ECO:0000305|PubMed:10775527};
DE Includes:
DE RecName: Full=Lysine ketoglutarate reductase {ECO:0000305|PubMed:10775527};
DE Short=LKR {ECO:0000303|PubMed:10775527};
DE Short=LOR;
DE EC=1.5.1.8 {ECO:0000269|PubMed:10775527, ECO:0000269|PubMed:463877};
DE Includes:
DE RecName: Full=Saccharopine dehydrogenase {ECO:0000305|PubMed:10775527};
DE Short=SDH {ECO:0000303|PubMed:10775527};
DE EC=1.5.1.9 {ECO:0000269|PubMed:10775527, ECO:0000269|PubMed:463877};
DE Flags: Precursor;
GN Name=AASS {ECO:0000312|HGNC:HGNC:17366};
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], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP INVOLVEMENT IN HYPLYS1, DOMAIN, AND REGION.
RX PubMed=10775527; DOI=10.1086/302919;
RA Sacksteder K.A., Biery B.J., Morrell J.C., Goodman B.K., Geisbrecht B.V.,
RA Cox R.P., Gould S.J., Geraghty M.T.;
RT "Identification of the alpha-aminoadipic semialdehyde synthase gene, which
RT is defective in familial hyperlysinemia.";
RL Am. J. Hum. Genet. 66:1736-1743(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Papes F., Kemper E.L., Cord-Neto G., Langone F., Arruda P.;
RT "Cloning and expression analysis of the LKR/SDH gene in human tissues.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INVOLVEMENT IN
RP HYPLYS1.
RX PubMed=463877;
RA Dancis J., Hutzler J., Cox R.P.;
RT "Familial hyperlysinemia: enzyme studies, diagnostic methods, comments on
RT terminology.";
RL Am. J. Hum. Genet. 31:290-299(1979).
RN [5]
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 [6]
RP INVOLVEMENT IN DECRD.
RX PubMed=24847004; DOI=10.1093/hmg/ddu218;
RA Houten S.M., Denis S., Te Brinke H., Jongejan A., van Kampen A.H.,
RA Bradley E.J., Baas F., Hennekam R.C., Millington D.S., Young S.P.,
RA Frazier D.M., Gucsavas-Calikoglu M., Wanders R.J.;
RT "Mitochondrial NADP(H) deficiency due to a mutation in NADK2 causes
RT dienoyl-CoA reductase deficiency with hyperlysinemia.";
RL Hum. Mol. Genet. 23:5009-5016(2014).
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] {ECO:0007744|PDB:5L78}
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 455-926 IN COMPLEX WITH NAD.
RA Kopec J., Yue W.W.;
RT "Crystal structure of human aminoadipate semialdehyde synthase,
RT saccharopine dehydrogenase domain (in NAD+ bound form).";
RL Submitted (JUN-2016) to the PDB data bank.
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the first two steps in
CC lysine degradation. {ECO:0000269|PubMed:10775527,
CC ECO:0000269|PubMed:463877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-saccharopine + NADP(+) = 2-oxoglutarate + H(+) + L-
CC lysine + NADPH; Xref=Rhea:RHEA:19373, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57951, ChEBI:CHEBI:58349; EC=1.5.1.8;
CC Evidence={ECO:0000269|PubMed:10775527, ECO:0000269|PubMed:463877};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19375;
CC Evidence={ECO:0000269|PubMed:10775527};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-saccharopine + NAD(+) = (S)-2-amino-6-oxohexanoate +
CC H(+) + L-glutamate + NADH; Xref=Rhea:RHEA:24520, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:57951, ChEBI:CHEBI:58321; EC=1.5.1.9;
CC Evidence={ECO:0000269|PubMed:10775527, ECO:0000269|PubMed:463877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24521;
CC Evidence={ECO:0000269|PubMed:10775527};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 1/6.
CC {ECO:0000269|PubMed:10775527}.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 2/6.
CC {ECO:0000269|PubMed:10775527}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q99K67}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:463877}.
CC -!- TISSUE SPECIFICITY: Expressed in all 16 tissues examined with highest
CC expression in the liver.
CC -!- INDUCTION: Induced by starvation. {ECO:0000250}.
