1T3D,1S80,1SST


Conserved Protein Domain Family
LbH_SAT

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cd03354: LbH_SAT 
Click on image for an interactive view with Cn3D
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.
Statistics
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PSSM-Id: 100045
View PSSM: cd03354
Aligned: 115 rows
Threshold Bit Score: 104.059
Threshold Setting Gi: 15824375
Created: 16-Aug-2001
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 16 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Comment:Based on the structures of serine acetyltransferase bound to CoA (1SST) and substrate (1T3D).
  • Comment:Serine acetyltransferase is hexameric, composed of a dimer of homotrimers. The active sites are located at the interface between two LbH subunits in the homotrimer. The trimer structure contains three active sites and each subunit contributes to two active sites via residues located on two surfaces.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                      ##                        ##     ##        ##          #       
1T3D_C    156 FQVDIHPaAKIGRGIXLDHa-----TGIVVGEtAVIENd-VSILQsVTLGGTgks--ggdRHPKIREGVXIGAGAKILGn 227 Escherichia coli
1SST_A    136 FDVDIHPaAKIGHGIMFDHa-----TGIVVGEtSVIENd-VSILQgVTLGGTgke--sgdRHPKVREGVMIGAGAKILGn 207 Haemophilus influe...
AAR35336   73 YGISIPYnTDIGPGLYIGHf-----GGIIVNAeATIGRn-CNINQeVTVGATygg--kypGTPVIMNNVYLGPGSKIIGg 144 Geobacter sulfurre...
BAD49535   72 TGVQISPyADIDGGLAIAHf-----SCIVISD-CKIGKh-FTIMQgSTIGSYrgs--ikgGSPSIGDNVVICAGAKVIGn 142 Bacteroides fragil...
EDO54107   73 TGIQIGFgTKIGKALMFPHy-----SCIVINGsAIIGDn-CTIYHgVTVGSVrgp---kgGAPHIGNNVVIASGAKVIGn 143 Bacteroides unifor...
EDO54113   78 FGIQMPLgTPVKGGLSFNHf-----SCIIINGaTQIGHn-CTIFHgVTTALKmgg--snaGVPSIGNNCVLGPGSKILGs 149 Bacteroides unifor...
CAH08497   75 LKITIYP-NTIGAGLRIYHv----gDFIHIGAqCHIGHn-CTLLPgVVFGNKyek--atdTQIIAGNNCYFGLGAKIFGs 146 Bacteroides fragil...
AAZ27890   54 AYFFQWL-NKLVNGCVIGSganfssGFVIMHPiGIVINskVIGGHnITLESGvvigdekgKSPCLENNIFIGSGAKIIGq 132 Colwellia psychrer...
YP_271658  65 NGCVIGSgANFSSGFVIMHp-----IGIVINSkVIGGHn-ITLESgVVIGDEk------gKSPCLENNIFIGSGAKIIGq 132 Colwellia psychrer...
YP_149162  59 IGSDIPKqIECGEGLRIPHg----gRGIIIHPtVKIGKn-VTIFHqVTIGVKep----iiQGATIENNVYIGAGAKIIGs 129 Geobacillus kausto...
Feature 1            # ##  # #       #    #
1T3D_C    228 IEVGRGAKIGAGSVVLQPVPPHTTAAGVP 256 Escherichia coli
1SST_A    208 IEVGKYAKIGANSVVLNPVPEYATAAGVP 236 Haemophilus influenzae
AAR35336  145 ITLGSHAAVGANCVVTKPVPDHGVVVGIP 173 Geobacter sulfurreducens PCA
BAD49535  143 IKLGNNAMVGANAVVVKDIPDNAVVAGVP 171 Bacteroides fragilis YCH46
EDO54107  144 ITIGNNVMIGSGAIVVTDIPDNSVVVGNP 172 Bacteroides uniformis ATCC 8492
EDO54113  150 VTLGDNVFVGANAVVTHDMPSNSIVAGIP 178 Bacteroides uniformis ATCC 8492
CAH08497  147 IIIGNNVTIGANAVVTKDIPDNAIVGGIP 175 Bacteroides fragilis NCTC 9343
AAZ27890  133 LSIEDNVKIGANAVLTKDAKYGSTMLGIP 161 Colwellia psychrerythraea 34H
YP_271658 133 LSIEDNVKIGANAVLTKDAKYGSTMLGIP 161 Colwellia psychrerythraea 34H
YP_149162 130 VLIGENCRIGANAVVVKDVPPNSTVVGIP 158 Geobacillus kaustophilus HTA426

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