ID A0A0V0R7Q2_PSEPJ Unreviewed; 424 AA.
AC A0A0V0R7Q2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Pyridoxal phosphate-dependent transferase {ECO:0000313|EMBL:KRX10513.1};
GN ORFNames=PPERSA_01525 {ECO:0000313|EMBL:KRX10513.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX10513.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX10513.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX10513.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX10513.1}.
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DR EMBL; LDAU01000026; KRX10513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0R7Q2; -.
DR EnsemblProtists; KRX10513; KRX10513; PPERSA_01525.
DR InParanoid; A0A0V0R7Q2; -.
DR OrthoDB; 176869at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383:SF2; (5-FORMYLFURAN-3-YL)METHYL PHOSPHATE TRANSAMINASE; 1.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW Transferase {ECO:0000313|EMBL:KRX10513.1}.
FT DOMAIN 48..415
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 424 AA; 47674 MW; 9CEDF4CD853B87D6 CRC64;
MQNKQILKTI QKSAHFQKNF STVKELVGKN PVRGFALEFA ELQKKNPRCI NLALGVPMDP
TPHQIIDAKI DYVKFSGETG NNGYGDPRGI ESLRVNLSKH IQEQYKVSPK HLNENNINIV
PGGTSNAISL TVEKLVRNDM GKGEIIVLAP FFGPYNGMIK LSNGVPVIID TDEQLQPDLK
KIEEAITPNT RGILINSPNN PSGKIYPKET IRKIVEIAAK HNCAVISDEI YEKFSYIESK
PHTTICSFYE DFPQVNLIQV NSASKTYGMI GDRIGYIISN QLDFIEDITI TLGYRFASSP
YLPQYAFDAV FSNWDEISQR IEATRILYKQ KAEFLVKGLR EIGFNAQDLE GGMFAMTEVK
SLTGMDGHQL SRYFIEQDAP VAVYPGGFFG ESFGNYLRFT TCPTMVTLER GLDQIDKYVK
QIKK
//