CC -!- DOMAIN: The N-terminal and the C-terminal domains contain respectively
CC the lysine ketoglutarate reductase and saccharopine dehydrogenase
CC activity. {ECO:0000303|PubMed:10775527}.
CC -!- DISEASE: Hyperlysinemia, 1 (HYPLYS1) [MIM:238700]: An autosomal
CC recessive metabolic condition with variable clinical features. Some
CC patients present with non-specific seizures, hypotonia, or mildly
CC delayed psychomotor development, and increased serum lysine and
CC pipecolic acid on laboratory analysis. However, about half of the
CC probands are reported to be asymptomatic, and hyperlysinemia is
CC generally considered to be a benign metabolic variant.
CC {ECO:0000269|PubMed:10775527}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. In hyperlysinemia 1, both
CC enzymatic functions of AASS are defective and patients have increased
CC serum lysine and possibly increased saccharopine. Some individuals,
CC however, retain significant amounts of lysine-ketoglutarate reductase
CC and present with saccharopinuria, a metabolic condition with few, if
CC any, clinical manifestations. {ECO:0000305|PubMed:463877}.
CC -!- DISEASE: 2,4-dienoyl-CoA reductase deficiency (DECRD) [MIM:616034]: A
CC rare, autosomal recessive, inborn error of polyunsaturated fatty acids
CC and lysine metabolism, resulting in mitochondrial dysfunction. Affected
CC individuals have a severe encephalopathy with neurologic and metabolic
CC abnormalities beginning in early infancy. Laboratory studies show
CC increased C10:2 carnitine levels and hyperlysinemia.
CC {ECO:0000269|PubMed:24847004}. Note=The protein represented in this
CC entry is involved in disease pathogenesis. A selective decrease in
CC mitochondrial NADP(H) levels due to NADK2 mutations causes a deficiency
CC of NADPH-dependent mitochondrial enzymes, such as DECR1 and AASS.
CC {ECO:0000269|PubMed:24847004}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AF229180; AAF44328.1; -; mRNA.
DR EMBL; AJ007714; CAA07619.2; -; mRNA.
DR EMBL; AC006020; AAF03526.1; -; Genomic_DNA.
DR CCDS; CCDS5783.1; -.
DR RefSeq; NP_005754.2; NM_005763.3.
DR PDB; 5L76; X-ray; 2.57 A; A=455-926.
DR PDB; 5L78; X-ray; 2.68 A; A/B=455-926.
DR PDB; 5O1N; X-ray; 2.28 A; A=455-926.
DR PDB; 5O1O; X-ray; 2.48 A; A/B=455-926.
DR PDB; 5O1P; X-ray; 1.90 A; A=455-926.
DR PDBsum; 5L76; -.
DR PDBsum; 5L78; -.
DR PDBsum; 5O1N; -.
DR PDBsum; 5O1O; -.
DR PDBsum; 5O1P; -.
DR AlphaFoldDB; Q9UDR5; -.
DR SMR; Q9UDR5; -.
DR BioGRID; 115459; 54.
DR IntAct; Q9UDR5; 11.
DR MINT; Q9UDR5; -.
DR STRING; 9606.ENSP00000377040; -.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB04207; L-Saccharopine.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB02338; NADPH.
DR CarbonylDB; Q9UDR5; -.
DR iPTMnet; Q9UDR5; -.
DR MetOSite; Q9UDR5; -.
DR PhosphoSitePlus; Q9UDR5; -.
DR BioMuta; AASS; -.
DR DMDM; 46396032; -.
DR EPD; Q9UDR5; -.
DR jPOST; Q9UDR5; -.
DR MassIVE; Q9UDR5; -.
DR MaxQB; Q9UDR5; -.
DR PaxDb; Q9UDR5; -.
DR PeptideAtlas; Q9UDR5; -.
DR PRIDE; Q9UDR5; -.
DR ProteomicsDB; 84114; -.
DR ABCD; Q9UDR5; 1 sequenced antibody.
DR Antibodypedia; 17598; 203 antibodies from 25 providers.
DR DNASU; 10157; -.
DR Ensembl; ENST00000393376.5; ENSP00000377040.1; ENSG00000008311.16.
