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Sequence of ECHA_HUMAN

EC Number:1.1.1.211

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
long-chain-3-hydroxyacyl-CoA dehydrogenase
P40939
Homo sapiens
763
83000
Reaction
a long-chain (S)-3-hydroxyacyl-CoA + NAD+ = a long-chain 3-oxoacyl-CoA + NADH + H+
Other sequences found for EC No. 1.1.1.211

EC Number:4.2.1.17

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
enoyl-CoA hydratase
P40939
Homo sapiens
763
83000
Reaction
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O
Other sequences found for EC No. 4.2.1.17

General information:

Sequence
show sequence in fasta format
  0 MVACRAIGIL SRFSAFRILR SRGYICRNFT GSSALLTRTH INYGVKGDVA VVRINSPNSK
 60 VNTLSKELHS EFSEVMNEIW ASDQIRSAVL ISSKPGCFIA GADINMLAAC KTLQEVTQLS
120 QEAQRIVEKL EKSTKPIVAA INGSCLGGGL EVAISCQYRI ATKDRKTVLG TPEVLLGALP
180 GAGGTQRLPK MVGVPAALDM MLTGRSIRAD RAKKMGLVDQ LVEPLGPGLK PPEERTIEYL
240 EEVAITFAKG LADKKISPKR DKGLVEKLTA YAMTIPFVRQ QVYKKVEEKV RKQTKGLYPA
300 PLKIIDVVKT GIEQGSDAGY LCESQKFGEL VMTKESKALM GLYHGQVLCK KNKFGAPQKD
360 VKHLAILGAG LMGAGIAQVS VDKGLKTILK DATLTALDRG QQQVFKGLND KVKKKALTSF
420 ERDSIFSNLT GQLDYQGFEK ADMVIEAVFE DLSLKHRVLK EVEAVIPDHC IFASNTSALP
480 ISEIAAVSKR PEKVIGMHYF SPVDKMQLLE IITTEKTSKD TSASAVAVGL KQGKVIIVVK
540 DGPGFYTTRC LAPMMSEVIR ILQEGVDPKK LDSLTTSFGF PVGAATLVDE VGVDVAKHVA
600 EDLGKVFGER FGGGNPELLT QMVSKGFLGR KSGKGFYIYQ EGVKRKDLNS DMDSILASLK
660 LPPKSEVSSD EDIQFRLVTR FVNEAVMCLQ EGILATPAEG DIGAVFGLGF PPCLGGPFRF
720 VDLYGAQKIV DRLKKYEAAY GKQFTPCQLL ADHANSPNKK FYQ
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
412475
Kamijo T.,Aoyama T.,Komiyama A.,Hashimoto T.
Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein.
Biochem. Biophys. Res. Commun.
199
818-825
1994
412476
Zhang Q.X.,Baldwin G.S.
Structures of the human cDNA and gene encoding the 78 kDa gastrin-binding protein and of a related pseudogene.
Biochim. Biophys. Acta
1219
567-575
1994
412477
Ota T.,Suzuki Y.,Nishikawa T.,Otsuki T.,Sugiyama T.,Irie R.,Wakamatsu A.,Hayashi K.,Sato H.,Nagai K.,Kimura K.,Makita H.,Sekine M.,Obayashi M.,Nishi T.,Shibahara T.,Tanaka T.,Ishii S.,Yamamoto J.,Saito K.,Kawai Y.,Isono Y.,Nakamura Y.,Nagahari K.,Murakami K.,Yasuda T.,Iwayanagi T.,Wagatsuma M.,Shiratori A.,Sudo H.,Hosoiri T.,Kaku Y.,Kodaira H.,Kondo H.,Sugawara M.,Takahashi M.,Kanda K.,Yokoi T.,Furuya T.,Kikkawa E.,Omura Y.,Abe K.,Kamihara K.,Katsuta N.,Sato K.,Tanikawa M.,Yamazaki M.,Ninomiya K.,Ishibashi T.,Yamashita H.,Murakawa K.,Fujimori K.,Tanai H.,Kimata M.,Watanabe M.,Hiraoka S.,Chiba Y.,Ishida S.,Ono Y.,Takiguchi S.,Watanabe S.,Yosida M.,Hotuta T.,Kusano J.,Kanehori K.,Takahashi-Fujii A.,Hara H.,Tanase T.