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Q9YBL2

- CYSO_AERPE

UniProt

Q9YBL2 - CYSO_AERPE

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Protein

Protein CysO

Gene

cysO

Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Cysteine synthase that can also catalyze the synthesis of S-sulfo-L-cysteine from thiosulfate and O(3)-acetyl-L-serine, as well as the sulfhydrylation of L-serine by sulfide.1 Publication

Catalytic activityi

O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate.
O-phospho-L-serine + H2S = L-cysteine + phosphate.
L-serine + L-homocysteine = L-cystathionine + H2O.

Cofactori

pyridoxal 5'-phosphate1 Publication

Kineticsi

  1. KM=28 mM for O(3)-acetyl-L-serine (in the presence of 1 mM sodium sulfide at pH 6.7 and 60 degrees Celsius)1 Publication
  2. KM=0.2 mM for sulfide (in the presence of 20 mM O(3)-acetyl-L-serine at pH 6.7 and 60 degrees Celsius)1 Publication
  3. 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
  4. 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
  5. KM=0.2 mM for sulfide (in the presence of 20 mM L-serine at pH 8.5 and 70 degrees Celsius)1 Publication
  6. KM=31 mM for L-serine (in the presence of 1 mM sodium sulfide at pH 8.5 and 70 degrees Celsius)1 Publication
  7. KM=13 mM for O(3)-acetyl-L-serine (in the presence of 20 mM thiosulfate at pH 6.1 and 85 degrees Celsius)1 Publication
  8. KM=21 mM for thiosulfate (in the presence of 20 mM O(3)-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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551Pyridoxal phosphate1 Publication
Binding sitei341 – 3411Pyridoxal phosphate1 Publication

GO - Molecular functioni

  1. cystathionine beta-synthase activity Source: UniProtKB-EC
  2. cysteine synthase activity Source: UniProtKB-EC
  3. O-phosphoserine sulfhydrylase activity Source: UniProtKB-EC

GO - Biological processi

  1. cysteine biosynthetic process from serine Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciAPER272557:GJD6-1077-MONOMER.
SABIO-RKQ9YBL2.
UniPathwayiUPA00136; UER00200.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein CysO
Alternative name(s):
Cystathionine beta-synthase (EC:4.2.1.22)
Cysteine synthase (EC:2.5.1.47)
O-acetylserine sulfhydrylase
O-phosphoserine sulfhydrylase (EC:2.5.1.65)
Serine sulfhydrase
Gene namesi
Name:cysO
Ordered Locus Names:APE_1586
OrganismiAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Taxonomic identifieri272557 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum
ProteomesiUP000002518: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 389388Protein CysOPRO_0000167131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei127 – 1271N6-(pyridoxal phosphate)lysine

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi272557.APE_1586.

Structurei

Secondary structure

1
389
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Helixi6 – 116Combined sources
Helixi12 – 154Combined sources
Helixi22 – 3110Combined sources
Beta strandi33 – 353Combined sources
Beta strandi37 – 393Combined sources
Helixi40 – 423Combined sources
Helixi44 – 5310Combined sources
Beta strandi56 – 638Combined sources
Beta strandi65 – 673Combined sources
Turni68 – 747Combined sources
Beta strandi83 – 864Combined sources
Helixi87 – 937Combined sources
Beta strandi99 – 1013Combined sources
Helixi107 – 1093Combined sources
Beta strandi110 – 1167Combined sources
Helixi117 – 1193Combined sources
Turni121 – 1233Combined sources
Helixi128 – 13811Combined sources
Turni139 – 1413Combined sources
Beta strandi147 – 1515Combined sources
Helixi154 – 16613Combined sources
Beta strandi170 – 1767Combined sources
Helixi181 – 1899Combined sources
Beta strandi193 – 1975Combined sources
Beta strandi201 – 2033Combined sources
Helixi204 – 2063Combined sources
Helixi207 – 21711Combined sources
Turni224 – 2263Combined sources
Helixi228 – 2369Combined sources
Helixi238 – 24811Combined sources
Beta strandi253 – 2586Combined sources
Beta strandi261 – 2633Combined sources
Helixi264 – 27613Combined sources
Beta strandi281 – 2877Combined sources
Helixi299 – 3013Combined sources
Helixi305 – 3084Combined sources
Beta strandi314 – 3185Combined sources
Helixi320 – 33415Combined sources
Helixi340 – 35415Combined sources
Beta strandi360 – 3678Combined sources
Helixi371 – 3733Combined sources
Helixi375 – 3828Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WKVX-ray2.00A/B1-389[»]
3VSAX-ray2.07A/B1-389[»]
3VSCX-ray2.07A/B1-389[»]
3VSDX-ray2.09A/B1-389[»]
ProteinModelPortaliQ9YBL2.
SMRiQ9YBL2. Positions 2-384.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9YBL2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni261 – 2655Pyridoxal phosphate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0031.
HOGENOMiHOG000217394.
KOiK10150.
OMAiHLEKDIR.

Family and domain databases

InterProiIPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9YBL2-1 [UniParc]FASTAAdd to Basket

« Hide

        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
Length:389
Mass (Da):41,981
Last modified:January 23, 2007 - v3
Checksum:iC103727AC1B9C72B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000002 Genomic DNA. Translation: BAA80586.1.
PIRiE72537.
RefSeqiNP_148041.1. NC_000854.2.
WP_010866467.1. NC_000854.2.

Genome annotation databases

EnsemblBacteriaiBAA80586; BAA80586; APE_1586.
GeneIDi1446114.
KEGGiape:APE_1586.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000002 Genomic DNA. Translation: BAA80586.1 .
PIRi E72537.
RefSeqi NP_148041.1. NC_000854.2.
WP_010866467.1. NC_000854.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q9YBL2.
SMRi Q9YBL2. Positions 2-384.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272557.APE_1586.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAA80586 ; BAA80586 ; APE_1586 .
GeneIDi 1446114.
KEGGi ape:APE_1586.

Phylogenomic databases

eggNOGi COG0031.
HOGENOMi HOG000217394.
KOi K10150.
OMAi HLEKDIR.

Enzyme and pathway databases

UniPathwayi UPA00136 ; UER00200 .
BioCyci APER272557:GJD6-1077-MONOMER.
SABIO-RK Q9YBL2.

Miscellaneous databases

EvolutionaryTracei Q9YBL2.

Family and domain databases

InterProi IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
[Graphical view ]
SUPFAMi SSF53686. SSF53686. 1 hit.
PROSITEi PS00901. CYS_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.
  2. "Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1."
    Mino K., Ishikawa K.
    J. Bacteriol. 185:2277-2284(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-8, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.
  3. "Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in L-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0 A resolution."
    Oda Y., Mino K., Ishikawa K., Ataka M.
    J. Mol. Biol. 351:334-344(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY.
    Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.

Entry informationi

Entry nameiCYSO_AERPE
AccessioniPrimary (citable) accession number: Q9YBL2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3