ID   D2Q947_BIFDB            Unreviewed;       336 AA.
AC   D2Q947;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=cystathionine beta-synthase {ECO:0000256|ARBA:ARBA00012041};
DE            EC=4.2.1.22 {ECO:0000256|ARBA:ARBA00012041};
GN   Name=cysK {ECO:0000313|EMBL:ADB09333.1};
GN   OrderedLocusNames=BDP_0670 {ECO:0000313|EMBL:ADB09333.1};
OS   Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB09333.1, ECO:0000313|Proteomes:UP000008693};
RN   [1] {ECO:0000313|EMBL:ADB09333.1, ECO:0000313|Proteomes:UP000008693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC   {ECO:0000313|Proteomes:UP000008693};
RX   PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA   Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA   Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA   Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA   Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT   "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT   adaptation to the human oral cavity.";
RL   PLoS Genet. 5:E1000785-E1000785(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homocysteine + L-serine = H2O + L,L-cystathionine;
CC         Xref=Rhea:RHEA:10112, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:58161, ChEBI:CHEBI:58199; EC=4.2.1.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00001175};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; CP001750; ADB09333.1; -; Genomic_DNA.
DR   RefSeq; WP_003836955.1; NC_013714.1.
DR   AlphaFoldDB; D2Q947; -.
DR   STRING; 401473.BDP_0670; -.
DR   GeneID; 69535004; -.
DR   KEGG; bde:BDP_0670; -.
DR   eggNOG; COG0031; Bacteria.
DR   HOGENOM; CLU_021018_1_0_11; -.
DR   Proteomes; UP000008693; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004122; F:cystathionine beta-synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:InterPro.
DR   CDD; cd01561; CBS_like; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR005857; Cysta_beta_synth.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01137; cysta_beta; 1.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF194; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008693};
KW   Transferase {ECO:0000313|EMBL:ADB09333.1}.
FT   DOMAIN          9..299
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   336 AA;  36363 MW;  2723187C57730A58 CRC64;
     MTIHDSLAEL IGNTPLVKLN HVTDGIKATI AVKVEYFNPG GSSKDRIAER IIDAAERSGE
     LKPGGVIVEP TSGNTGVGLA LVAQQRGYRT IFTLPDKVSE AKRAVLRAYG AEVVVTPTDA
     GPDDPRSYYQ VAERLAKAIP GGYRPNQYDN PNGPESHYHT TGPEIWQATD HKITHFVAGI
     GTGGTISGTG RYLKDVSDGA VQVIGADPEG SIYSNPDDVH QYKIEGVGED FYPKAFDRGL
     PDEIVQVNDA EAFEMTRRLA GEEGLLVGGS SGMAVVAAIK YAREHDLDER QTVVVLLPDS
     GRGYMEKIFD DDWMRANGFA DIVERTTKPS LAEQYL
//