DR Ensembl; ENST00000417368.7; ENSP00000403768.2; ENSG00000008311.16.
DR Ensembl; ENST00000679511.1; ENSP00000505381.1; ENSG00000008311.16.
DR Ensembl; ENST00000679864.1; ENSP00000505958.1; ENSG00000008311.16.
DR GeneID; 10157; -.
DR KEGG; hsa:10157; -.
DR MANE-Select; ENST00000417368.7; ENSP00000403768.2; NM_005763.4; NP_005754.2.
DR UCSC; uc003vka.4; human.
DR CTD; 10157; -.
DR DisGeNET; 10157; -.
DR GeneCards; AASS; -.
DR HGNC; HGNC:17366; AASS.
DR HPA; ENSG00000008311; Tissue enhanced (liver).
DR MalaCards; AASS; -.
DR MIM; 238700; phenotype.
DR MIM; 605113; gene.
DR MIM; 616034; phenotype.
DR neXtProt; NX_Q9UDR5; -.
DR OpenTargets; ENSG00000008311; -.
DR Orphanet; 2203; Hyperlysinemia.
DR Orphanet; 3124; Saccharopinuria.
DR PharmGKB; PA24369; -.
DR VEuPathDB; HostDB:ENSG00000008311; -.
DR eggNOG; KOG0172; Eukaryota.
DR GeneTree; ENSGT00390000013249; -.
DR HOGENOM; CLU_005231_0_1_1; -.
DR InParanoid; Q9UDR5; -.
DR OMA; KMEGRSE; -.
DR OrthoDB; 498994at2759; -.
DR PhylomeDB; Q9UDR5; -.
DR TreeFam; TF105728; -.
DR BioCyc; MetaCyc:HS00244-MON; -.
DR PathwayCommons; Q9UDR5; -.
DR Reactome; R-HSA-71064; Lysine catabolism.
DR SABIO-RK; Q9UDR5; -.
DR SignaLink; Q9UDR5; -.
DR UniPathway; UPA00868; UER00835.
DR UniPathway; UPA00868; UER00836.
DR BioGRID-ORCS; 10157; 15 hits in 1079 CRISPR screens.
DR ChiTaRS; AASS; human.
DR GeneWiki; AASS; -.
DR GenomeRNAi; 10157; -.
DR Pharos; Q9UDR5; Tbio.
DR PRO; PR:Q9UDR5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UDR5; protein.
DR Bgee; ENSG00000008311; Expressed in mucosa of stomach and 175 other tissues.
DR ExpressionAtlas; Q9UDR5; baseline and differential.
DR Genevisible; Q9UDR5; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:FlyBase.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR GO; GO:0042393; F:histone binding; ISS:FlyBase.
DR GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IMP:UniProtKB.
DR GO; GO:0004754; F:saccharopine dehydrogenase (NAD+, L-lysine-forming) activity; ISS:FlyBase.
DR GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IMP:UniProtKB.
DR GO; GO:0004753; F:saccharopine dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:FlyBase.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
DR GO; GO:0006554; P:lysine catabolic process; IMP:UniProtKB.
DR GO; GO:0031061; P:negative regulation of histone methylation; ISS:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:FlyBase.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032095; Sacchrp_dh-like_C.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF16653; Sacchrp_dh_C; 1.
