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Database: UniProt
Entry: A0A109J700_9BRAD
LinkDB: A0A109J700_9BRAD
Original site: A0A109J700_9BRAD 
ID   A0A109J700_9BRAD        Unreviewed;       431 AA.
AC   A0A109J700;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:KWV43542.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:KWV43542.1};
GN   ORFNames=AS156_24795 {ECO:0000313|EMBL:KWV43542.1};
OS   Bradyrhizobium macuxiense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV43542.1, ECO:0000313|Proteomes:UP000057737};
RN   [1] {ECO:0000313|EMBL:KWV43542.1, ECO:0000313|Proteomes:UP000057737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR 10303 {ECO:0000313|EMBL:KWV43542.1,
RC   ECO:0000313|Proteomes:UP000057737};
RA   Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT   "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT   from nodules of Centrolobium paraense.";
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:KWV43542.1}.
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DR   EMBL; LNCU01000132; KWV43542.1; -; Genomic_DNA.
DR   RefSeq; WP_066516125.1; NZ_LNCU01000132.1.
DR   AlphaFoldDB; A0A109J700; -.
DR   OrthoDB; 7316598at2; -.
DR   Proteomes; UP000057737; 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   Transferase {ECO:0000313|EMBL:KWV43542.1}.
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   431 AA;  45814 MW;  EB31DA6E5C7CAC7F CRC64;
     MPAPKPPAFE TLSLHAGQRP DPLTGARAVP IYQTTSYVFQ DADHAAALFN LERAGHIYTR
     ISNPTTSVLE ERIAALECGV GAICTASGMA AMHLAIATLL NAGDHIVASA SLYGGTINLL
     AHTLPRFGIT TTFVKPCALD DFRAAIKPNT RLVIGETIGN PGLEVLDIPA VAQIAHDAKI
     PLLIDNTFAT PYLSQPIELG ADITMNSATK WMGGHGIAIG GVIVDGGRFD WRASGKFPQL
     TEPYAGYHGI VFDEQFGKAA FIMRARTEGL RDFGACLSPT NAFQLLQGIE TLGVRMDRHM
     SNTHAVLEAL AANKAVDWVL HPALESHPDH ALAKKLLPRG AGSIISFGIK GGRAAGKKFI
     ESLKLISHLA NVGDAKTLVI HPASTTHQQM DAEQLKAAGI GEELVRLSVG IETAQDIIDD
     LGQALRASQR T
//
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