ID   A0A239A519_9ACTN        Unreviewed;       465 AA.
AC   A0A239A519;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=SAMN04488107_0566 {ECO:0000313|EMBL:SNR90747.1};
OS   Geodermatophilus saharensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1137994 {ECO:0000313|EMBL:SNR90747.1, ECO:0000313|Proteomes:UP000198386};
RN   [1] {ECO:0000313|EMBL:SNR90747.1, ECO:0000313|Proteomes:UP000198386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45423 {ECO:0000313|EMBL:SNR90747.1,
RC   ECO:0000313|Proteomes:UP000198386};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000256|ARBA:ARBA00007103}.
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DR   EMBL; FZOH01000001; SNR90747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239A519; -.
DR   OrthoDB; 9805733at2; -.
DR   UniPathway; UPA00136; UER00201.
DR   Proteomes; UP000198386; Unassembled WGS sequence.
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   CDD; cd04608; CBS_pair_CBS; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   InterPro; IPR046353; CBS_C.
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; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
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}.
FT   DOMAIN          343..404
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   REGION          141..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   465 AA;  49149 MW;  CF330BF7680B7F1D CRC64;
     MQYAESVVDL IGGTPLVRLS RVTRDLGPDA PLVLAKVEYL NPGGSVKDRI AVRMVDDAEA
     SGELEPGGTI VEPTSGNTGI GLALVAQQRG YRCVFVCPDK VSQDKINVLR AYGAEVHVCP
     TAVDPSDPRS YYSVSDRLAR ETPGGWKPDQ YANPANPRSH YETTGPEIWE QTEGKVTCFV
     TGVGTGGTIS GIGRYLKEAS DGRVRVVGVD PEGSVYSGGT GRPYLVEGVG EDFWPDAYDR
     GIADEIVPVS DADSFHMTRR LAREEGLLVG GSCGMAVAGA LRAAEKLTKD DVVVVLLPDG
     GRGYLNKIFN DQWMADYGFL DVTTGGETVG ELLEAKSRDG GGATPVLVHT HPNETVRDAI
     DILREYGVSQ MPVVKAEPPV TAGEVVGSVD EKVLLDALFA GRASLSDRVE KHMSAPLPII
     GSGEPVSAAV AEFGEADALI VHVDGKPAGV VTRQDVLGHL AGVTR
//