CYSO_AERPE
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 03-AUG-2022, entry version 125.
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; Crenarchaeota; 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 O(3)-acetyl-L-
CC 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 S-sulfo-L-
CC cysteine synthase activity, 70-80 degrees Celsius for O-acetylserine
CC sulfhydrylase A activity, and 80 degrees Celsius for both
CC cystathionine beta-synthase and L-serine sulfhdrylase activities.
CC {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}.
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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 OMA; GIRRWPE; -.
DR BioCyc; MetaCyc:MON-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 InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 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
