ID A0A086ZUN6_9BIFI Unreviewed; 438 AA.
AC A0A086ZUN6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:KFI50236.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:KFI50236.1};
GN ORFNames=BCAL_2224 {ECO:0000313|EMBL:KFI50236.1};
OS Bifidobacterium callitrichos DSM 23973.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437609 {ECO:0000313|EMBL:KFI50236.1, ECO:0000313|Proteomes:UP000029072};
RN [1] {ECO:0000313|EMBL:KFI50236.1, ECO:0000313|Proteomes:UP000029072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23973 {ECO:0000313|EMBL:KFI50236.1,
RC ECO:0000313|Proteomes:UP000029072};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFI50236.1}.
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DR EMBL; JGYS01000030; KFI50236.1; -; Genomic_DNA.
DR RefSeq; WP_043166599.1; NZ_JGYS01000030.1.
DR AlphaFoldDB; A0A086ZUN6; -.
DR STRING; 1437609.BCAL_2224; -.
DR eggNOG; COG2873; Bacteria.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000029072; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:KFI50236.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Transferase {ECO:0000313|EMBL:KFI50236.1}.
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 438 AA; 47604 MW; 23ABFD8F56A966FC CRC64;
MAEKNKNYRF ETLQLHVGQE QADPATDSRA VPIYATTSYV FHNFDHAEAR FGLADPGNIY
GRLTNSTQGV FEDRIAALEG GTAGIAVASG AAAVEYAVRN ITQSGDHIVS SKNIYGGTFN
LLKHTLPRDG ITTTFVDPEV PQNFEDAIQE NTKLVYFETF GNPNADLPDF EAISAIAHKH
HLPVIVDNTF ATPYLFRPLE HGADVVVESA TKFIGGHGTT LGGVVVEGGN FNWAEVPGKF
PTLTEPDPSY HGLNFYEALG GAAFVTRIRA ILLRDTGATL SPFAAFLLLQ GTETLSLRVE
RHVENALKVV EYLQTVPEVE SVSHPSIEGR RDHALYEKYF PNGAGSIFTF DIKGGKDAAR
VFIDNLHLFS LLANVADVKS LVIHPASTTH SQETLEELED QGIHQGTIRL SIGTENIEDI
LDDLKGGFEA VRASGLAK
//
