ID G8JWF6_ERECY Unreviewed; 492 AA.
AC G8JWF6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Cystathionine beta-synthase {ECO:0000256|ARBA:ARBA00026192, ECO:0000256|RuleBase:RU361204};
DE EC=4.2.1.22 {ECO:0000256|ARBA:ARBA00012041, ECO:0000256|RuleBase:RU361204};
GN OrderedLocusNames=Ecym_7341 {ECO:0000313|EMBL:AET41171.1};
OS Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS NRRL Y-17582) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=931890 {ECO:0000313|EMBL:AET41171.1, ECO:0000313|Proteomes:UP000006790};
RN [1] {ECO:0000313|Proteomes:UP000006790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC {ECO:0000313|Proteomes:UP000006790};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
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 ECO:0000256|RuleBase:RU361204};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU361204};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-homocysteine and L-serine: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005003}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|RuleBase:RU361204}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002503; AET41171.1; -; Genomic_DNA.
DR RefSeq; XP_003647988.1; XM_003647940.1.
DR AlphaFoldDB; G8JWF6; -.
DR STRING; 931890.G8JWF6; -.
DR GeneID; 11469741; -.
DR KEGG; erc:Ecym_7341; -.
DR eggNOG; KOG1252; Eukaryota.
DR HOGENOM; CLU_021018_0_0_1; -.
DR InParanoid; G8JWF6; -.
DR OMA; KFADDEW; -.
DR OrthoDB; 5487987at2759; -.
DR UniPathway; UPA00136; UER00201.
DR Proteomes; UP000006790; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004122; F:cystathionine beta-synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:UniProtKB-UniRule.
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; 1.
DR Pfam; PF00291; PALP; 1.
DR SMART; SM00116; CBS; 1.
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 Amino-acid biosynthesis {ECO:0000256|RuleBase:RU361204};
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192,
KW ECO:0000256|RuleBase:RU361204};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361204};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU361204};
KW Reference proteome {ECO:0000313|Proteomes:UP000006790}.
FT DOMAIN 359..416
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 492 AA; 54034 MW; 63469B61AAC0C8C5 CRC64;
MVDNRHQVID LVGNTPLIEL SKLPAALNIK PKVYAKLELY NPGGSIKDRI AKSMIEHAEA
EGIINPSRTT LIEPTSGNTG IGLALIGAIK GYRTIITLPE KMSNEKVSVL KALGAEIIRT
PTAAAWDSPE SHIGVAKRLE KEIPGAIILD QYNNIRNPLA HYNGTGREIH EQLNSLGLFN
KLHGVVAGAG TGGTISGISR YLKEQNDKIQ IIGADPKGSI LAQPASLNDS DVTEYKVEGI
GYDFVPEVLD RSLVDYWYKT EDKSAFKYAR QLISNEGVLI GGSSGSAFAA LVQYTQDHPE
LTEDDVLVVI FPDSIRSYLT KFVDDEWLKT NNLWDDSIIA PLAKNDVDAF KGAVVKDLDL
KPVVSVNETA PITEVVKILK DHGFDQLPVL AENSKKLVGL VTLSQLLKKL SSGKDVRSIK
GLFYDFRKLN NFDEISSYNE NKSGKKKFVR FTVESTLSEL NHFFERHSAA IITQGLTPVH
IVTKVDLLSY LA
//
