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UniProtKB - Q9YBL2 (CYSO_AERPE)
Protein
Protein CysO
Gene
cysO
Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Status
Functioni
Cysteine synthase that can also catalyze the synthesis of S-sulfo-L-cysteine from thiosulfate and O3-acetyl-L-serine, as well as the sulfhydrylation of L-serine by sulfide.
1 PublicationCatalytic activityi
Cofactori
pyridoxal 5'-phosphate1 Publication
Kineticsi
- KM=28 mM for O3-acetyl-L-serine (in the presence of 1 mM sodium sulfide at pH 6.7 and 60 degrees Celsius)1 Publication
- KM=0.2 mM for sulfide (in the presence of 20 mM O3-acetyl-L-serine at pH 6.7 and 60 degrees Celsius)1 Publication
- KM=8 mM for L-serine (in the presence of 0.7 mM L-homocysteine at pH 8.3 and 85 degrees Celsius)1 Publication
- KM=0.5 mM for L-homocysteine (in the presence of 30 mM L-serine at pH 8.3 and 85 degrees Celsius)1 Publication
- KM=0.2 mM for sulfide (in the presence of 20 mM L-serine at pH 8.5 and 70 degrees Celsius)1 Publication
- KM=31 mM for L-serine (in the presence of 1 mM sodium sulfide at pH 8.5 and 70 degrees Celsius)1 Publication
- KM=13 mM for O3-acetyl-L-serine (in the presence of 20 mM thiosulfate at pH 6.1 and 85 degrees Celsius)1 Publication
- KM=21 mM for thiosulfate (in the presence of 20 mM O3-acetyl-L-serine at pH 6.1 and 85 degrees Celsius)1 Publication
pH dependencei
Optimum pH is 6.7 for O-acetylserine sulfhydrylase A activity and 8.1-8.8 for cystathionine beta-synthase activity.1 Publication
Temperature dependencei
Optimum temperature is above 90 degrees Celsius for S-sulfo-L-cysteine synthase activity, 70-80 degrees Celsius for O-acetylserine sulfhydrylase A activity, and 80 degrees Celsius for both cystathionine beta-synthase and L-serine sulfhdrylase activities.1 Publication
: L-cysteine biosynthesis Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes L-cysteine from L-serine. This subpathway is part of the pathway L-cysteine biosynthesis, which is itself part of Amino-acid biosynthesis.View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-cysteine from L-serine, the pathway L-cysteine biosynthesis and in Amino-acid biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 155 | Pyridoxal phosphate1 Publication | 1 | |
Binding sitei | 341 | Pyridoxal phosphate1 Publication | 1 |
GO - Molecular functioni
- cystathionine beta-synthase activity Source: UniProtKB-EC
- cysteine synthase activity Source: UniProtKB-EC
- O-phosphoserine sulfhydrylase activity Source: UniProtKB-EC
GO - Biological processi
- cysteine biosynthetic process from serine Source: InterPro
Keywordsi
Molecular function | Lyase, Transferase |
Biological process | Amino-acid biosynthesis, Cysteine biosynthesis |
Ligand | Pyridoxal phosphate |
Enzyme and pathway databases
BRENDAi | 2.5.1.47, 171 2.5.1.65, 171 |
SABIO-RKi | Q9YBL2 |
UniPathwayi | UPA00136;UER00200 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:cysO Ordered Locus Names:APE_1586 |
Organismi | Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) |
Taxonomic identifieri | 272557 [NCBI] |
Taxonomic lineagei | Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000167131 | 2 – 389 | Protein CysOAdd BLAST | 388 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 127 | N6-(pyridoxal phosphate)lysine | 1 |
Interactioni
Subunit structurei
Homodimer.
