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Database: UniProt
Entry: A0A100IP60_ASPNG
LinkDB: A0A100IP60_ASPNG
Original site: A0A100IP60_ASPNG 
ID   A0A100IP60_ASPNG        Unreviewed;       602 AA.
AC   A0A100IP60;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:GAQ44794.1};
GN   ORFNames=ABL_07455 {ECO:0000313|EMBL:GAQ44794.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ44794.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ44794.1}.
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DR   EMBL; BCMY01000013; GAQ44794.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100IP60; -.
DR   PaxDb; 5061-CADANGAP00009255; -.
DR   VEuPathDB; FungiDB:An11g11160; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1095019; -.
DR   VEuPathDB; FungiDB:ATCC64974_95680; -.
DR   VEuPathDB; FungiDB:M747DRAFT_231440; -.
DR   OMA; MVLNPQS; -.
DR   Proteomes; UP000068243; 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; PTHR42699; -; 1.
DR   PANTHER; PTHR42699:SF1; CYSTATHIONINE GAMMA-SYNTHASE-RELATED; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   REGION          184..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   602 AA;  66784 MW;  7A735E15DF5A5C88 CRC64;
     MIQDIGGPVP PHTDHAVSVS LPTWKANVAY EEGESWVVNK MQCGYPRFFI HPIIQDLARE
     IVRRYGSPEL ETAILFPSLK TSGVCYSFLK SKIQAEEPCN VRTIHFALPI QGEDAPSGTD
     LILSCVIYPI QYAPIAKQVW QHTGNGISSR RAEFCLNALR DGSLVERKPV AQSIASPRFF
     KGPRRYQGRE SISGKSQGNG THARDSTTGT ITTTSSMQDG REHVQFIEER FGRNLSTSLA
     GQARLAVRRR IAGVLTADVE LNEALEEESG EGRVAGLTES DVFLFPTGMS SIFNAHQMLM
     VAKGDMKSIC FGFPYTDTLK ILQKWGPGCL FYGHGSSEDL DDLESRLLKG ERFLALFTEF
     PGNPLLKAPD LKRIRSLADR YNFAVVVDET VGNFLNINVL PYADIVVSSL TKIFSGDSNV
     MGGSAVLNPH GHHYGSLKDI FAREYEDNLW AEDAVFLERN SRDFISRIDK INKTTEDITA
     MLEDSPLVKK VYYPKYNSSR PLYEAFRNKN GGYGGLFSVT FHSTAAAVAF FDQLEVLKGP
     SLGTNFTLSC PYTLLAHYGE LEWASSFGVD FDLVRISVGL EDVSDLRQRF QQALNAVAEV
     NT
//
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