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
//