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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
DOI=10.1038/nature03481; PubMed=15875012 [NCBI, ExPASy, EBI, Israel, Japan]
Eichinger L.,
Pachebat J.A.,
Gloeckner G.,
Rajandream M.A.,
Sucgang R.,
Berriman M.,
Song J.,
Olsen R.,
Szafranski K.,
Xu Q.,
Tunggal B.,
Kummerfeld S.,
Madera M.,
Konfortov B.A.,
Rivero F.,
Bankier A.T.,
Lehmann R.,
Hamlin N.,
Davies R., ![]()
Gaudet P.,
Fey P.,
Pilcher K.,
Chen G.,
Saunders D.,
Sodergren E.J.,
Davis P.,
Kerhornou A.,
Nie X.,
Hall N.,
Anjard C.,
Hemphill L.,
Bason N.,
Farbrother P.,
Desany B.,
Just E.,
Morio T.,
Rost R.,
Churcher C.M.,
Cooper J.,
Haydock S.,
van Driessche N.,
Cronin A.,
Goodhead I.,
Muzny D.M.,
Mourier T.,
Pain A.,
Lu M.,
Harper D.,
Lindsay R.,
Hauser H.,
James K.D.,
Quiles M.,
Madan Babu M.,
Saito T.,
Buchrieser C.,
Wardroper A.,
Felder M.,
Thangavelu M.,
Johnson D.,
Knights A.,
Loulseged H.,
Mungall K.L.,
Oliver K.,
Price C.,
Quail M.A.,
Urushihara H.,
Hernandez J.,
Rabbinowitsch E.,
Steffen D.,
Sanders M.,
Ma J.,
Kohara Y.,
Sharp S.,
Simmonds M.N.,
Spiegler S.,
Tivey A.,
Sugano S.,
White B.,
Walker D.,
Woodward J.R.,
Winckler T.,
Tanaka Y.,
Shaulsky G.,
Schleicher M.,
Weinstock G.M.,
Rosenthal A.,
Cox E.C.,
Chisholm R.L.,
Gibbs R.A.,
Loomis W.F.,
Platzer M.,
Kay R.R.,
Williams J.G.,
Dear P.H.,
Noegel A.A.,
Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
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- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
- CATALYTIC ACTIVITY: 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2.
- COFACTOR: Thiamine pyrophosphate (By similarity).
- SUBUNIT: Heterotetramer of alpha and beta chains (By similarity).
- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
- MISCELLANEOUS: Bound potassium ions stabilize the protein structure (By similarity).
- SIMILARITY: Belongs to the BCKDHA family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 441 AA [This is the length of the unprocessed precursor] |
Molecular weight: 50326 Da [This is the MW of the unprocessed precursor] |
CRC64: E4ECC73ADFFC0538 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MISQSYRILS RISRNNELKK TFLTNLNCKS SSPSIIRSFC KKQNLDENFE YTNKLEVQEL
70 80 90 100 110 120
KHYIPCYTIM DQEGVVSKPD QDPNFSKEEV IKMYTTMLTL NVMDSILYDV QRQGRISFYM
130 140 150 160 170 180
TSFGEEAIHI GSAAALEMSD TIFAQYRETG VFMWRGFTIN DIINQCCTNE HDLGKGRQMP
190 200 210 220 230 240
MHFGSRKINL QTISSPLTTQ LPQAVGSSYA QKLAGEKNCT IVYFGEGAAS EGDFHAAMNF
250 260 270 280 290 300
AAALSTPTIF FCRNNKWAIS TPSKEQYKGD GIAGRGPNGY GMKTIRVDGN DIWAVYNVTK
310 320 330 340 350 360
LARKIAVEEQ VPVLIEAMTY RVGHHSTSDD SSRYRTVEEI NAWKEGKNPI SRLRNYMNHK
370 380 390 400 410 420
GWWSDAQEKE TIANARTTVR ESLVNAEKQY KPSINEIFTD VYDKPTPNLI EQQKELIEHL
430 440
KLYPDEYPLN QFADSKLILK D
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Q54M22 in FASTA format |
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