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Database: UniProt
Entry: A0A0G3CJY0_9GAMM
LinkDB: A0A0G3CJY0_9GAMM
Original site: A0A0G3CJY0_9GAMM 
ID   A0A0G3CJY0_9GAMM        Unreviewed;       422 AA.
AC   A0A0G3CJY0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:AKJ42269.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:AKJ42269.1};
GN   ORFNames=QQ39_09350 {ECO:0000313|EMBL:AKJ42269.1};
OS   Pragia fontium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Pragia.
OX   NCBI_TaxID=82985 {ECO:0000313|EMBL:AKJ42269.1, ECO:0000313|Proteomes:UP000068021};
RN   [1] {ECO:0000313|EMBL:AKJ42269.1, ECO:0000313|Proteomes:UP000068021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=24613 {ECO:0000313|EMBL:AKJ42269.1,
RC   ECO:0000313|Proteomes:UP000068021};
RX   PubMed=26159528;
RA   Snopkova K., Sedlar K., Bosak J., Chaloupkova E., Provaznik I., Smajs D.;
RT   "Complete Genome Sequence of Pragia fontium 24613, an Environmental
RT   Bacterium from the Family Enterobacteriaceae.";
RL   Genome Announc. 3:e00740-15(2015).
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; CP010423; AKJ42269.1; -; Genomic_DNA.
DR   RefSeq; WP_047781004.1; NZ_CP010423.1.
DR   AlphaFoldDB; A0A0G3CJY0; -.
DR   STRING; 82985.QQ39_09350; -.
DR   KEGG; pfq:QQ39_09350; -.
DR   PATRIC; fig|82985.3.peg.1956; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000068021; 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   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:UP000068021};
KW   Transferase {ECO:0000313|EMBL:AKJ42269.1}.
FT   MOD_RES         204
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   422 AA;  45421 MW;  37179E014EEDFA8F CRC64;
     MKDATLALHH GFQCDPTTKS VAVPIYQTVA YEFDNAQHGA DLFNLAVPGN IYTRIMNPTN
     DILEKRMAAL EGGVAGLVVS AGSAAISYAI QTLAQVGDNI VSTPQLYGGT YTLFAHMLPG
     FGINVKFARD DSPQAIAELI DENTKAVYCE SIGNPAGNIV DIEGIAEVAH ARGVPLIVDN
     TVASPVLCKP IQFGADIVVH SITKYVGGHG NSLGGVIVDS GKFPWTEHKE RFPMFSSPEP
     AYHGVIYTES FGAAAFVARA RTVPLRNCGA ALSPMNAFLL LQGLETLSLR MERHVENARK
     VANYLKQHDK VAWVSYAGLP EHPHYALAQK YMQGTPSAIL SFGLKGGYQA GVQFYDALQI
     FKRLVNIGDA KSLACHPAST THRQMSEEEQ AKAGVKPEMI RLSIGIEAIE DILADLEQAL
     AD
//
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