strla-d2z028

Streptomyces lavendulae subsp. lavendula, dcsE, metX, Homoserine O-acetyltransferase

Comment

Relationship

Block : X

Position in NCBI Life Tree : Streptomyces lavendulae subsp. lavendulae

(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)

> cellular organisms N E > Bacteria N E > Terrabacteria group N E > Actinobacteria [phylum] N E > Actinobacteria [class] N E > Streptomycetales N E > Streptomycetaceae N E > Streptomyces N E > Streptomyces lavendulae N E > Streptomyces lavendulae subsp. lavendulae N E > cellular organisms N E > Bacteria N E > Terrabacteria group N E > Actinobacteria [phylum] N E > Actinobacteria [class] N E > Streptomycetales N E > Streptomycetaceae N E > Streptomyces N E > Streptomyces lavendulae N E > Streptomyces lavendulae subsp. lavendulae N E > cellular organisms N E > Bacteria N E > Terrabacteria group N E > Actinobacteria [phylum] N E > Actinobacteria [class] N E > Streptomycetales N E > Streptomycetaceae N E > Streptomyces N E > Streptomyces lavendulae N E > Streptomyces lavendulae subsp. lavendulae N E

Molecular evidence

No mutation

3VVL - Crystal structure of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway 3VVL - Crystal structure of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway 3VVL - Crystal structure of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway 3VVM - Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway 3VVM - Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway 3VVM - Crystal structure of G52A-P55G mutant of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway

No kinetic

No disease

No substrate

No inhibitor

Database

No Genbank

D2Z028

Sequence

Peptide

MREFIPPASR FIELPDGFAM RRGGALYGAR IAYETFGSLN AARDNAVLVL TGLSPDAHAA SRPDDPTPGW WEAMVGPGKP VDTDLWHVIC VNSLGSCKGS TGPASTDPRT GEPYRLSFPE LSIEDIADAA AHTVRALGIS RLACVVGASM GGMSALALLA RHPELARTHI SLSGAVHALP FSIAVRSLQR EAIRSDPGWL QGHYDEGEGP RRGMLTARKL GMMTYRSAQE WDCRFGRTRI GERRRADQGR FGPEFEVESY LDFHAQRFAD RFDPNSYLYL SHAMDQFDLG DGGGGGGGAP GALSRMRVER ALVMGARTDI LFPLSQQQEI ADGLSAGGAD VSFLPVDTPA GHDAFLVDIE RFGPPVAKFL AIVA

References (3)

Title : Crystallographic Study To Determine the Substrate Specificity of an L-Serine-Acetylating Enzyme Found in the D-Cycloserine Biosynthetic Pathway - Oda_2013_J.Bacteriol_195_1741

Author(s) : Oda K , Matoba Y , Kumagai T , Noda M , Sugiyama M

Ref : Journal of Bacteriology , 195 :1741 , 2013

Abstract :

PubMedSearch : Oda_2013_J.Bacteriol_195_1741

PubMedID: 23396912

Gene_locus related to this paper: strla-d2z028

Title : Crystallographic Study To Determine the Substrate Specificity of an L-Serine-Acetylating Enzyme Found in the D-Cycloserine Biosynthetic Pathway - Oda_2013_J.Bacteriol_195_1741

Author(s) : Oda K , Matoba Y , Kumagai T , Noda M , Sugiyama M

Ref : Journal of Bacteriology , 195 :1741 , 2013

Abstract :

PubMedSearch : Oda_2013_J.Bacteriol_195_1741

PubMedID: 23396912

Gene_locus related to this paper: strla-d2z028

Title : Crystallographic Study To Determine the Substrate Specificity of an L-Serine-Acetylating Enzyme Found in the D-Cycloserine Biosynthetic Pathway - Oda_2013_J.Bacteriol_195_1741

Author(s) : Oda K , Matoba Y , Kumagai T , Noda M , Sugiyama M

Ref : Journal of Bacteriology , 195 :1741 , 2013

Abstract :

PubMedSearch : Oda_2013_J.Bacteriol_195_1741

PubMedID: 23396912

Gene_locus related to this paper: strla-d2z028

strla-d2z028

Comment

Relationship

Molecular evidence

Mutation (0)

Structure (6)

Kinetic (0)

Disease (0)

Substrate (0)

Inhibitor (0)

Database

Genbank (0)

Interpro (1)

Pfam (1)

UniProt (1)

PIRSF (1)

SUPERFAM (1)

Sequence

Peptide

References (3)

1. Crystallographic Study To Determine the Substrate Specificity of an L-Serine-Acetylating Enzyme Found in the D-Cycloserine Biosynthetic Pathway - Oda_2013_J.Bacteriol_195_1741

2. Crystallographic Study To Determine the Substrate Specificity of an L-Serine-Acetylating Enzyme Found in the D-Cycloserine Biosynthetic Pathway - Oda_2013_J.Bacteriol_195_1741

3. Crystallographic Study To Determine the Substrate Specificity of an L-Serine-Acetylating Enzyme Found in the D-Cycloserine Biosynthetic Pathway - Oda_2013_J.Bacteriol_195_1741