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Database: UniProt
Entry: K9WSS0_9NOST
LinkDB: K9WSS0_9NOST
Original site: K9WSS0_9NOST 
ID   K9WSS0_9NOST            Unreviewed;       457 AA.
AC   K9WSS0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=cystathionine beta-synthase {ECO:0000256|ARBA:ARBA00012041};
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=Cylst_0490 {ECO:0000313|EMBL:AFZ22831.1};
OS   Cylindrospermum stagnale PCC 7417.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Cylindrospermum.
OX   NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ22831.1, ECO:0000313|Proteomes:UP000010475};
RN   [1] {ECO:0000313|EMBL:AFZ22831.1, ECO:0000313|Proteomes:UP000010475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ22831.1,
RC   ECO:0000313|Proteomes:UP000010475};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Cylindrospermum stagnale PCC 7417.";
RL   Submitted (JUN-2012) 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         ECO:0000256|PIRSR:PIRSR605856-50};
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DR   EMBL; CP003642; AFZ22831.1; -; Genomic_DNA.
DR   RefSeq; WP_015206088.1; NC_019757.1.
DR   AlphaFoldDB; K9WSS0; -.
DR   STRING; 56107.Cylst_0490; -.
DR   KEGG; csg:Cylst_0490; -.
DR   PATRIC; fig|56107.3.peg.548; -.
DR   eggNOG; COG0031; Bacteria.
DR   eggNOG; COG3620; Bacteria.
DR   HOGENOM; CLU_021018_0_0_3; -.
DR   OrthoDB; 9808024at2; -.
DR   Proteomes; UP000010475; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004122; F:cystathionine beta-synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:InterPro.
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; IPR005856; Cys_synth.
DR   InterPro; IPR005857; Cysta_beta_synth.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01136; cysKM; 1.
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.
PE   4: Predicted;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AFZ22831.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR605856-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010475}.
FT   DOMAIN          335..390
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          399..453
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   BINDING         74
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         181..185
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         268
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         44
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   457 AA;  49767 MW;  507280F05E461367 CRC64;
     MATYDNILQT IGRTPLVRLN RTTENIPSSI YVKVEYLNPG GSTKDRIALA MIKAAEKAGQ
     LQPGGTIIEA TAGNTGVGLA LIAAVKKYRC IFVMPDKMSQ DKINLLKAYG AEVVVTPTSV
     PPDSPESYNG VAERLAKEIP GAYRPNQFEN PNNPLAHYLT TGPEIWSDSN GKIDVFVAGM
     GTGGTISGVA KYLKERNQNI IIVGADPEGS ILSGDSPKSY KVEGIGEDFI PKTFNRQLVD
     EMVRVSDKES FNMARRLARE EGLLVGGSCG TAVAAALKYA ARLSQPQYIV VLLPDTGRNY
     INKIYSDVWM QENGFWEGTT VRPIKIGEIL VQKTDFPSLI AVSPRDTLSK ATNLLQKLNI
     SQLPVIDHNH VVGSLNEASL MKYLHDGINF SNQEVSAVMG KPLPSLDEEV DISEAYRVLL
     SGTTGIIITQ QKVPIGLITR ADLIRYWISQ NQESNGI
//
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