8C80

Cryo-EM structure of the yeast SPT-Orm1-Monomer complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003674	molecular_function	molecular_function
A	0005515	molecular_function	protein binding
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006629	biological_process	lipid metabolic process
A	0006665	biological_process	sphingolipid metabolic process
A	0006672	biological_process	ceramide metabolic process
A	0006897	biological_process	endocytosis
A	0006986	biological_process	response to unfolded protein
A	0016020	cellular_component	membrane
A	0017059	cellular_component	serine palmitoyltransferase complex
A	0030148	biological_process	sphingolipid biosynthetic process
A	0090155	biological_process	negative regulation of sphingolipid biosynthetic process
A	0090156	biological_process	intracellular sphingolipid homeostasis
B	0004758	molecular_function	serine C-palmitoyltransferase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006629	biological_process	lipid metabolic process
B	0006665	biological_process	sphingolipid metabolic process
B	0009058	biological_process	biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0017059	cellular_component	serine palmitoyltransferase complex
B	0030148	biological_process	sphingolipid biosynthetic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0046512	biological_process	sphingosine biosynthetic process
B	0046513	biological_process	ceramide biosynthetic process
B	0090156	biological_process	intracellular sphingolipid homeostasis
C	0004758	molecular_function	serine C-palmitoyltransferase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005783	cellular_component	endoplasmic reticulum
C	0006629	biological_process	lipid metabolic process
C	0006665	biological_process	sphingolipid metabolic process
C	0009058	biological_process	biosynthetic process
C	0016020	cellular_component	membrane
C	0016740	molecular_function	transferase activity
C	0016746	molecular_function	acyltransferase activity
C	0017059	cellular_component	serine palmitoyltransferase complex
C	0030148	biological_process	sphingolipid biosynthetic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	0046512	biological_process	sphingosine biosynthetic process
C	0046513	biological_process	ceramide biosynthetic process
C	0090156	biological_process	intracellular sphingolipid homeostasis
D	0005783	cellular_component	endoplasmic reticulum
D	0005789	cellular_component	endoplasmic reticulum membrane
D	0006629	biological_process	lipid metabolic process
D	0006665	biological_process	sphingolipid metabolic process
D	0006666	biological_process	3-keto-sphinganine metabolic process
D	0008047	molecular_function	enzyme activator activity
D	0017059	cellular_component	serine palmitoyltransferase complex
D	0090154	biological_process	positive regulation of sphingolipid biosynthetic process
D	0090156	biological_process	intracellular sphingolipid homeostasis

Functional Information from PROSITE/UniProt

site_id	PS00599
Number of Residues	10
Details	AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFTKSFGAAG

Chain	Residue	Details
C	THR363-GLY372

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	140
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	47
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	95
Details	Transmembrane: {"description":"Helical"}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	256
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15485854","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	52
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"15485854","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---