ID   A0A0P0SB71_9PSEU        Unreviewed;       455 AA.
AC   A0A0P0SB71;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Cystathionine beta-synthase {ECO:0000256|ARBA:ARBA00026192};
DE            EC=4.2.1.22 {ECO:0000256|ARBA:ARBA00012041};
DE   AltName: Full=Beta-thionase {ECO:0000256|ARBA:ARBA00030337};
DE   AltName: Full=Serine sulfhydrase {ECO:0000256|ARBA:ARBA00031579};
GN   ORFNames=AD017_09460 {ECO:0000313|EMBL:ALL81370.1};
OS   Pseudonocardia sp. EC080619-01.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL81370.1, ECO:0000313|Proteomes:UP000066228};
RN   [1] {ECO:0000313|EMBL:ALL81370.1, ECO:0000313|Proteomes:UP000066228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL81370.1,
RC   ECO:0000313|Proteomes:UP000066228};
RX   PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA   Van Arnam E.B., Sit C.S.;
RT   "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL   J. Am. Chem. Soc. 137:14272-14274(2015).
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};
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR   EMBL; CP012184; ALL81370.1; -; Genomic_DNA.
DR   RefSeq; WP_010242993.1; NZ_CP012184.1.
DR   AlphaFoldDB; A0A0P0SB71; -.
DR   STRING; 1096856.AD017_09460; -.
DR   KEGG; pecq:AD017_09460; -.
DR   PATRIC; fig|1096856.3.peg.1992; -.
DR   OrthoDB; 9805733at2; -.
DR   UniPathway; UPA00136; UER00201.
DR   Proteomes; UP000066228; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004122; F:cystathionine beta-synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProt.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
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   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR005857; Cysta_beta_synth.
DR   InterPro; IPR001216; P-phosphate_BS.
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; PF00571; CBS; 2.
DR   Pfam; PF00291; PALP; 1.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   4: Predicted;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW   ProRule:PRU00703}; Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000066228}.
FT   DOMAIN          335..397
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          405..455
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   455 AA;  47979 MW;  87CFC3AE9AD0AC95 CRC64;
     MRYVEHVVDL VGNTPLVRLG ATAEGIAPPV LAKVEYLNPG GSVKDRIALR MVEAAEASGE
     LRPGGTIVEP TSGNTGVGLA MVAQRKGYHC VFVCPDKVGE DKRNVLQAYG AEVVVCPTAV
     DPDHPDSYYR TSDRLVEEID GAWKPNQYAN PANPESHYHS TGPEIWEQTD GKITHFVAGI
     GTGGTISGIG RYLKEVSGGA VKIIGADPEG SVYSGGTGRP YLVEGVGEDF WPTTYDRDVC
     DEIVAVSDTD SFHMTRRLAR EEALLVGGSC GMAAVAALRV AATLPADAVV VVLLPDGGRG
     YLGKVFNDRW MASYGFLPPS EGATIGDVLR RKDGSMPALV HAHPNETVAD AALYLREFGV
     SQMPVVKAEP PVMAAEVAGA VVERDLLDAL FTGRAQLADR LEDHMSPPLP TLGAGESVQD
     AMEAFAKADA ALVLMDGKPA GVVTRSDVIG FLGNG
//