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1Z7D

Ornithine aminotransferase PY00104 from Plasmodium Yoelii

Functional Information from GO Data
ChainGOidnamespacecontents
A0004587molecular_functionornithine aminotransferase activity
A0005737cellular_componentcytoplasm
A0008483molecular_functiontransaminase activity
A0010121biological_processL-arginine catabolic process to proline via ornithine
A0016740molecular_functiontransferase activity
A0019544biological_processL-arginine catabolic process to L-glutamate
A0030170molecular_functionpyridoxal phosphate binding
A0042802molecular_functionidentical protein binding
A0055129biological_processL-proline biosynthetic process
B0004587molecular_functionornithine aminotransferase activity
B0005737cellular_componentcytoplasm
B0008483molecular_functiontransaminase activity
B0010121biological_processL-arginine catabolic process to proline via ornithine
B0016740molecular_functiontransferase activity
B0019544biological_processL-arginine catabolic process to L-glutamate
B0030170molecular_functionpyridoxal phosphate binding
B0042802molecular_functionidentical protein binding
B0055129biological_processL-proline biosynthetic process
C0004587molecular_functionornithine aminotransferase activity
C0005737cellular_componentcytoplasm
C0008483molecular_functiontransaminase activity
C0010121biological_processL-arginine catabolic process to proline via ornithine
C0016740molecular_functiontransferase activity
C0019544biological_processL-arginine catabolic process to L-glutamate
C0030170molecular_functionpyridoxal phosphate binding
C0042802molecular_functionidentical protein binding
C0055129biological_processL-proline biosynthetic process
D0004587molecular_functionornithine aminotransferase activity
D0005737cellular_componentcytoplasm
D0008483molecular_functiontransaminase activity
D0010121biological_processL-arginine catabolic process to proline via ornithine
D0016740molecular_functiontransferase activity
D0019544biological_processL-arginine catabolic process to L-glutamate
D0030170molecular_functionpyridoxal phosphate binding
D0042802molecular_functionidentical protein binding
D0055129biological_processL-proline biosynthetic process
E0004587molecular_functionornithine aminotransferase activity
E0005737cellular_componentcytoplasm
E0008483molecular_functiontransaminase activity
E0010121biological_processL-arginine catabolic process to proline via ornithine
E0016740molecular_functiontransferase activity
E0019544biological_processL-arginine catabolic process to L-glutamate
E0030170molecular_functionpyridoxal phosphate binding
E0042802molecular_functionidentical protein binding
E0055129biological_processL-proline biosynthetic process
F0004587molecular_functionornithine aminotransferase activity
F0005737cellular_componentcytoplasm
F0008483molecular_functiontransaminase activity
F0010121biological_processL-arginine catabolic process to proline via ornithine
F0016740molecular_functiontransferase activity
F0019544biological_processL-arginine catabolic process to L-glutamate
F0030170molecular_functionpyridoxal phosphate binding
F0042802molecular_functionidentical protein binding
F0055129biological_processL-proline biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FVaDEVqt.GLgRtGkllcvhhynvkp....DVIllGKalsGG
ChainResidueDetails
APHE229-GLY266

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"P04181","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
ALYS261
AASP232

site_idCSA10
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
DASP232

site_idCSA11
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
EASP232

site_idCSA12
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
FASP232

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
BPHE173
BLYS261
BASP232

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
CLYS261
CASP232

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
DLYS261
DASP232

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
ELYS261
EASP232

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
FLYS261
FASP232

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
AASP232

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
BPHE173
BASP232

site_idCSA9
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
CASP232

246031

PDB entries from 2025-12-10

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