ID B6HAD5_PENRW Unreviewed; 392 AA.
AC B6HAD5;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE SubName: Full=Pc16g12440 protein {ECO:0000313|EMBL:CAP93914.1};
GN ORFNames=Pc16g12440 {ECO:0000313|EMBL:CAP93914.1}, PCH_Pc16g12440
GN {ECO:0000313|EMBL:CAP93914.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP93914.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP93914.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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}.
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DR EMBL; AM920431; CAP93914.1; -; Genomic_DNA.
DR RefSeq; XP_002561543.1; XM_002561497.1.
DR AlphaFoldDB; B6HAD5; -.
DR STRING; 500485.B6HAD5; -.
DR GeneID; 8314969; -.
DR KEGG; pcs:Pc16g12440; -.
DR VEuPathDB; FungiDB:PCH_Pc16g12440; -.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_3_0_1; -.
DR OMA; DWTKQLF; -.
DR OrthoDB; 5482552at2759; -.
DR BioCyc; PCHR:PC16G12440-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c16.
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:UP000000724}.
FT MOD_RES 203
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 392 AA; 42962 MW; 65C86105FDBCBE4E CRC64;
MTSNNAHPST KALHADDVLN LVTDVAPPIH LSTTFRYPND PDQLVPSEDP VDEFNGKNYV
YSREFAPNAT RFESVLSSLL GGRAVSYSTG LAALHAALTL LNPRRISVGE GYHGSHEVIS
VVSRLSGLQK LPLDCPAESL DAGDVILLET PVNPLGTAFS IEEHAHKAHS RGAFLIVDST
FAPPGLQDPL LWGADIVMHS GSKYFGGHSD MLCGVLATKR ADWTKQLFED RIALGSVMGN
MESWLGIRSL RTLEVRVQRA SQNSAKLISW LHAAMQASSP AVGSEEMIVQ SVLKKIYHAS
LQDEPWLQKQ MPNGFGPVFS IVLDNEEFAK VLPTKLHFFQ HATSLGGVES LIEWRALSDP
RVDRKLLRVS VGLENWEDLK NDLLQAFKSL LG
//
