CBS_DICDI
ID CBS_DICDI Reviewed; 498 AA.
AC P46794; Q55FN2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cystathionine beta-synthase;
DE EC=4.2.1.22;
DE AltName: Full=Beta-thionase;
DE AltName: Full=Serine sulfhydrase;
GN Name=cysB; ORFNames=DDB_G0267386;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX3;
RA Jho E., Kopachik W.;
RT "Cloning and sequencing analysis of Dictyostelium discoideum cDNA encoding
RT cystathionine beta synthase.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-homocysteine and L-serine: step 1/2.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA70099.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U27536; AAA70099.1; ALT_FRAME; mRNA.
DR EMBL; AAFI02000003; EAL73145.1; -; Genomic_DNA.
DR RefSeq; XP_647501.1; XM_642409.1.
DR AlphaFoldDB; P46794; -.
DR SMR; P46794; -.
DR STRING; 44689.DDB0191292; -.
DR PaxDb; P46794; -.
DR EnsemblProtists; EAL73145; EAL73145; DDB_G0267386.
DR GeneID; 8616308; -.
DR KEGG; ddi:DDB_G0267386; -.
DR dictyBase; DDB_G0267386; cysB.
DR eggNOG; KOG1252; Eukaryota.
DR HOGENOM; CLU_021018_0_0_1; -.
DR InParanoid; P46794; -.
DR OMA; IEITMDT; -.
DR PhylomeDB; P46794; -.
DR Reactome; R-DDI-1614603; Cysteine formation from homocysteine.
DR UniPathway; UPA00136; UER00201.
DR PRO; PR:P46794; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR GO; GO:0004122; F:cystathionine beta-synthase activity; ISS:dictyBase.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
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 GO; GO:0006534; P:cysteine metabolic process; ISS:dictyBase.
DR CDD; cd04608; CBS_pair_CBS; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR046353; CBS_C.
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; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00291; PALP; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF53686; SSF53686; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR TIGRFAMs; TIGR01137; cysta_beta; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; CBS domain; Cysteine biosynthesis; Lyase;
KW Pyridoxal phosphate; Reference proteome; Repeat.
FT CHAIN 1..498
FT /note="Cystathionine beta-synthase"
FT /id="PRO_0000167132"
FT DOMAIN 374..430
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 435..497
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 210..214
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 73
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 140
FT /note="A -> G (in Ref. 1; AAA70099)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="G -> A (in Ref. 1; AAA70099)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 54458 MW; 31FD69EFB68B6432 CRC64;
MSAPEGPSKC TWTPNTTENT PHTTRRTPKK LIMDNILDNI GGTPLVRVNK VSSDLECELV
AKCEFFNAGG SVKDRIGHRM IVDAEESGRI KKGDTLIEPT SGNTGIGLAL TAAIKGYKMI
ITLPEKMSQE KVDVLKALGA EIIRTPTEAA FDAPESHIGV AKKLNSEIPN SHILDQYGNP
SNPLAHYDGT AEELLEQCEG KIDMIVCTAG TGGTITGIAR KIKERLPNCI VVGVDPHGSI
LAQPESLNNT NKSYKIEGIG YDFIPNVLER KLVDQWIKTD DKESFIMARR LIKEEGLLCG
GSSGSAMVGA LLAAKQLKKG QRCVVLLADS IRNYMTKHLN DDWLVDNGFV DPEYKTKDQQ
EEEKYHGATV KDLTLPKPIT ISATTTCAAA VQLLQQYGFD QLPVVSESKK VLGQLTLGNL
LSHIASKKAV PTDAVSKVMF RFTKNEKYIP ITQSTSLATL SKFFENHSSA IVTENDEIIS
IVTKIDLLTY LMKSQQKN
