ID A0A2A9E1E0_9MICO Unreviewed; 465 AA.
AC A0A2A9E1E0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=ATL42_0296 {ECO:0000313|EMBL:PFG32456.1};
OS Sanguibacter antarcticus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC Sanguibacter.
OX NCBI_TaxID=372484 {ECO:0000313|EMBL:PFG32456.1, ECO:0000313|Proteomes:UP000225548};
RN [1] {ECO:0000313|EMBL:PFG32456.1, ECO:0000313|Proteomes:UP000225548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18966 {ECO:0000313|EMBL:PFG32456.1,
RC ECO:0000313|Proteomes:UP000225548};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-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 -!- 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:PFG32456.1}.
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DR EMBL; PDJG01000001; PFG32456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9E1E0; -.
DR OrthoDB; 9805733at2; -.
DR UniPathway; UPA00136; UER00201.
DR Proteomes; UP000225548; 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 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; 1.
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:UP000225548}.
FT DOMAIN 346..408
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 465 AA; 48758 MW; 568B80BBAC55C05F CRC64;
MRYAEHISEL VGNTPLVRLN AVTTGLSATI LAKIEYVNPG GSVKDRIALK MIEAAEASGE
LRPGGTIVEP TSGNTGVGLA LVAQRKGYKC VFVCPDKVSV DKRDVLKAYG AEVVVTPTAV
APEHPSSYYS VSDRLVAEIP GAWKPNQYAN PNGPASHYET TGPEIWADTD GRVTHFVTGV
GTGGTISGTG RFLRDVSADR ATGEVHVVGS DPEGSVYSGG TGRPYLVEGV GEDFWPAAYD
PSVPHEIIAV SDADSFEMTR RLAREEGLLV GGSCGMAVVS ALRLARRLED EDPAAAVEAV
IVVLLPDGGR GYMSKIFSDA WMRSYGFIGA EDGITAGDIL RGKSGALPDL VHTHPVETVR
DAIEILREFG VSQMPVVLAE PPVVIGEVAG AVSERALLDA VFSGGAALTD TVGTHMAGRL
PLIGSGEPVE AVRAALQDDD ALMVIDDGKP VGVLTRHDLL GFLAH
//