ID A0A0S9N128_9BURK Unreviewed; 430 AA.
AC A0A0S9N128;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:KQP38958.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:KQP38958.1};
GN ORFNames=ASF44_11035 {ECO:0000313|EMBL:KQP38958.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP38958.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP38958.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP38958.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP38958.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP38958.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQP38958.1}.
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DR EMBL; LMNA01000025; KQP38958.1; -; Genomic_DNA.
DR RefSeq; WP_056901046.1; NZ_LMNA01000025.1.
DR AlphaFoldDB; A0A0S9N128; -.
DR STRING; 1736318.ASF44_11035; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000051759; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000051759};
KW Transferase {ECO:0000313|EMBL:KQP38958.1}.
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 430 AA; 46031 MW; 58F4DCE336722391 CRC64;
MSKDWKFETL SVHAGYSPDP TTRAVVPPIY QTAAYAFDSA QHGADLFDLK VPGNIYTRIM
NPTQDVLEQR VAALEGGIAA LALASGQAAV TYAIQTIAEA GDNIISSTAL YGGTYNLFAH
TLPQFGITTR FADHRDPASF DKLFDDRTKA VFVESLGNPA GNVTDIATIA AIAHRHGVPL
IVDNTVPSPY LSRPIEHGAD IVVHSLTKYL GGHGNSIGGA IVDSGKFPWA QHKARFKRLN
EPDVSYHGVV YTEALGPAAY IGRARVVPLR NTGAAISPFN AFLILQGIET LALRMDRITA
NTLAIAQHLQ GHAKVSWVNY AGLEDHPEHA LARKYLRGTG SGILTFGVQG HGGGREAGAR
FLDALGLFTR LVNIGDVRSL ATHPASTTHR QLSPEELAKT GVTEETVRLS VGIEHIDDLK
ADLEQALAAV
//
