ID A7EUA9_SCLS1 Unreviewed; 535 AA.
AC A7EUA9;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
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 ORFNames=SS1G_08916 {ECO:0000313|EMBL:EDN93051.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN93051.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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}.
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DR EMBL; CH476632; EDN93051.1; -; Genomic_DNA.
DR RefSeq; XP_001590152.1; XM_001590102.1.
DR AlphaFoldDB; A7EUA9; -.
DR STRING; 665079.A7EUA9; -.
DR GeneID; 5486308; -.
DR KEGG; ssl:SS1G_08916; -.
DR VEuPathDB; FungiDB:sscle_14g100510; -.
DR InParanoid; A7EUA9; -.
DR OMA; KFADDEW; -.
DR OrthoDB; 5487987at2759; -.
DR UniPathway; UPA00136; UER00201.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004122; F:cystathionine beta-synthase activity; IBA:GO_Central.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central.
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:UP000001312}.
FT DOMAIN 369..426
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 336..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 57338 MW; 9DE04096DE20BB05 CRC64;
MASTTSPVRA PVLAMSASEL IGNTPLVRLN KIPQSLGIEA EVYAKVELFN AGGSIKDRIA
LRMIEEAEKS GRIKPGDTLI EPTSGNTGIG LALVGAIKGY KTIITLPEKM SPEKVAVLRA
LGATIIRTPT QAAWDAPESH IGVARRLLKE IPNSHILDQY ANENNPLAHE FGTAEEIWKQ
TDGKITAVVA GAGTGGTITG LSKGLKKHNK DVKIIAADPH GSILAVPESL NQEHANESYK
VEGIGYDFIP DVLDRDSVDV WYKTDDRESF AYARRLIAEE GLLVGGSSGS AIAAMVKGVR
ELGLGKGDTV VVILPDSIRS YLSKFADDDW LAANDLLPPT PESSTPASPV VEAQSKKDPY
SGATLRSLRL KPVTSVLANS PCSEAIETMR EKGFDQLPVL APKGDKLVGL VTLGNLLSWI
SRGRATGKSP VSDVMFDFSH IPEVITDPKD ISHLSSPPKS NGIETTQEGK KQTTPKRKFV
EITLDTPISA LSKFFEWNSA AIVTEKGSEK NGLSKPVAVV TKVDLLSWMV KQTKV
//
