ID   A0A0A7I304_9BIFI        Unreviewed;       437 AA.
AC   A0A0A7I304;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:AIZ14276.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:AIZ14276.1};
GN   ORFNames=AH68_03490 {ECO:0000313|EMBL:AIZ14276.1};
OS   Bifidobacterium catenulatum PV20-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1447716 {ECO:0000313|EMBL:AIZ14276.1, ECO:0000313|Proteomes:UP000030625};
RN   [1] {ECO:0000313|EMBL:AIZ14276.1, ECO:0000313|Proteomes:UP000030625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV20-2 {ECO:0000313|EMBL:AIZ14276.1,
RC   ECO:0000313|Proteomes:UP000030625};
RX   PubMed=25614572;
RA   Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Jans C.,
RA   Stevens M.J.;
RT   "Complete and Assembled Genome Sequence of Bifidobacterium kashiwanohense
RT   PV20-2, Isolated from the Feces of an Anemic Kenyan Infant.";
RL   Genome Announc. 3:0-0(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; CP007456; AIZ14276.1; -; Genomic_DNA.
DR   RefSeq; WP_039197671.1; NZ_CP007456.1.
DR   AlphaFoldDB; A0A0A7I304; -.
DR   STRING; 1447716.AH68_03490; -.
DR   KEGG; bka:AH68_03490; -.
DR   HOGENOM; CLU_018986_4_0_11; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000030625; 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   Transferase {ECO:0000313|EMBL:AIZ14276.1}.
FT   MOD_RES         211
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   437 AA;  47516 MW;  86B07BFD3C7D2233 CRC64;
     MADSKNYRFE TLQLHVGQEQ ADPATDSRAV PIYQTTSYVF HNFDHAEARF GLADPGNIYG
     RLTNSTQSVF EDRIAALEGG TAGLAVASGA AAVEYAVRNI TQSGDHIVAA KNIYGGTFNL
     LRHTLPRDGI TTTFVSAENP QEFEDAIQEN TKLVYFETFG NPNADLPDFE AITAIAHKHH
     LPVIVDNTFA TPYLFRPLEH GADVVVESAT KFIGGHGTTL GGVIVEGGNF NWAEVPGKFP
     TLTEPDPSYH GLNFYEALGG SAFVTRIRAI LLRDTGATLS PFAAFLLLQG TETLSLRVER
     HVENALKVID YLKTVPEVES ISHPSIEGRK DNELYKKYFP NGGGSIFTFD IKGGKDAARV
     FIDNLHLFSL LANVADAKSL VIHPASTTHS QETVEELEDQ GIHQGTIRLS IGTENIEDIL
     DDLKGGFAAL RESGLAK
//