2 PublicationsProtein-protein interaction databases
STRINGi | 272557.APE_1586 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q9YBL2 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9YBL2 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 261 – 265 | Pyridoxal phosphate binding | 5 |
Sequence similaritiesi
Belongs to the cysteine synthase/cystathionine beta-synthase family.Curated
Phylogenomic databases
eggNOGi | arCOG01430, Archaea |
OMAi | MWGAEII |
Family and domain databases
Gene3Di | 3.40.50.1100, 2 hits |
InterProi | View protein in InterPro IPR001216, P-phosphate_BS IPR001926, PLP-dep IPR036052, Trypto_synt_PLP_dependent |
Pfami | View protein in Pfam PF00291, PALP, 1 hit |
SUPFAMi | SSF53686, SSF53686, 1 hit |
PROSITEi | View protein in PROSITE PS00901, CYS_SYNTHASE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q9YBL2-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MALADISGYL DVLDSVRGFS YLENAREVLR SGEARCLGNP RSEPEYVKAL
60 70 80 90 100
YVIGASRIPV GDGCSHTLEE LGVFDISVPG EMVFPSPLDF FERGKPTPLV
110 120 130 140 150
RSRLQLPNGV RVWLKLEWYN PFSLSVKDRP AVEIISRLSR RVEKGSLVAD
160 170 180 190 200
ATSSNFGVAL SAVARLYGYR ARVYLPGAAE EFGKLLPRLL GAQVIVDPEA
210 220 230 240 250
PSTVHLLPRV MKDSKNEGFV HVNQFYNDAN FEAHMRGTAR EIFVQSRRGG
260 270 280 290 300
LALRGVAGSL GTSGHMSAAA FYLQSVDPSI RAVLVQPAQG DSIPGIRRVE
310 320 330 340 350
TGMLWINMLD ISYTLAEVTL EEAMEAVVEV ARSDGLVIGP SGGAAVKALA
360 370 380
KKAAEGDLEP GDYVVVVPDT GFKYLSLVQN ALEGAGDSV
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BA000002 Genomic DNA Translation: BAA80586.1 |
PIRi | E72537 |
Genome annotation databases
EnsemblBacteriai | BAA80586; BAA80586; APE_1586 |
KEGGi | ape:APE_1586 |
PATRICi | fig|272557.25.peg.1071 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BA000002 Genomic DNA Translation: BAA80586.1 |
PIRi | E72537 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1WKV | X-ray | 2.00 | A/B | 1-389 | [»] | |
3VSA | X-ray | 2.07 | A/B | 1-389 | [»] | |
3VSC | X-ray | 2.07 | A/B | 1-389 | [»] | |
3VSD | X-ray | 2.09 | A/B | 1-389 | [»] | |
5B36 | X-ray | 2.15 | A/B | 1-389 | [»] | |
5B3A | X-ray | 2.14 | A/B | 1-389 | [»] | |
6L0P | X-ray | 1.79 | A/B/C/D | 1-389 | [»] | |
6L0Q | X-ray | 1.58 | A/B/C/D | 1-389 | [»] | |
6L0R | X-ray | 1.79 | A/B/C/D | 1-389 | [»] | |
6L0S | X-ray | 1.96 | A/B/C/D | 1-389 | [»] | |
SMRi | Q9YBL2 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 272557.APE_1586 |
Genome annotation databases
EnsemblBacteriai | BAA80586; BAA80586; APE_1586 |
KEGGi | ape:APE_1586 |
PATRICi | fig|272557.25.peg.1071 |
Phylogenomic databases
eggNOGi | arCOG01430, Archaea |
OMAi | MWGAEII |
Enzyme and pathway databases
UniPathwayi | UPA00136;UER00200 |
BRENDAi | 2.5.1.47, 171 2.5.1.65, 171 |
SABIO-RKi | Q9YBL2 |
Miscellaneous databases
EvolutionaryTracei | Q9YBL2 |
Family and domain databases
Gene3Di | 3.40.50.1100, 2 hits |
InterProi | View protein in InterPro IPR001216, P-phosphate_BS IPR001926, PLP-dep IPR036052, Trypto_synt_PLP_dependent |
Pfami | View protein in Pfam PF00291, PALP, 1 hit |
SUPFAMi | SSF53686, SSF53686, 1 hit |
PROSITEi | View protein in PROSITE PS00901, CYS_SYNTHASE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CYSO_AERPE | |
Accessioni | Q9YBL2Primary (citable) accession number: Q9YBL2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 24, 2006 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 123 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families