GenomeNet

Database: UniProt
Entry: O08749
LinkDB: O08749
Original site: O08749 
ID   DLDH_MOUSE              Reviewed;         509 AA.
AC   O08749; Q3TG55; Q3U5W5; Q3UWP7; Q99LD3;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   15-MAR-2017, entry version 154.
DE   RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial;
DE            EC=1.8.1.4 {ECO:0000250|UniProtKB:P09622};
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   Flags: Precursor;
GN   Name=Dld;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=DBA/2J;
RX   PubMed=9169128; DOI=10.1006/geno.1997.4670;
RA   Johnson M., Yang H.S., Johanning G.L., Patel M.S.;
RT   "Characterization of the mouse dihydrolipoamide dehydrogenase (Dld)
RT   gene: genomic structure, promoter sequence, and chromosomal
RT   localization.";
RL   Genomics 41:320-326(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Heart;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 73-89; 216-259; 289-334; 316-334; 347-365; 421-428
RP   AND 483-509, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15888450; DOI=10.1074/jbc.M500310200;
RA   Mitra K., Rangaraj N., Shivaji S.;
RT   "Novelty of the pyruvate metabolic enzyme dihydrolipoamide
RT   dehydrogenase in spermatozoa: correlation of its localization,
RT   tyrosine phosphorylation, and activity during sperm capacitation.";
RL   J. Biol. Chem. 280:25743-25753(2005).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17404228; DOI=10.1073/pnas.0610618104;
RA   Babady N.E., Pang Y.P., Elpeleg O., Isaya G.;
RT   "Cryptic proteolytic activity of dihydrolipoamide dehydrogenase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:6158-6163(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66 AND LYS-410,
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-104; LYS-122;
RP   LYS-132; LYS-143; LYS-159; LYS-166; LYS-273; LYS-277; LYS-334;
RP   LYS-410; LYS-430 AND LYS-505, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast, and 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.,
RA   Zhang Y., 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   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-104; LYS-122;
RP   LYS-132; LYS-143; LYS-334; LYS-346; LYS-410; LYS-420 AND LYS-505, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [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.,
RA   Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in
RT   mitochondria identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine
CC       cleavage system as well as an E3 component of the alpha-ketoacid
CC       dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and
CC       branched-chain amino acid-dehydrogenase complex). In monomeric
CC       form has additional moonlighting function as serine protease
CC       (PubMed:17404228). Involved in the hyperactivation of spermatazoa
CC       during capacitation and in the spermatazoal acrosome reaction (By
CC       similarity). {ECO:0000250|UniProtKB:Q811C4,
CC       ECO:0000269|PubMed:17404228}.
CC   -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
CC       protein N(6)-(lipoyl)lysine + NADH.
CC       {ECO:0000250|UniProtKB:P09622}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P09622};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P09622};
CC   -!- SUBUNIT: Homodimer. Part of the multimeric pyruvate dehydrogenase
CC       complex that contains multiple copies of pyruvate dehydrogenase
CC       (subunits PDH1A and PDHB, E1), dihydrolipoamide acetyltransferase
CC       (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits
CC       are bound to an inner core composed of about 48 DLAT and 12 PDHX
CC       molecules (by non covalent bonds). Interacts with PDHX.
CC       {ECO:0000250|UniProtKB:P09622}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000305|PubMed:9169128}. Cytoplasmic vesicle, secretory
CC       vesicle, acrosome {ECO:0000269|PubMed:15888450}. Cell projection,
CC       cilium, flagellum {ECO:0000250|UniProtKB:Q811C4}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver (at protein level).
CC       {ECO:0000269|PubMed:17404228}.
CC   -!- PTM: Acetylation of Lys-127 is observed in liver mitochondria from
CC       fasted mice but not from fed mice. {ECO:0000269|PubMed:23806337}.
CC   -!- PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q811C4}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
DR   EMBL; U73445; AAC53170.1; -; mRNA.
DR   EMBL; AK117104; BAE43405.1; -; mRNA.
DR   EMBL; AK136193; BAE22867.1; -; mRNA.
DR   EMBL; AK153399; BAE31961.1; -; mRNA.
DR   EMBL; AK168875; BAE40693.1; -; mRNA.
DR   EMBL; BC003368; AAH03368.1; -; mRNA.
DR   CCDS; CCDS36428.1; -.
DR   RefSeq; NP_031887.2; NM_007861.5.
DR   UniGene; Mm.3131; -.
DR   UniGene; Mm.471230; -.
DR   ProteinModelPortal; O08749; -.
DR   SMR; O08749; -.
DR   BioGrid; 199227; 4.
DR   IntAct; O08749; 10.
DR   MINT; MINT-4124146; -.
DR   STRING; 10090.ENSMUSP00000106481; -.
DR   ChEMBL; CHEMBL2176826; -.
DR   iPTMnet; O08749; -.
DR   PhosphoSitePlus; O08749; -.
DR   SwissPalm; O08749; -.
DR   REPRODUCTION-2DPAGE; O08749; -.
DR   SWISS-2DPAGE; O08749; -.
DR   EPD; O08749; -.
DR   MaxQB; O08749; -.
DR   PaxDb; O08749; -.
DR   PeptideAtlas; O08749; -.
DR   PRIDE; O08749; -.
DR   Ensembl; ENSMUST00000110857; ENSMUSP00000106481; ENSMUSG00000020664.
DR   GeneID; 13382; -.
DR   KEGG; mmu:13382; -.
DR   UCSC; uc007nhg.3; mouse.
DR   CTD; 1738; -.
DR   MGI; MGI:107450; Dld.
DR   eggNOG; KOG1335; Eukaryota.
DR   eggNOG; COG1249; LUCA.