DR Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Mitochondrion; Multifunctional enzyme; NAD;
KW NADP; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT CHAIN 28..926
FT /note="Alpha-aminoadipic semialdehyde synthase,
FT mitochondrial"
FT /id="PRO_0000001052"
FT REGION 28..476
FT /note="Lysine-ketoglutarate reductase"
FT /evidence="ECO:0000303|PubMed:10775527"
FT REGION 477..926
FT /note="Saccharopine dehydrogenase"
FT /evidence="ECO:0000303|PubMed:10775527"
FT BINDING 488
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:5L78"
FT BINDING 512
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:5L78"
FT BINDING 516
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:5L78"
FT BINDING 533
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:5L78"
FT BINDING 554
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:5L78"
FT BINDING 576
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:5L78"
FT BINDING 577..578
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT BINDING 577
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:5L78"
FT BINDING 603
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:5L78"
FT BINDING 604
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT BINDING 604
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:5L78"
FT BINDING 605
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:5L78"
FT BINDING 703
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT BINDING 724..726
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 93
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 93
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 138
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 138
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 274
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 286
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 286
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 333
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 458
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 458
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 523
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 523
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 535
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 535
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 584
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 584
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 707
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 732
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 739
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 761
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 761
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 780
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT CONFLICT 589
FT /note="S -> C (in Ref. 2; CAA07619)"
FT /evidence="ECO:0000305"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 492..499
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 507..512
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 514..523
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 527..530
FT /evidence="ECO:0007829|PDB:5O1P"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 537..545
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 559..569
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 572..577
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 581..584
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 587..593
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:5O1P"
FT TURN 603..606
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 607..620
FT /evidence="ECO:0007829|PDB:5O1P"
FT TURN 621..623
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 625..637
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 639..641
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 650..652
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 655..660
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 665..669
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 672..676
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 679..685
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 687..689
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 697..701
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 703..705
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 708..712
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 718..727
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 730..740
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 760..768
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 775..785
FT /evidence="ECO:0007829|PDB:5O1P"
FT TURN 787..789
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 791..800
FT /evidence="ECO:0007829|PDB:5O1P"
FT TURN 801..803
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 814..825
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 834..845
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 851..861
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 864..866
FT /evidence="ECO:0007829|PDB:5L76"
FT HELIX 869..886
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 894..896
FT /evidence="ECO:0007829|PDB:5O1P"
FT HELIX 901..910
FT /evidence="ECO:0007829|PDB:5O1P"
FT TURN 911..915
FT /evidence="ECO:0007829|PDB:5O1P"
FT STRAND 917..924
FT /evidence="ECO:0007829|PDB:5O1P"
SQ SEQUENCE 926 AA; 102132 MW; CB4194014351A18D CRC64;
MLQVHRTGLG RLGVSLSKGL HHKAVLAVRR EDVNAWERRA PLAPKHIKGI TNLGYKVLIQ
PSNRRAIHDK DYVKAGGILQ EDISEACLIL GVKRPPEEKL MSRKTYAFFS HTIKAQEANM
GLLDEILKQE IRLIDYEKMV DHRGVRVVAF GQWAGVAGMI NILHGMGLRL LALGHHTPFM
HIGMAHNYRN SSQAVQAVRD AGYEISLGLM PKSIGPLTFV FTGTGNVSKG AQAIFNELPC
EYVEPHELKE VSQTGDLRKV YGTVLSRHHH LVRKTDAVYD PAEYDKHPER YISRFNTDIA
PYTTCLINGI YWEQNTPRLL TRQDAQSLLA PGKFSPAGVE GCPALPHKLV AICDISADTG
GSIEFMTECT TIEHPFCMYD ADQHIIHDSV EGSGILMCSI DNLPAQLPIE ATECFGDMLY
PYVEEMILSD ATQPLESQNF SPVVRDAVIT SNGTLPDKYK YIQTLRESRE RAQSLSMGTR
RKVLVLGSGY ISEPVLEYLS RDGNIEITVG SDMKNQIEQL GKKYNINPVS MDICKQEEKL
GFLVAKQDLV ISLLPYVLHP LVAKACITNK VNMVTASYIT PALKELEKSV EDAGITIIGE
LGLDPGLDHM LAMETIDKAK EVGATIESYI SYCGGLPAPE HSNNPLRYKF SWSPVGVLMN
VMQSATYLLD GKVVNVAGGI SFLDAVTSMD FFPGLNLEGY PNRDSTKYAE IYGISSAHTL
LRGTLRYKGY MKALNGFVKL GLINREALPA FRPEANPLTW KQLLCDLVGI SPSSEHDVLK
EAVLKKLGGD NTQLEAAEWL GLLGDEQVPQ AESILDALSK HLVMKLSYGP EEKDMIVMRD
SFGIRHPSGH LEHKTIDLVA YGDINGFSAM AKTVGLPTAM AAKMLLDGEI GAKGLMGPFS
KEIYGPILER IKAEGIIYTT QSTIKP
