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Database: UniProt
Entry: A0A1Q5U1M2_9EURO
LinkDB: A0A1Q5U1M2_9EURO
Original site: A0A1Q5U1M2_9EURO 
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
//
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