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
//