ID F4P4C4_BATDJ Unreviewed; 503 AA.
AC F4P4C4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=BATDEDRAFT_35224 {ECO:0000313|EMBL:EGF79897.1};
OS Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF79897.1, ECO:0000313|Proteomes:UP000007241};
RN [1] {ECO:0000313|EMBL:EGF79897.1, ECO:0000313|Proteomes:UP000007241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA Stajich J., Eisen M., Grigoriev I.V.;
RT "The draft genome of Batrachochytrium dendrobatidis.";
RL Submitted (DEC-2009) 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 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; GL882885; EGF79897.1; -; Genomic_DNA.
DR RefSeq; XP_006679546.1; XM_006679483.1.
DR AlphaFoldDB; F4P4C4; -.
DR STRING; 684364.F4P4C4; -.
DR GeneID; 18240697; -.
DR HOGENOM; CLU_021018_0_0_1; -.
DR InParanoid; F4P4C4; -.
DR OMA; KFADDEW; -.
DR OrthoDB; 5487987at2759; -.
DR UniPathway; UPA00136; UER00201.
DR Proteomes; UP000007241; 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:UP000007241}.
FT DOMAIN 372..431
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 54715 MW; B1D5B1BFD1D438F6 CRC64;
MSTVPASTTH QNKQSTSPPY AWDRGHILNN ILEHIGGTPV VRINRIGVEE GLECELVAKC
EFFNAGGSVK DRIGCRMVEY GEIDGKLTPG ATIIEPTSGN TGIGLALAAA VKGYRAVITL
PEKMSQEKVD VLKALGAEII RTPTEAAWDS PDSHIGVAKR LNHEIPNSWI PDQYSNMNNP
LAHYYGTAEE IYQQCGGKLD MLVATVGTGG TIAGIGKRLK ELIPNVQIVG VDPYGSILAL
PESLNHEGVH SYQVEGIGYD FVPQVLDRQY VDSWIKTNDK ESFLMARRLI KSEGLLCGGS
CGAAMAGAIQ AAKSLKKGQR CLVLFADSVR NYMTKFLNDD WMKKMGYIDE KTQKEEDIKK
SQWCGATIKD LNLSSAITVP QKTPVLKAIK LLQDNGFDQL PVTSASDSLH LVGLVTLGGL
LAKIASGRTK VTDPVESSMY EFRTAKKFTE VTIDTRLESL SKFFESNSSA VVTFRDSDGE
LHVSSVVTKV DLLAFLVKKS SVI
//
