ID C3MCJ0_SINFN Unreviewed; 346 AA. AC C3MCJ0; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAR-2024, entry version 79. DE SubName: Full=Cysteine synthase protein {ECO:0000313|EMBL:ACP25269.1}; DE EC=2.5.1.47 {ECO:0000313|EMBL:ACP25269.1}; GN Name=cysK2 {ECO:0000313|EMBL:ACP25269.1}; GN OrderedLocusNames=NGR_c14980 {ECO:0000313|EMBL:ACP25269.1}; OS Sinorhizobium fredii (strain NBRC 101917 / NGR234). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP25269.1, ECO:0000313|Proteomes:UP000001054}; RN [1] {ECO:0000313|EMBL:ACP25269.1, ECO:0000313|Proteomes:UP000001054} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054}; RX PubMed=19376903; DOI=10.1128/AEM.00515-09; RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A., RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A., RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A., RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.; RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion RT systems."; RL Appl. Environ. Microbiol. 75:4035-4045(2009). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933}; 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; CP001389; ACP25269.1; -; Genomic_DNA. DR RefSeq; WP_012708041.1; NC_012587.1. DR RefSeq; YP_002826022.1; NC_012587.1. DR AlphaFoldDB; C3MCJ0; -. DR STRING; 394.NGR_c14980; -. DR KEGG; rhi:NGR_c14980; -. DR PATRIC; fig|394.7.peg.4311; -. DR eggNOG; COG0031; Bacteria. DR HOGENOM; CLU_021018_1_0_5; -. DR OrthoDB; 9805733at2; -. DR Proteomes; UP000001054; Chromosome. DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro. DR CDD; cd01561; CBS_like; 1. DR Gene3D; 3.40.50.1100; -; 2. 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 PANTHER; PTHR10314:SF211; PALP DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR Pfam; PF00291; PALP; 1. DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1. DR PROSITE; PS00901; CYS_SYNTHASE; 1. PE 4: Predicted; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}; KW Reference proteome {ECO:0000313|Proteomes:UP000001054}; KW Transferase {ECO:0000313|EMBL:ACP25269.1}. FT DOMAIN 8..306 FT /note="Tryptophan synthase beta chain-like PALP" FT /evidence="ECO:0000259|Pfam:PF00291" SQ SEQUENCE 346 AA; 36387 MW; E325BB538FE75A29 CRC64; MSVYPSVLEA IGNTPLIRLN AVSEATGCTI LGKAEFLNPG QSVKDRAALW IIREAEKAGQ LRPGGVIVEG TAGNTGIGLA VVGSALGYRT VIVIPETQSQ EKKDALRLLG AELVEVPAVP YKNPNNYVKI SGRLAAELAK TEPNGAIWAN QFDNVANREA HVQTTAPEIW RDTDGKVDGF ICAVGSGGTI AGVAEGLRAK NPAVKIGIAD PEGAALYNYY AHGELKASGS SITEGIGQGR VTANLEGFTP DFAYQIPDSE AVPYVFDLIE KEGLCVGGSS GINIAGAVRL ARELGPGHTI VTILCDYGNR YQSKLFNPDF LASKGLPVPA WLNKSSNITV PYEPIG //