ID D5STP0_PLAL2 Unreviewed; 309 AA. AC D5STP0; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 02-SEP-2026, entry version 92. DE RecName: Full=Cysteine synthase {ECO:0000256|ARBA:ARBA00012681, ECO:0000256|RuleBase:RU003985}; DE EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681, ECO:0000256|RuleBase:RU003985}; GN OrderedLocusNames=Plim_3256 {ECO:0000313|EMBL:ADG69069.1}; OS Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290) OS (Planctomyces limnophilus). OC Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia; OC Planctomycetales; Planctomycetaceae; Planctopirus. OX NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG69069.1, ECO:0000313|Proteomes:UP000002220}; RN [1] {ECO:0000313|EMBL:ADG69069.1, ECO:0000313|Proteomes:UP000002220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290 RC {ECO:0000313|Proteomes:UP000002220}; RX PubMed=21304691; DOI=10.4056/sigs.1052813; RA Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S., RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Planctomyces limnophilus type strain (Mu RT 290)."; RL Stand. Genomic Sci. 3:47-56(2010). RN [2] {ECO:0007829|PDB:5XA2} RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS), AND PYRIDOXAL PHOSPHATE AT LYS-44. RA Singh R.P., Kumaran S.; RT "Crystal Structure of O-acetylserine sulfhydrylase from Planctomyces RT Limnophila."; RL Submitted (MAR-2017) to the PDB data bank. RN [3] {ECO:0007829|PDB:5XOQ} RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS), AND PYRIDOXAL PHOSPHATE AT LYS-44. RA Singh R.P., Saini N.; RT "Crystal structure of O-Acetylserine Sulfhydrylase with bound Transcription RT Factor peptide inhibitor from Planctomyces limnophilus."; RL Submitted (MAY-2017) to the PDB data bank. 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 ECO:0000256|RuleBase:RU003985}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|PIRSR:PIRSR605856-50, ECO:0000256|RuleBase:RU003985}; CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine CC from L-serine: step 2/2. {ECO:0000256|ARBA:ARBA00004962}. CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- CC synthase family. {ECO:0000256|ARBA:ARBA00007103, CC ECO:0000256|RuleBase:RU003985}. 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; CP001744; ADG69069.1; -; Genomic_DNA. DR RefSeq; WP_013111500.1; NC_014148.1. DR PDB; 5XA2; X-ray; 2.03 A; A/B=1-309. DR PDB; 5XOQ; X-ray; 1.87 A; A/B=1-309. DR AlphaFoldDB; D5STP0; -. DR SMR; D5STP0; -. DR STRING; 521674.Plim_3256; -. DR KEGG; plm:Plim_3256; -. DR eggNOG; COG0031; Bacteria. DR HOGENOM; CLU_021018_1_0_0; -. DR OrthoDB; 9808024at2; -. DR Proteomes; UP000002220; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA. DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-UniRule. DR CDD; cd01561; CBS_like; 1. DR FunFam; 3.40.50.1100:FF:000067; Cysteine synthase; 1. DR Gene3D; 3.40.50.1100; -; 2. DR InterPro; IPR005856; Cys_synth. DR InterPro; IPR050214; Cys_Synth/Cystath_Beta-Synth. DR InterPro; IPR005859; CysK. DR InterPro; IPR001216; P-phosphate_BS. DR InterPro; IPR001926; TrpB-like_PALP. DR InterPro; IPR036052; TrpB-like_PALP_sf. DR NCBIfam; TIGR01139; cysK; 1. DR NCBIfam; TIGR01136; cysKM; 1. DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1. DR Pfam; PF00291; PALP; 1. DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1. DR PROSITE; PS00901; CYS_SYNTHASE; 1. DR PDBsum; 5XA2; -. DR PDBsum; 5XOQ; -. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:5XA2, ECO:0007829|PDB:5XOQ}; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, KW ECO:0000256|RuleBase:RU003985}; KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192, KW ECO:0000256|RuleBase:RU003985}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, KW ECO:0000256|PIRSR:PIRSR605856-50}; KW Reference proteome {ECO:0000313|Proteomes:UP000002220}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}. FT DOMAIN 9..294 FT /note="Tryptophan synthase beta chain-like PALP" FT /evidence="ECO:0000259|Pfam:PF00291" FT BINDING 74 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50" FT BINDING 177..181 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50" FT BINDING 266 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50" FT MOD_RES 44 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51, FT ECO:0007829|PDB:5XA2" SQ SEQUENCE 309 AA; 32618 MW; C0E2F4A8F5574195 CRC64; MPIFKDNSES IGRTPLVQIN RLTAGLSSRV LAKIEGRNPA YSVKCRIGAA MIWDAEQSGK LKPGMHVVEP TSGNTGIALA FVCAARGYKL TLTMPETMSI ERRMMLKSFG ADLVLTPGAD GMKGAISKAE ELAAQPGWFI PQQFKNPANP AIHVKTTGPE IWNDTEGQVD VFVAGVGTGG TITGVARFLK HEKKHPVHVV AVEPAASPVL AGGPAGRHKI QGIGAGFVPD TFDRSVVDEI LSVTDDEAIE TARKLAMEEG ISCGISCGAA MAGALKVAAR PEFAGKTIVT VLPDAGERYL STALFENLR //