ID CYSO_AERPE Reviewed; 389 AA. AC Q9YBL2; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 130. DE RecName: Full=Protein CysO; DE AltName: Full=Cystathionine beta-synthase; DE EC=4.2.1.22 {ECO:0000269|PubMed:12644499, ECO:0000269|PubMed:16005886}; DE AltName: Full=Cysteine synthase; DE EC=2.5.1.47 {ECO:0000269|PubMed:12644499}; DE AltName: Full=O-acetylserine sulfhydrylase {ECO:0000303|PubMed:12644499}; DE AltName: Full=O-phosphoserine sulfhydrylase {ECO:0000303|PubMed:16005886}; DE EC=2.5.1.65 {ECO:0000269|PubMed:16005886}; DE AltName: Full=Serine sulfhydrase; GN Name=cysO; OrderedLocusNames=APE_1586; OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / OS K1). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Aeropyrum. OX NCBI_TaxID=272557; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1; RX PubMed=10382966; DOI=10.1093/dnares/6.2.83; RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S., RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.; RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, RT Aeropyrum pernix K1."; RL DNA Res. 6:83-101(1999). RN [2] RP PROTEIN SEQUENCE OF 2-8, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, RP AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1; RX PubMed=12644499; DOI=10.1128/jb.185.7.2277-2284.2003; RA Mino K., Ishikawa K.; RT "Characterization of a novel thermostable O-acetylserine sulfhydrylase from RT Aeropyrum pernix K1."; RL J. Bacteriol. 185:2277-2284(2003). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, RP AND CATALYTIC ACTIVITY. RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1; RX PubMed=16005886; DOI=10.1016/j.jmb.2005.05.064; RA Oda Y., Mino K., Ishikawa K., Ataka M.; RT "Three-dimensional structure of a new enzyme, O-phosphoserine RT sulfhydrylase, involved in L-cysteine biosynthesis by a hyperthermophilic RT archaeon, Aeropyrum pernix K1, at 2.0 A resolution."; RL J. Mol. Biol. 351:334-344(2005). CC -!- FUNCTION: Cysteine synthase that can also catalyze the synthesis of S- CC sulfo-L-cysteine from thiosulfate and O(3)-acetyl-L-serine, as well as CC the sulfhydrylation of L-serine by sulfide. CC {ECO:0000269|PubMed:12644499}. CC -!- CATALYTIC ACTIVITY: CC Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine; 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:0000269|PubMed:12644499}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + hydrogen sulfide + O-phospho-L-serine = L-cysteine + CC phosphate; Xref=Rhea:RHEA:10252, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29919, ChEBI:CHEBI:35235, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57524; EC=2.5.1.65; CC Evidence={ECO:0000269|PubMed:16005886}; 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:0000269|PubMed:12644499, ECO:0000269|PubMed:16005886}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:12644499}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=28 mM for O(3)-acetyl-L-serine (in the presence of 1 mM sodium CC sulfide at pH 6.7 and 60 degrees Celsius) CC {ECO:0000269|PubMed:12644499}; CC KM=0.2 mM for sulfide (in the presence of 20 mM O(3)-acetyl-L-serine CC at pH 6.7 and 60 degrees Celsius) {ECO:0000269|PubMed:12644499}; CC KM=8 mM for L-serine (in the presence of 0.7 mM L-homocysteine at pH CC 8.3 and 85 degrees Celsius) {ECO:0000269|PubMed:12644499}; CC KM=0.5 mM for L-homocysteine (in the presence of 30 mM L-serine at pH CC 8.3 and 85 degrees Celsius) {ECO:0000269|PubMed:12644499}; CC KM=0.2 mM for sulfide (in the presence of 20 mM L-serine at pH 8.5 CC and 70 degrees Celsius) {ECO:0000269|PubMed:12644499}; CC KM=31 mM for L-serine (in the presence of 1 mM sodium sulfide at pH CC 8.5 and 70 degrees Celsius) {ECO:0000269|PubMed:12644499}; CC KM=13 mM for O(3)-acetyl-L-serine (in the presence of 20 mM CC thiosulfate at pH 6.1 and 85 degrees Celsius) CC {ECO:0000269|PubMed:12644499}; CC KM=21 mM for thiosulfate (in the presence of 20 mM CC O(3)-acetyl-L-serine at pH 6.1 and 85 degrees Celsius) CC {ECO:0000269|PubMed:12644499}; CC pH dependence: CC Optimum pH is 6.7 for O-acetylserine sulfhydrylase A activity and CC 8.1-8.8 for cystathionine beta-synthase activity. CC {ECO:0000269|PubMed:12644499}; CC Temperature dependence: CC Optimum temperature is above 90 degrees Celsius for CC S-sulfo-L-cysteine synthase activity, 70-80 degrees Celsius for CC O-acetylserine sulfhydrylase A activity, and 80 degrees Celsius for CC both cystathionine beta-synthase and L-serine sulfhdrylase CC activities. {ECO:0000269|PubMed:12644499}; CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine CC from L-serine: step 2/2. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12644499, CC ECO:0000269|PubMed:16005886}. CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- CC synthase family. {ECO:0000305}. 