ID C3JFG0_RHOER Unreviewed; 437 AA.
AC C3JFG0;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:EEN89747.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:EEN89747.1};
GN ORFNames=RHOER0001_2946 {ECO:0000313|EMBL:EEN89747.1};
OS Rhodococcus erythropolis SK121.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=596309 {ECO:0000313|EMBL:EEN89747.1, ECO:0000313|Proteomes:UP000005836};
RN [1] {ECO:0000313|EMBL:EEN89747.1, ECO:0000313|Proteomes:UP000005836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK121 {ECO:0000313|EMBL:EEN89747.1,
RC ECO:0000313|Proteomes:UP000005836};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (APR-2009) 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}.
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:EEN89747.1}.
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DR EMBL; ACNO01000001; EEN89747.1; -; Genomic_DNA.
DR RefSeq; WP_003939848.1; NZ_ACNO01000001.1.
DR AlphaFoldDB; C3JFG0; -.
DR Proteomes; UP000005836; Unassembled WGS sequence.
DR GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Transferase {ECO:0000313|EMBL:EEN89747.1}.
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 219
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 437 AA; 46303 MW; 85D780FC63C8FDA3 CRC64;
MSENTPVDTD PTADWSFETK QVHAGQGPDS ATNARALPIY QTTSYVFDNT DHAAALFGLA
EPGNIYTRIM NPTQDAVEQR IAALEGGVAA LLVASGQAAE SFAILNLAEA GDHIVSSPRL
YGGTYNLFHY TLPKLGITVD FVEDPDNLDH WREAIRPNTK AFYGETISNP KNDVFDIPGI
SAVAHEHGIP LIVDNTVATP YLIQPLKHGA DIVVHSATKY LGGHGTAIAG VIVDGGTFDW
TQGRHTNFTT PDPSYHGVTF ADLGAPAYAL KARVQLLRDL GSAIAPFNAF LISQGIETLS
LRIERHVSNA QKVAEFLEGR AEVTSVAYAG LESSPWHERG KQLAPKGTGA IVAFELAGGV
DAGKKFVNAL TLHSHVANIG DVRSLVIHPA STTHSQLTPE EQLASGVTPG LVRLAVGIEG
IDDILADLET GLAAAAS
//
