8SKR

human liver mitochondrial Aspartate aminotransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0003824	molecular_function	catalytic activity
A	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005886	cellular_component	plasma membrane
A	0006103	biological_process	2-oxoglutarate metabolic process
A	0006520	biological_process	amino acid metabolic process
A	0006531	biological_process	aspartate metabolic process
A	0006533	biological_process	L-aspartate catabolic process
A	0006536	biological_process	glutamate metabolic process
A	0006869	biological_process	lipid transport
A	0008483	molecular_function	transaminase activity
A	0009058	biological_process	biosynthetic process
A	0015908	biological_process	fatty acid transport
A	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
A	0016740	molecular_function	transferase activity
A	0019470	biological_process	trans-4-hydroxy-L-proline catabolic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0043490	biological_process	malate-aspartate shuttle
A	0045471	biological_process	response to ethanol
A	0070062	cellular_component	extracellular exosome
C	0003723	molecular_function	RNA binding
C	0003824	molecular_function	catalytic activity
C	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0005886	cellular_component	plasma membrane
C	0006103	biological_process	2-oxoglutarate metabolic process
C	0006520	biological_process	amino acid metabolic process
C	0006531	biological_process	aspartate metabolic process
C	0006533	biological_process	L-aspartate catabolic process
C	0006536	biological_process	glutamate metabolic process
C	0006869	biological_process	lipid transport
C	0008483	molecular_function	transaminase activity
C	0009058	biological_process	biosynthetic process
C	0015908	biological_process	fatty acid transport
C	0016212	molecular_function	kynurenine-oxoglutarate transaminase activity
C	0016740	molecular_function	transferase activity
C	0019470	biological_process	trans-4-hydroxy-L-proline catabolic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	0043490	biological_process	malate-aspartate shuttle
C	0045471	biological_process	response to ethanol
C	0070062	cellular_component	extracellular exosome

Functional Information from PROSITE/UniProt

site_id	PS00105
Number of Residues	14
Details	AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYAKnmGLyGERVG

Chain	Residue	Details
A	SER276-GLY289

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P05202","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	22
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P05202","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine; alternate","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P05202","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P05202","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P12344","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Asymmetric dimethylarginine","evidences":[{"source":"UniProtKB","id":"P05202","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---