ID   B3QG70_RHOPT            Unreviewed;       433 AA.
AC   B3QG70;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:ACF01107.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:ACF01107.1};
GN   OrderedLocusNames=Rpal_2594 {ECO:0000313|EMBL:ACF01107.1};
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960 {ECO:0000313|EMBL:ACF01107.1, ECO:0000313|Proteomes:UP000001725};
RN   [1] {ECO:0000313|EMBL:ACF01107.1, ECO:0000313|Proteomes:UP000001725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1 {ECO:0000313|EMBL:ACF01107.1,
RC   ECO:0000313|Proteomes:UP000001725};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) 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; CP001096; ACF01107.1; -; Genomic_DNA.
DR   RefSeq; WP_012495826.1; NC_011004.1.
DR   AlphaFoldDB; B3QG70; -.
DR   KEGG; rpt:Rpal_2594; -.
DR   HOGENOM; CLU_018986_4_2_5; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000001725; Chromosome.
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   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   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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Transferase {ECO:0000313|EMBL:ACF01107.1}.
FT   MOD_RES         211
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   433 AA;  46341 MW;  5694C6906959BC85 CRC64;
     MFAQASTLDD NHAVQPLHPS TFVLRGARGR AGVSRRPSPR IDEGAAAPLQ FGNERLDARY
     RAVSHPVLRE LESRLAAFEG GASALAVASG QAASTFSVLN LAQAGDNFVT STGLYGGTWI
     LFDNTLRELG IEARFVDPSD PENFRRATDA RTRLYYAETL PNPKLEVFPI REVAAIGRSL
     GVPLVMDNTA VPGVVRPLDH GAAIVMYSTT KYIGGHGTTL GGAIIDGGNF PWQQHAERFP
     LLTAPDAVDP QVVWTDVARP FGPIAFSLRA RLKLLGDLGA GMAPIAVSQI LQGLETLPIR
     MEQHNANAIV VADYLKDHPK VAAVHFPGLQ SGELRRRADA SMRGGYGALI GFELRDGQAA
     GQRFIEALKL FYHVANIGDA RSLAIQPSAT THSQLSEQDQ LAAGVTPGFI RLSIGIEHPD
     DILADLAQAL DAA
//