-O.,Nomura Y.,Togiya S.,Komai F.,Hara R.,Takeuchi K.,Arita M.,Imose N.,Musashino K.,Yuuki H.,Oshima A.,Sasaki N.,Aotsuka S.,Yoshikawa Y.,Matsunawa H.,Ichihara T.,Shiohata N.,Sano S.,Moriya S.,Momiyama H.,Satoh N.,Takami S.,Terashima Y.,Suzuki O.,Nakagawa S.,Senoh A.,Mizoguchi H.,Goto Y.,Shimizu F.,Wakebe H.,Hishigaki H.,Watanabe T.,Sugiyama A.,Takemoto M.,Kawakami B.,Yamazaki M.,Watanabe K.,Kumagai A.,Itakura S.,Fukuzumi Y.,Fujimori Y.,Komiyama M.,Tashiro H.,Tanigami A.,Fujiwara T.,Ono T.,Yamada K.,Fujii Y.,Ozaki K.,Hirao M.,Ohmori Y.,Kawabata A.,Hikiji T.,Kobatake N.,Inagaki H.,Ikema Y.,Okamoto S.,Okitani R.,Kawakami T.,Noguchi S.,Itoh T.,Shigeta K.,Senba T.,Matsumura K.,Nakajima Y.,Mizuno T.,Morinaga M.,Sasaki M.,Togashi T.,Oyama M.,Hata H.,Watanabe M.,Komatsu T.,Mizushima-Sugano J.,Satoh T.,Shirai Y.,Takahashi Y.,Nakagawa K.,Okumura K.,Nagase T.,Nomura N.,Kikuchi H.,Masuho Y.,Yamashita R.,Nakai K.,Yada T.,Nakamura Y.,Ohara O.,Isogai T.,Sugano S.
Complete sequencing and characterization of 21,243 full-length human cDNAs.
Nat. Genet.
36
40-45
2004
412478
Hillier L.W.,Graves T.A.,Fulton R.S.,Fulton L.A.,Pepin K.H.,Minx P.,Wagner-McPherson C.,Layman D.,Wylie K.,Sekhon M.,Becker M.C.,Fewell G.A.,Delehaunty K.D.,Miner T.L.,Nash W.E.,Kremitzki C.,Oddy L.,Du H.,Sun H.,Bradshaw-Cordum H.,Ali J.,Carter J.,Cordes M.,Harris A.,Isak A.,van Brunt A.,Nguyen C.,Du F.,Courtney L.,Kalicki J.,Ozersky P.,Abbott S.,Armstrong J.,Belter E.A.,Caruso L.,Cedroni M.,Cotton M.,Davidson T.,Desai A.,Elliott G.,Erb T.,Fronick C.,Gaige T.,Haakenson W.,Haglund K.,Holmes A.,Harkins R.,Kim K.,Kruchowski S.S.,Strong C.M.,Grewal N.,Goyea E.,Hou S.,Levy A.,Martinka S.,Mead K.,McLellan M.D.,Meyer R.,Randall-Maher J.,Tomlinson C.,Dauphin-Kohlberg S.,Kozlowicz-Reilly A.,Shah N.,Swearengen-Shahid S.,Snider J.,Strong J.T.,Thompson J.,Yoakum M.,Leonard S.,Pearman C.,Trani L.,Radionenko M.,Waligorski J.E.,Wang C.,Rock S.M.,Tin-Wollam A.-M.,Maupin R.,Latreille P.,Wendl M.C.,Yang S.-P.,Pohl C.,Wallis J.W.,Spieth J.,Bieri T.A.,Berkowicz N.,Nelson J.O.,Osborne J.,Ding L.,Meyer R.,Sabo A.,Shotland Y.,Sinha P.,Wohldmann P.E.,Cook L.L.,Hickenbotham M.T.,Eldred J.,Williams D.,Jones T.A.,She X.,Ciccarelli F.D.,Izaurralde E.,Taylor J.,Schmutz J.,Myers R.M.,Cox D.R.,Huang X.,McPherson J.D.,Mardis E.R.,Clifton S.W.,Warren W.C.,Chinwalla A.T.,Eddy S.R.,Marra M.A.,Ovcharenko I.,Furey T.S.,Miller W.,Eichler E.E.,Bork P.,Suyama M.,Torrents D.,Waterston R.H.,Wilson R.K.
Generation and annotation of the DNA sequences of human chromosomes 2 and 4.
Nature
434
724-731
2005
412480
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
412481
Orii K.E.,Orii K.O.,Souri M.,Orii T.,Kondo N.,Hashimoto T.,Aoyama T.
Genes for the human mitochondrial trifunctional protein alpha- and beta-subunits are divergently transcribed from a common promoter region.
J. Biol. Chem.
274
8077-8084
1999
412482
Carpenter K.,Pollitt R.J.,Middleton B.
Human liver long-chain 3-hydroxyacyl-coenzyme A dehydrogenase is a multifunctional membrane-bound beta-oxidation enzyme of mitochondria.
Biochem. Biophys. Res. Commun.
183
443-448
1992
412483
Kamijo T.,Wanders R.J.,Saudubray J.-M.,Aoyama T.,Komiyama A.,Hashimoto T.
Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients.
J. Clin. Invest.
93
1740-1747
1994
412484
Ushikubo S.,Aoyama T.,Kamijo T.,Wanders R.J.A.,Rinaldo P.,Vockley J.,Hashimoto T.
Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both alpha- and beta-subunits.
Am. J. Hum. Genet.
58
979-988
1996
412485
Choudhary C.,Kumar C.,Gnad F.,Nielsen M.L.,Rehman M.,Walther T.C.,Olsen J.V.,Mann M.
Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Science
325
834-840
2009
412486
Burkard T.R.,Planyavsky M.,Kaupe I.,Breitwieser F.P.,Buerckstuemmer T.,Bennett K.L.,Superti-Furga G.,Colinge J.
Initial characterization of the human central proteome.
BMC Syst. Biol.
5
17-17
2011
412487
Taylor W.A.,Mejia E.M.,Mitchell R.W.,Choy P.C.,Sparagna G.C.,Hatch G.M.
Human trifunctional protein alpha links cardiolipin remodeling to beta-oxidation.
PLoS ONE
7
0-0
2012
412488
Zhou H.,Di Palma S.,Preisinger C.,Peng M.,Polat A.N.,Heck A.J.,Mohammed S.
Toward a comprehensive characterization of a human cancer cell phosphoproteome.
J. Proteome Res.
12
260-271
2013
412489
Bian Y.,Song C.,Cheng K.,Dong M.,Wang F.,Huang J.,Sun D.,Wang L.,Ye M.,Zou H.
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
J. Proteomics
96
253-262
2014
412490
Vaca Jacome A.S.,Rabilloud T.,Schaeffer-Reiss C.,Rompais M.,Ayoub D.,Lane L.,Bairoch A.,Van Dorsselaer A.,Carapito C.
N-terminome analysis of the human mitochondrial proteome.
Proteomics
15
2519-2524
2015
412491
Liang K.,Li N.,Wang X.,Dai J.,Liu P.,Wang C.,Chen X.W.,Gao N.,Xiao J.
Cryo-EM structure of human mitochondrial trifunctional protein.
Proc. Natl. Acad. Sci. U.S.A.
115
7039-7044
2018
412492
Xia C.,Fu Z.,Battaile K.P.,Kim J.P.
Crystal structure of human mitochondrial trifunctional protein, a fatty acid beta-oxidation metabolon.
Proc. Natl. Acad. Sci. U.S.A.
116
6069-6074
2019
412493
Ijlst L.,Wanders R.J.A.,Ushikubo S.,Kamijo T.,Hashimoto T.
Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: identification of the major disease-causing mutation in the alpha-subunit of the mitochondrial trifunctional protein.
Biochim. Biophys. Acta
1215
347-350
1994
412494
Sims H.F.,Brackett J.C.,Powell C.K.,Treem W.R.,Hale D.E.,Bennett M.J.,Gibson B.,Shapiro S.,Strauss A.W.
The molecular basis of pediatric long chain 3-hydroxyacyl-CoA dehydrogenase deficiency associated with maternal acute fatty liver of pregnancy.
Proc. Natl. Acad. Sci. U.S.A.
92
841-845
1995
412495
Ijlst L.,Ruiter J.P.N.,Hoovers J.M.N.,Jakobs M.E.,Wanders R.J.A.
Common missense mutation G1528C in long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency. Characterization and expression of the mutant protein, mutation analysis on genomic DNA and chromosomal localization of the mitochondrial trifunctional protein alpha subunit gene.
J. Clin. Invest.
98
1028-1033
1996
412496
Ijlst L.,Oostheim W.,Ruiter J.P.N.,Wanders R.J.A.
Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: identification of two new mutations.
J. Inherit. Metab. Dis.
20
420-422
1997
412497
Ibdah J.A.,Tein I.,Dionisi-Vici C.,Bennett M.J.,Ijlst L.,Gibson B.,Wanders R.J.A.,Strauss A.W.
Mild trifunctional protein deficiency is associated with progressive neuropathy and myopathy and suggests a novel genotype-phenotype correlation.
J. Clin. Invest.
102
1193-1199
1998