ID C5WSS1_SORBI Unreviewed; 454 AA. AC C5WSS1; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 02-SEP-2026, entry version 94. DE RecName: Full=cysteine synthase {ECO:0000256|ARBA:ARBA00012681}; DE EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681}; GN ORFNames=SORBI_3001G455600 {ECO:0000313|EMBL:EER95270.1}; OS Sorghum bicolor (Sorghum) (Sorghum vulgare). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum. OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EER95270.1, ECO:0000313|Proteomes:UP000000768}; RN [1] {ECO:0000313|EMBL:EER95270.1, ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=19189423; DOI=10.1038/nature07723; RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J., RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J., RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J., RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M., RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L., RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P., RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman, RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.; RT "The Sorghum bicolor genome and the diversification of grasses."; RL Nature 457:551-556(2009). RN [2] {ECO:0000313|EMBL:EER95270.1} RP NUCLEOTIDE SEQUENCE. RA Paterson A., Mullet J., Bowers J., Bruggmann R., Dubchak I., Grimwood J., RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J., RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A., Chapman J., Feltus F., RA Gowik U., Grigoriev I., Lyons E., Maher C., Martis M., Narechania A., RA Otillar R., Penning B., Salamov A., Wang Y., Zhang L., Carpita N., RA Freeling M., Gingle A., Hash C., Keller B., Klein P., Kresovich S., RA Mccann M., Ming R., Peterson D., Rahman M., Ware D., Westhoff P., Mayer K., RA Messing J., Sims D., Jenkins J., Shu S., Rokhsar D.; RT "WGS assembly of Sorghum bicolor."; RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=29161754; DOI=10.1111/tpj.13781; RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D., RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A., RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.; RT "The Sorghum bicolor reference genome: improved assembly, gene annotations, RT a transcriptome atlas, and signatures of genome organization."; RL Plant J. 93:338-354(2018). CC -!- CATALYTIC ACTIVITY: CC Reaction=O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate; CC Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, CC ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47; CC Evidence={ECO:0000256|ARBA:ARBA00047931}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933}; CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- CC synthase family. {ECO:0000256|ARBA:ARBA00007103}. 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; CM000760; EER95270.1; -; Genomic_DNA. DR EMBL; CM000760; KXG39861.1; -; Genomic_DNA. DR EMBL; CM000760; KXG39862.1; -; Genomic_DNA. DR EMBL; CM000760; KXG39864.1; -; Genomic_DNA. DR AlphaFoldDB; C5WSS1; -. DR SMR; C5WSS1; -. DR STRING; 4558.C5WSS1; -. DR Gramene; EER95270; EER95270; SORBI_3001G455600. DR Gramene; KXG39861; KXG39861; SORBI_3001G455600. DR Gramene; KXG39862; KXG39862; SORBI_3001G455600. DR Gramene; KXG39864; KXG39864; SORBI_3001G455600. DR KEGG; sbi:8056886; -. DR eggNOG; KOG1481; Eukaryota. DR HOGENOM; CLU_021018_1_0_1; -. DR OMA; GYKCLII; -. DR OrthoDB; 10259545at2759; -. DR Proteomes; UP000000768; Chromosome 1. DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC. DR CDD; cd01561; CBS_like; 1. DR FunFam; 3.40.50.1100:FF:000061; Cysteine synthase; 1. DR FunFam; 3.40.50.1100:FF:000077; Cysteine synthase; 1. DR FunFam; 3.40.50.1100:FF:000049; Cysteine synthase, putative; 1. DR FunFam; 3.40.50.1100:FF:000098; Predicted protein; 1. DR Gene3D; 3.40.50.1100; -; 4. DR InterPro; IPR050214; Cys_Synth/Cystath_Beta-Synth. DR InterPro; IPR001216; P-phosphate_BS. DR InterPro; IPR001926; TrpB-like_PALP. DR InterPro; IPR036052; TrpB-like_PALP_sf. DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1. DR Pfam; PF00291; PALP; 2. DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1. DR PROSITE; PS00901; CYS_SYNTHASE; 1. PE 3: Inferred from homology; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}; KW Reference proteome {ECO:0000313|Proteomes:UP000000768}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 55..212 FT /note="Tryptophan synthase beta chain-like PALP" FT /evidence="ECO:0000259|Pfam:PF00291" FT DOMAIN 246..422 FT /note="Tryptophan synthase beta chain-like PALP" FT /evidence="ECO:0000259|Pfam:PF00291" SQ SEQUENCE 454 AA; 48716 MW; AD70096A5B2BC39A CRC64; MAAATAAGAA AAAAAVSLIA CYLLLHKGRP NLPWVPTVGF SRASGRRARR RGLVEAIGNT PLIRINSLSD ATGCEILGKA EFLNPGGSVK DRVAVKIIEE ALESGDLVYG GTVTEGSAGS TAISLATVAP AYGCRCHVVI PDDAAIEKSQ IIEALGATVE RVRPVSITHR DHFVNIARRR ALEANKLAAA QSESNEKQTN GLAHVGSEMM DDKLTAMQRE SNKMQNNDPA LFSTETLHSG KCDVNSDSKG GFFADQFENM ANYRAHYEWT GPEIWKQTKG NLHAFVAAAG TGGTIAGVSR YLKEKNRSIK CFLMDPPGSG LFNKVTRGVM YTKEEAEGKR LKNPFDTITE GIGINRVTKN FMMAELDGAY RGSDREAVEM SRFLLKNDGL FVGSSSAMNC VGAVRVAQDL GPGHTIVTIL CDSGMRHLSK FFNEQYLADH GLTPAATALE FLDK //