ID A0A0A2KYS2_PENIT Unreviewed; 436 AA.
AC A0A0A2KYS2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Pyridoxal phosphate-dependent transferase, major region, subdomain 2 {ECO:0000313|EMBL:KGO72078.1};
GN ORFNames=PITC_075440 {ECO:0000313|EMBL:KGO72078.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO72078.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO72078.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO72078.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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:KGO72078.1}.
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DR EMBL; JQGA01000901; KGO72078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KYS2; -.
DR STRING; 40296.A0A0A2KYS2; -.
DR HOGENOM; CLU_018986_4_0_1; -.
DR OMA; NAFQIIQ; -.
DR OrthoDB; 6018at2759; -.
DR PhylomeDB; A0A0A2KYS2; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR PANTHER; PTHR43797:SF2; HOMOCYSTEINE_CYSTEINE SYNTHASE; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Transferase {ECO:0000313|EMBL:KGO72078.1}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 436 AA; 47027 MW; 68C9722273A33204 CRC64;
MSENLHFDTL QLHAGHEPDS ATNSRAVPIY ATSSYVFNDS AHGARLFGLK EFGNIYSRIM
NPTVDVFEKR IAALEGGVAA VAASSGQAAQ FMAITALAHA GDNIVSTSNL YGGTYNQFKV
TLPRMGITTK FVQGDSPEDI AAAIDDRTKA VYLESIGNPR YNVPDFEAIA KAAHEKGVPV
VVDNTFGAGG YFVRPIDHGA DIVVHSATKW IGGHGTTIGG VVIDSGKFDW GKNAARFPQF
VKPSEGYHGL KFWETFGSLA YALRVRVEML RDLGSTLNPF AAQQLILGLE TLSLRCERHA
TNAAALAKWL QTNENVSWVS YLGLEDHPSH ELAKKYLPRG FGGVLSVGIK GGATAGAQVV
DNFKLISNLA NVGDSKTLAI HPWSTTHEQL SEQERRDSGV KEDAIRISVG TEYIGDIIAD
FEQSFQASKA LPDRTA
//
