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Database: UniProt
Entry: A0A0V0Q8S1_PSEPJ
LinkDB: A0A0V0Q8S1_PSEPJ
Original site: A0A0V0Q8S1_PSEPJ 
ID   A0A0V0Q8S1_PSEPJ        Unreviewed;       799 AA.
AC   A0A0V0Q8S1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Pyridoxal phosphate-dependent transferase {ECO:0000313|EMBL:KRW98636.1};
GN   ORFNames=PPERSA_02784 {ECO:0000313|EMBL:KRW98636.1};
OS   Pseudocohnilembus persalinus (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC   Pseudocohnilembus.
OX   NCBI_TaxID=266149 {ECO:0000313|EMBL:KRW98636.1, ECO:0000313|Proteomes:UP000054937};
RN   [1] {ECO:0000313|EMBL:KRW98636.1, ECO:0000313|Proteomes:UP000054937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=36N120E {ECO:0000313|EMBL:KRW98636.1};
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:KRW98636.1}.
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DR   EMBL; LDAU01000233; KRW98636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0Q8S1; -.
DR   EnsemblProtists; KRW98636; KRW98636; PPERSA_02784.
DR   InParanoid; A0A0V0Q8S1; -.
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; PTHR43807; FI04487P; 1.
DR   PANTHER; PTHR43807:SF20; FI04487P; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW   Transferase {ECO:0000313|EMBL:KRW98636.1}.
FT   DOMAIN          394..780
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   COILED          210..237
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   799 AA;  93499 MW;  9CBB8FBE7BCC2DFC CRC64;
     MIYQQILENQ QQQYCQQSGH QNSRLIYYCF TQDKKKLFQC EICCQENQKL ASLKFNNQKF
     DIDKILDNKI LDNWPPIYNK NLKKWVKEIQ EQGSISASIE QVENDIFKNI EQYFSLKIKE
     ITDILLKIKK QKQGQFSQQI KIWKNGNWPN NLQNIYDIEN IKNDINKYFE GNIQLDQVYE
     NQKKFIGKFK QEEDLYNIMY QFDQQKRQIY DSMQKLIDEF DNKFKDVKKK LQIFQNESVL
     KYRNKCEFLF YRSSFNQMQE EILMQKNSCK KITFLDRHYG YGGEFWKQVY SQILEKNMTY
     QIKAKIKSDG NHEKIGVVAG VGCHSDRDGD LYNQKYNYIS IINCLSKPEG NNNFRFDGQY
     PIDFINNDRA KRLTGLDRPT IWTKFGALVA ETQPVNLGQG FPQWNPPQFF LDALMEANKS
     QSQQYTRAFG TPSLTKSISD FYSPIFNREL DPNNNIVVCN GGVAVLNSIF SSMINPGEEV
     ILLDPSYDCY AAQIQIAGGV VKSVPMKPKH LQSKQELLNK KNRYEIGEND LWEIDFDLLK
     KTFNEKTRAI VINSPHNPTG KIFSEEEYKK IAEIVKQNDI CIVIEDQVYE HLTFETCEPF
     QNPRMAKVDG MWERTVNVSS AGKLFSATGI RVGWAIGPNS IIKCMQGFHQ YNVFCMHGPT
     QEAVAISLQQ SKTNGYFQDL NQKMMGLRNL FIDQLIEGYQ DFNIWIPQGG YFILCDISKI
     QVPEKYYTNP LFSDYDISKD LAFSFYQANE TKVLPIPCSI FYQKEHKEEG QNFVRYAICK
     EKETLLEAGQ KLKKQLQQQ
//
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