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Sequence of METAA_BACC1

EC Number:2.3.1.31

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
homoserine O-acetyltransferase
Q72X44
Bacillus cereus (strain ATCC 10987 / NRS 248)
301
35340
Reaction
acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Other sequences found for EC No. 2.3.1.31

EC Number:2.3.1.46

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
homoserine O-succinyltransferase
Q72X44
Bacillus cereus (strain ATCC 10987 / NRS 248)
301
35340
Reaction
succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine
Other sequences found for EC No. 2.3.1.46

General information:

Sequence
show sequence in fasta format
  0 MPIIIDKDLP ARKVLQEENI FVMTKERAET QDIRALKIAI LNLMPTKQET EAQLLRLIGN
 60 TPLQLDVHLL HMESHLSRNV AQEHLTSFYK TFRDIENEKF DGLIITGAPV ETLSFEEVDY
120 WEELKRIMEY SKTNVTSTLH ICWGAQAGLY HHYGVQKYPL KEKMFGVFEH EVREQHVKLL
180 QGFDELFFAP HSRHTEVRES DIREVKELTL LANSEEAGVH LVIGQEGRQV FALGHSEYSC
240 DTLKQEYERD RDKGLNIDVP KNYFKHDNPN EKPLVRWRSH GNLLFSNWLN YYVYQETPYV
300 L
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
569177
Rasko D.A.,Ravel J.,Oekstad O.A.,Helgason E.,Cer R.Z.,Jiang L.,Shores K.A.,Fouts D.E.,Tourasse N.J.,Angiuoli S.V.,Kolonay J.F.,Nelson W.C.,Kolstoe A.-B.,Fraser C.M.,Read T.D.
The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1.
Nucleic Acids Res.
32
977-988
2004
569178
Bastard K.,Perret A.,Mariage A.,Bessonnet T.,Pinet-Turpault A.,Petit J.L.,Darii E.,Bazire P.,Vergne-Vaxelaire C.,Brewee C.,Debard A.,Pellouin V.,Besnard-Gonnet M.,Artiguenave F.,Medigue C.,Vallenet D.,Danchin A.,Zaparucha A.,Weissenbach J.,Salanoubat M.,de Berardinis V.
Parallel evolution of non-homologous isofunctional enzymes in methionine biosynthesis.
Nat. Chem. Biol.
13
858-866
2017
569179
Zubieta C.,Krishna S.S.,McMullan D.,Miller M.D.,Abdubek P.,Agarwalla S.,Ambing E.,Astakhova T.,Axelrod H.L.,Carlton D.,Chiu H.J.,Clayton T.,Deller M.,DiDonato M.,Duan L.,Elsliger M.A.,Grzechnik S.K.,Hale J.,Hampton E.,Han G.W.,Haugen J.,Jaroszewski L.,Jin K.K.,Klock H.E.,Knuth M.W.,Koesema E.,Kumar A.,Marciano D.,Morse A.T.,Nigoghossian E.,Oommachen S.,Reyes R.,Rife C.L.,van den Bedem H.,Weekes D.,White A.,Xu Q.,Hodgson K.O.,Wooley J.,Deacon A.M.,Godzik A.,Lesley S.A.,Wilson I.A.
Crystal structure of homoserine O-succinyltransferase from Bacillus cereus at 2.4 A resolution.
Proteins
68
999-1005
2007
569180
Zubieta C.,Arkus K.A.,Cahoon R.E.,Jez J.M.
A single amino acid change is responsible for evolution of acyltransferase specificity in bacterial methionine biosynthesis.
J. Biol. Chem.
283
7561-7567
2008