ID A0A1Q5U1M2_9EURO Unreviewed; 395 AA.
AC A0A1Q5U1M2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE RecName: Full=Trans-sulfuration enzyme {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENSUB_6369 {ECO:0000313|EMBL:OKP06379.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP06379.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKP06379.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP06379.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|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:OKP06379.1}.
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DR EMBL; MNBE01000598; OKP06379.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5U1M2; -.
DR STRING; 1316194.A0A1Q5U1M2; -.
DR OrthoDB; 5482552at2759; -.
DR Proteomes; UP000186955; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF84; ENZYME FAMILY PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G13810)-RELATED; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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:UP000186955}.
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 395 AA; 43400 MW; A4FE133D62104D4A CRC64;
MAPLNNSHPA TQALHADDRL NLVHDVAPPI HLSTTFRYSN TPDELVLSED PVAEFNGKNY
VYSREFAPNA TRFEAVLSPL LKGHAVSYAT GLAALHAALT LLNPRQISVG EGYHGSHEVI
SVVSRLSGLK KLPIDCPTES LNKGDVILLE TPINPFGTAY NIEEYAQKAH SRGAFLIVDS
TFAPPGLQDP FLWGADIVMH SGSKYFGGHS DMLCGVLAVK RDDWAKQLFE DRMALGNVLG
NLEGWLGTRS LRTLEVRVQR ASENSAKVIS WLNDALNAPS PAPGSEEAVV QTVLKKIYHA
SLQDEPWLKK QMPNGFGPVF SVILHSEDFA RTLPSKLHFF QHATSLGGVE SLIEWRALSD
ARVDRKLLRI SVGLENWEDL KNDLLQAFKS LAGAR
//