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Protein

Cysteine synthase

Gene

cysK

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate.

Cofactori

Pathwayi: L-cysteine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-cysteine from L-serine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Serine acetyltransferase (cysE)
  2. Cysteine synthase (cysK)
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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei7 – 71Allosteric inhibitorBy similarity
Binding sitei72 – 721Pyridoxal phosphateBy similarity
Binding sitei268 – 2681Allosteric inhibitor; via amide nitrogenBy similarity
Binding sitei272 – 2721Pyridoxal phosphateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.5.1.47. 2529.
UniPathwayiUPA00136; UER00200.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine synthase (EC:2.5.1.47)
Short name:
CSase
Alternative name(s):
O-acetylserine (thiol)-lyase
Short name:
OAS-TL
O-acetylserine sulfhydrylase
Gene namesi
Name:cysK
Ordered Locus Names:HI_1103
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
Proteomesi
  • UP000000579 Componenti: Chromosome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075088.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Cysteine synthasePRO_0000167090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiP45040.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi71421.HI1103.

Chemistry

BindingDBiP45040.

Structurei

Secondary structure

1
316
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 104Combined sources
Beta strandi16 – 183Combined sources
Beta strandi20 – 245Combined sources
Beta strandi28 – 325Combined sources
Helixi37 – 393Combined sources
Helixi42 – 5514Combined sources
Beta strandi64 – 685Combined sources
Helixi72 – 8413Combined sources
Beta strandi88 – 936Combined sources
Beta strandi94 – 974Combined sources
Helixi98 – 1069Combined sources
Beta strandi110 – 1145Combined sources
Helixi116 – 1183Combined sources
Helixi119 – 13315Combined sources
Turni135 – 1373Combined sources
Beta strandi138 – 1403Combined sources
Turni143 – 1453Combined sources
Helixi148 – 1558Combined sources
Helixi157 – 1648Combined sources
Turni165 – 1673Combined sources
Beta strandi169 – 1757Combined sources
Beta strandi177 – 1793Combined sources
Helixi180 – 19112Combined sources
Beta strandi198 – 2047Combined sources
Helixi209 – 2157Combined sources
Helixi240 – 2423Combined sources
Beta strandi245 – 2495Combined sources
Helixi251 – 26515Combined sources
Helixi271 – 28414Combined sources
Helixi287 – 2893Combined sources
Beta strandi293 – 2986Combined sources
Helixi302 – 3054Combined sources
Turni308 – 3103Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y7LX-ray1.55A1-316[»]
3IQGX-ray1.90X1-316[»]
3IQHX-ray1.90X1-316[»]
3IQIX-ray1.70X1-316[»]
4HO1X-ray1.86X1-316[»]
4LI3X-ray2.59X1-316[»]
4NU8X-ray2.07X1-316[»]
4OREX-ray2.20X1-316[»]
4ZU1X-ray2.20X1-316[»]
4ZU6X-ray2.03X1-316[»]
5DBEX-ray2.25X1-316[»]
5DBHX-ray1.98X1-316[»]
ProteinModelPortaliP45040.
SMRiP45040. Positions 2-311.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45040.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni177 – 1815Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C6T. Bacteria.
COG0031. LUCA.
KOiK01738.
OMAiVKCRIGS.
OrthoDBiEOG6Q2SP8.
PhylomeDBiP45040.

Family and domain databases

InterProiIPR005856. Cys_synth.
IPR005859. CysK.
IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01139. cysK. 1 hit.
TIGR01136. cysKM. 1 hit.
PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P45040-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIYADNSYS IGNTPLVRLK HFGHNGNVVV KIEGRNPSYS VKCRIGANMV
60 70 80 90 100
WQAEKDGTLT KGKEIVDATS GNTGIALAYV AAARGYKITL TMPETMSLER
110 120 130 140 150
KRLLCGLGVN LVLTEGAKGM KGAIAKAEEI VASDPSRYVM LKQFENPANP
160 170 180 190 200
QIHRETTGPE IWKDTDGKVD VVVAGVGTGG SITGISRAIK LDFGKQITSV
210 220 230 240 250
AVEPVESPVI SQTLAGEEVK PGPHKIQGIG AGFIPKNLDL SIIDRVETVD
260 270 280 290 300
SDTALATARR LMAEEGILAG ISSGAAVAAA DRLAKLPEFA DKLIVVILPS
310
ASERYLSTAL FEGIEG
Length:316
Mass (Da):33,384
Last modified:November 1, 1995 - v1
Checksum:iCA753FC79BBD05BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22758.1.
PIRiF64182.
RefSeqiNP_439260.1. NC_000907.1.
WP_005693427.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22758; AAC22758; HI_1103.
GeneIDi950077.
KEGGihin:HI1103.
PATRICi20190873. VBIHaeInf48452_1149.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22758.1.
PIRiF64182.
RefSeqiNP_439260.1. NC_000907.1.
WP_005693427.1. NC_000907.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y7LX-ray1.55A1-316[»]
3IQGX-ray1.90X1-316[»]
3IQHX-ray1.90X1-316[»]
3IQIX-ray1.70X1-316[»]
4HO1X-ray1.86X1-316[»]
4LI3X-ray2.59X1-316[»]
4NU8X-ray2.07X1-316[»]
4OREX-ray2.20X1-316[»]
4ZU1X-ray2.20X1-316[»]
4ZU6X-ray2.03X1-316[»]
5DBEX-ray2.25X1-316[»]
5DBHX-ray1.98X1-316[»]
ProteinModelPortaliP45040.
SMRiP45040. Positions 2-311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI1103.

Chemistry

BindingDBiP45040.
ChEMBLiCHEMBL1075088.

Proteomic databases

PRIDEiP45040.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC22758; AAC22758; HI_1103.
GeneIDi950077.
KEGGihin:HI1103.
PATRICi20190873. VBIHaeInf48452_1149.

Phylogenomic databases

eggNOGiENOG4105C6T. Bacteria.
COG0031. LUCA.
KOiK01738.
OMAiVKCRIGS.
OrthoDBiEOG6Q2SP8.
PhylomeDBiP45040.

Enzyme and pathway databases

UniPathwayiUPA00136; UER00200.
BRENDAi2.5.1.47. 2529.

Miscellaneous databases

EvolutionaryTraceiP45040.

Family and domain databases

InterProiIPR005856. Cys_synth.
IPR005859. CysK.
IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01139. cysK. 1 hit.
TIGR01136. cysKM. 1 hit.
PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
  2. "The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase."
    Huang B., Vetting M.W., Roderick S.L.
    J. Bacteriol. 187:3201-3205(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH SAT.

Entry informationi

Entry nameiCYSK_HAEIN
AccessioniPrimary (citable) accession number: P45040
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 17, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.