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; BA000002; BAA80586.1; -; Genomic_DNA. DR PIR; E72537; E72537. DR PDB; 1WKV; X-ray; 2.00 A; A/B=1-389. DR PDB; 3VSA; X-ray; 2.07 A; A/B=1-389. DR PDB; 3VSC; X-ray; 2.07 A; A/B=1-389. DR PDB; 3VSD; X-ray; 2.09 A; A/B=1-389. DR PDB; 5B36; X-ray; 2.15 A; A/B=1-389. DR PDB; 5B3A; X-ray; 2.14 A; A/B=1-389. DR PDB; 6L0P; X-ray; 1.79 A; A/B/C/D=1-389. DR PDB; 6L0Q; X-ray; 1.58 A; A/B/C/D=1-389. DR PDB; 6L0R; X-ray; 1.79 A; A/B/C/D=1-389. DR PDB; 6L0S; X-ray; 1.96 A; A/B/C/D=1-389. DR PDBsum; 1WKV; -. DR PDBsum; 3VSA; -. DR PDBsum; 3VSC; -. DR PDBsum; 3VSD; -. DR PDBsum; 5B36; -. DR PDBsum; 5B3A; -. DR PDBsum; 6L0P; -. DR PDBsum; 6L0Q; -. DR PDBsum; 6L0R; -. DR PDBsum; 6L0S; -. DR AlphaFoldDB; Q9YBL2; -. DR SMR; Q9YBL2; -. DR STRING; 272557.APE_1586; -. DR EnsemblBacteria; BAA80586; BAA80586; APE_1586. DR KEGG; ape:APE_1586; -. DR PATRIC; fig|272557.25.peg.1071; -. DR eggNOG; arCOG01430; Archaea. DR BioCyc; MetaCyc:MONOMER-20567; -. DR BRENDA; 2.5.1.47; 171. DR BRENDA; 2.5.1.65; 171. DR SABIO-RK; Q9YBL2; -. DR UniPathway; UPA00136; UER00200. DR EvolutionaryTrace; Q9YBL2; -. DR Proteomes; UP000002518; Chromosome. DR GO; GO:0004122; F:cystathionine beta-synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0033847; F:O-phosphoserine sulfhydrylase activity; IEA:UniProtKB-EC. DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro. DR Gene3D; 3.40.50.1100; -; 2. DR Gene3D; 3.90.1530.20; -; 1. 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:SF194; 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. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Cysteine biosynthesis; KW Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome; KW Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12644499" FT CHAIN 2..389 FT /note="Protein CysO" FT /id="PRO_0000167131" FT BINDING 155 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:16005886" FT BINDING 261..265 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT BINDING 341 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:16005886" FT MOD_RES 127 FT /note="N6-(pyridoxal phosphate)lysine" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 6..8 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 12..15 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 21..31 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 37..40 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 44..53 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 56..63 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:6L0P" FT TURN 68..74 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 83..86 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 87..93 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:6L0Q" FT TURN 107..109 FT /evidence="ECO:0007829|PDB:6L0P" FT STRAND 110..116 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:6L0Q" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 128..138 FT /evidence="ECO:0007829|PDB:6L0Q" FT TURN 139..141 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 147..151 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 155..166 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 170..176 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 181..189 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 193..199 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:1WKV" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 207..217 FT /evidence="ECO:0007829|PDB:6L0Q" FT TURN 224..226 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 228..236 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 238..249 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 253..258 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 264..276 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 281..287 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 299..301 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 305..308 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 314..318 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 320..334 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 340..355 FT /evidence="ECO:0007829|PDB:6L0Q" FT STRAND 360..367 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 371..373 FT /evidence="ECO:0007829|PDB:6L0Q" FT HELIX 375..382 FT /evidence="ECO:0007829|PDB:6L0Q" SQ SEQUENCE 389 AA; 41981 MW; C103727AC1B9C72B CRC64; MALADISGYL DVLDSVRGFS YLENAREVLR SGEARCLGNP RSEPEYVKAL YVIGASRIPV GDGCSHTLEE LGVFDISVPG EMVFPSPLDF FERGKPTPLV RSRLQLPNGV RVWLKLEWYN PFSLSVKDRP AVEIISRLSR RVEKGSLVAD ATSSNFGVAL SAVARLYGYR ARVYLPGAAE EFGKLLPRLL GAQVIVDPEA PSTVHLLPRV MKDSKNEGFV HVNQFYNDAN FEAHMRGTAR EIFVQSRRGG LALRGVAGSL GTSGHMSAAA FYLQSVDPSI RAVLVQPAQG DSIPGIRRVE TGMLWINMLD ISYTLAEVTL EEAMEAVVEV ARSDGLVIGP SGGAAVKALA KKAAEGDLEP GDYVVVVPDT GFKYLSLVQN ALEGAGDSV //