DR   GeneTree; ENSGT00550000074844; -.
DR   HOGENOM; HOG000276708; -.
DR   HOVERGEN; HBG002290; -.
DR   InParanoid; O08749; -.
DR   KO; K00382; -.
DR   OMA; VYTQPEI; -.
DR   OrthoDB; EOG091G05AA; -.
DR   PhylomeDB; O08749; -.
DR   TreeFam; TF300414; -.
DR   Reactome; R-MMU-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR   Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-MMU-5362517; Signaling by Retinoic Acid.
DR   Reactome; R-MMU-6783984; Glycine degradation.
DR   Reactome; R-MMU-70268; Pyruvate metabolism.
DR   Reactome; R-MMU-70895; Branched-chain amino acid catabolism.
DR   Reactome; R-MMU-71064; Lysine catabolism.
DR   Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
DR   PRO; PR:O08749; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   Bgee; ENSMUSG00000020664; -.
DR   CleanEx; MM_DLD; -.
DR   Genevisible; O08749; MM.
DR   GO; GO:0043159; C:acrosomal matrix; IDA:MGI.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR   GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:Ensembl.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; ISO:MGI.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IMP:MGI.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:Ensembl.
DR   GO; GO:0043544; F:lipoamide binding; IEA:Ensembl.
DR   GO; GO:0051287; F:NAD binding; IEA:Ensembl.
DR   GO; GO:0034604; F:pyruvate dehydrogenase (NAD+) activity; IEA:Ensembl.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0051068; P:dihydrolipoamide metabolic process; IEA:Ensembl.
DR   GO; GO:0007369; P:gastrulation; IMP:MGI.
DR   GO; GO:0009106; P:lipoate metabolic process; IEA:Ensembl.
DR   GO; GO:0061732; P:mitochondrial acetyl-CoA biosynthetic process from pyruvate; ISO:MGI.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:MGI.
DR   GO; GO:0006508; P:proteolysis; IDA:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR   GO; GO:0048240; P:sperm capacitation; IDA:MGI.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR006258; Lipoamide_DH.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell projection; Cilium; Complete proteome;
KW   Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; FAD;
KW   Flagellum; Flavoprotein; Mitochondrion; NAD; Oxidoreductase;
KW   Phosphoprotein; Redox-active center; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1     35       Mitochondrion. {ECO:0000250}.
FT   CHAIN        36    509       Dihydrolipoyl dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000030297.
FT   NP_BIND      71     80       FAD. {ECO:0000250}.
FT   NP_BIND     183    185       FAD. {ECO:0000250}.
FT   NP_BIND     220    227       NAD. {ECO:0000250}.
FT   NP_BIND     361    364       FAD. {ECO:0000250}.
FT   ACT_SITE    487    487       Proton acceptor. {ECO:0000250}.
FT   BINDING      89     89       FAD. {ECO:0000250}.
FT   BINDING     154    154       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000250}.
FT   BINDING     243    243       NAD. {ECO:0000250}.
FT   BINDING     278    278       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000250}.
FT   BINDING     314    314       NAD; via amide nitrogen. {ECO:0000250}.
FT   BINDING     355    355       FAD. {ECO:0000250}.
FT   SITE        448    448       Important for interaction with PDHX and
FT                                activity of pyruvate dehydrogenase
FT                                complex. {ECO:0000250|UniProtKB:P09622}.
FT   SITE        473    473       Important for interaction with PDHX and
FT                                activity of pyruvate dehydrogenase
FT                                complex. {ECO:0000250|UniProtKB:P09622}.
FT   MOD_RES      66     66       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753,
FT                                ECO:0000244|PubMed:23806337}.
FT   MOD_RES      66     66       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     104    104       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     104    104       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     122    122       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     122    122       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     132    132       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     132    132       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     143    143       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     143    143       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     159    159       N6-succinyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     166    166       N6-succinyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     273    273       N6-succinyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     277    277       N6-succinyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     285    285       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     297    297       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q6P6R2}.
FT   MOD_RES     334    334       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     334    334       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     346    346       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     410    410       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753,
FT                                ECO:0000244|PubMed:23806337}.
FT   MOD_RES     410    410       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     417    417       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P09622}.
FT   MOD_RES     420    420       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     430    430       N6-succinyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     505    505       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     505    505       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   DISULFID     80     85       Redox-active. {ECO:0000250}.
FT   CONFLICT     54     54       Y -> C (in Ref. 1; AAC53170).
FT                                {ECO:0000305}.
FT   CONFLICT    144    144       Q -> T (in Ref. 2; BAE22867).
FT                                {ECO:0000305}.
FT   CONFLICT    149    149       H -> L (in Ref. 2; BAE31961).
FT                                {ECO:0000305}.
FT   CONFLICT    283    283       K -> E (in Ref. 2; BAE40693).
FT                                {ECO:0000305}.
SQ   SEQUENCE   509 AA;  54272 MW;  2C381852BAAD0441 CRC64;
     MQSWSRVYRS LAKKGHFNRI SHGLQGVSSV PLRTYADQPI EADVTVIGSG PGGYVAAIKS
     AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEIPEVRLNL
     EKMMEQKHSA VKALTGGIAH LFKQNKVVHV NGFGKITGKN QVTATKADGS TQVIDTKNIL
     VATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT
     AVEFLGHVGG IGIDMEISKN FQRILQRQGF KFKLNTKVTG ATKKSDGKID VSVEAASGGK
     AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPKGRIPVN NRFQTKIPNI YAIGDVVAGP
     MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEFKIGK
     FPFAANSRAK TNADTDGMVK ILGHKSTDRV LGAHILGPGA GEMVNEAALA LEYGASCEDI
     ARVCHAHPTL SEAFREANLA AAFGKPINF
//
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