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Database: UniProt
Entry: F3ZCY3_9ACTN
LinkDB: F3ZCY3_9ACTN
Original site: F3ZCY3_9ACTN 
ID   F3ZCY3_9ACTN            Unreviewed;       475 AA.
AC   F3ZCY3;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Putative O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:EGJ76443.1};
GN   ORFNames=STTU_3654 {ECO:0000313|EMBL:EGJ76443.1};
OS   Streptomyces sp. Tu6071.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ76443.1};
RN   [1] {ECO:0000313|EMBL:EGJ76443.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ76443.1};
RA   Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA   Gunther S.;
RT   "Genome sequence of Streptomyces sp. Tu6071.";
RL   Submitted (APR-2011) 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|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; CM001165; EGJ76443.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3ZCY3; -.
DR   HOGENOM; CLU_018986_4_0_11; -.
DR   Proteomes; UP000003955; Chromosome.
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:0009058; P:biosynthetic process; IEA:UniProt.
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   Transferase {ECO:0000313|EMBL:EGJ76443.1}.
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         252
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   475 AA;  50414 MW;  A1BFA154CD6F0A5E CRC64;
     MPGPARPPRA SLVGRPPSSP YDRPDVRPPS RTRSAMSTQP AESAAESWSF ETKQVHAGAV
     PDPATGARAT PIYQTSSFVF RDTRHAADLF SLAEPGNIYT RIHNPTQDVF EQRIAALEGG
     VGAVAVASGQ AAETLALLTL ARAGDHVVSS ASLYGGTYNL FRHTLPRLGI EVSFVDDPDD
     PEAWRAAARP HTKAFFAETL GNPRGNVLDI RAVSDVAHAV GVPLVVDNTV PTPYLLRPLE
     HGADIVVHSA TKFLGGHGTA IAGVVVDGGT FDFGAHAARF PDFSEPDPSY HGLQYWPALG
     PGAYAVKLRV QLLRDLGPAL SPHSAFLLLQ GVETLSLRIE RHTANAAALA TWLEGRDEVS
     AVHYAGLESS PWYEKGRTYL PRGAGAIVSF ELRGGVEAGK RFVDAVELFS HLANIGDVRS
     LIIHPASTTH SQLGEEELRA TGTAPGLVRL SVGIENLADL KADLEAGFRA AKGAA
//
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