ID K9FXQ0_PEND2 Unreviewed; 671 AA.
AC K9FXQ0;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Serine palmitoyltransferase 2, putative {ECO:0000313|EMBL:EKV05826.1};
GN ORFNames=PDIG_80230 {ECO:0000313|EMBL:EKV05826.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV05826.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:EKV05826.1}.
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DR EMBL; AKCT01000296; EKV05826.1; -; Genomic_DNA.
DR AlphaFoldDB; K9FXQ0; -.
DR STRING; 1170229.K9FXQ0; -.
DR eggNOG; KOG1357; Eukaryota.
DR HOGENOM; CLU_015846_7_2_1; -.
DR InParanoid; K9FXQ0; -.
DR OMA; NDCFSRP; -.
DR OrthoDB; 9643at2759; -.
DR Proteomes; UP000009882; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd06454; KBL_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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR PANTHER; PTHR13693:SF3; LD36009P; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009882};
KW Transferase {ECO:0000313|EMBL:EKV05826.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 147..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..602
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 74117 MW; 38A313B22E6B6C16 CRC64;
MPRRFSSNSS NDTSTNPPFF SPSSGKGGIS IKAPTVKSNR LSQLFSSSPK SRTETVQGGH
SQPSNSSPPI SLASLSLPTI SLSTATADNP SMDELPTTLF QPPTPEEARR LAKQHAQFGP
IGHPSHRYSS RHPGGVFPEP VMDEPPYYYL LTTYISYLIL IAFGHVRDFF GKRFREENYR
HLKPRNGYAA LNNDFDNFYV RRLKLRINDC FERPVTGVPG RTITLIDRGT DDHNQHFFLT
GTTTDTLNLS SYNYLGFAQS DGPCADIAEE SIRKYGIAAP STRAESGTQD MHVEVEDLIA
RFVGKEASMV FSMGFGTNAT VFPALVSKGC LLISDELNHA SIRFGARLSG ASIAMFKHND
MKDLELRLRE AISQGQPRTH RPWKKILVVV EGLYSMEGSM CNLPGLVQLK RRYKFNLFVD
EAHSVGAIGP KGRGVCDYFG IDTAEVDILM GTLTKSFGAN GGYIAADKVM IDQLRAINPG
VYYGESPAPA VLSQIASALR IISGELVPGQ GEERLQRLAF NSRYLRLGLK RLGFIVYGHD
DSPIVPLLLF NPAKMPAFSH EMLRRKISVV VVGYPATPLV SSRARFCVSA AHTKDDLDRV
LAACDEIGNI LQLKFSTGIA GGALPAAEQQ TPPPELEKEW HRKRSEHISP PRWRVEDVIR
RGVQDVKNPL Y
//