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Database: UniProt
Entry: A0A151GH47_9HYPO
LinkDB: A0A151GH47_9HYPO
Original site: A0A151GH47_9HYPO 
ID   A0A151GH47_9HYPO        Unreviewed;       518 AA.
AC   A0A151GH47;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=DCS_03430 {ECO:0000313|EMBL:KYK56430.1};
OS   Drechmeria coniospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX   NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK56430.1, ECO:0000313|Proteomes:UP000076580};
RN   [1] {ECO:0000313|EMBL:KYK56430.1, ECO:0000313|Proteomes:UP000076580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK56430.1,
RC   ECO:0000313|Proteomes:UP000076580};
RX   PubMed=26975455; DOI=10.1038/srep23122;
RA   Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA   Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA   Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA   Molnar I., Lin M.;
RT   "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT   Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL   Sci. Rep. 6:23122-23122(2016).
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   -!- 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:KYK56430.1}.
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DR   EMBL; LAYC01000002; KYK56430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151GH47; -.
DR   STRING; 98403.A0A151GH47; -.
DR   InParanoid; A0A151GH47; -.
DR   OrthoDB; 5487987at2759; -.
DR   UniPathway; UPA00136; UER00201.
DR   Proteomes; UP000076580; Chromosome 02.
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:UP000076580}.
FT   DOMAIN          370..426
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   518 AA;  55709 MW;  E41BBE0146D1C9FD CRC64;
     MASVPHVGRK PATVLSATEL IGNTPLIRLN KVPQSLGIEC EVYAKTELFN AGGSVKDRIA
     LRMIEQAEKS GRIKPGDTLI EPTSGNTGIG LALVGAIKGY KTIITMPEKM SAEKVSVLRA
     LGATIIRTPN QAAWDAPESH IGVARRLEKE MPNAHILDQY SNLDNPLAHE HGTAEEIWEQ
     TGGRIDAVVA GAGTGGTITG IARGLKKHDG KIKVIAADPQ GSILALPESL NEEHVNEPYK
     VEGIGYDFVP DVLERTIVDR WYKTDDDESF YLARRLIAEE GLLVGGSSGS AMAAMLKAVK
     DYGFKKGDVV VVVMPDSIRS YLSKFADDDW LAANNLLPVR GDVQVNGVES AAVKTDANDP
     YAGATVASLR LKPVTSVSDT ARCSEAVETM RDKGFDQLPV LSASHKLVGL VTLGNLLSYM
     SRGRATGSSP VRDVMFNFGR FDEIVTDLRH GATGETVGPK RKFVEITVDT PLSTLSSFFE
     WNSAAVVTEK SADGKSLSKP IAVVTKVDLL TWMVNRKQ
//
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