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Protein

Cysteine synthase B

Gene

cysM

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product.

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 B (cysM), Cysteine synthase A (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 sitei71 – 711Pyridoxal phosphate1 Publication
Binding sitei255 – 2551Pyridoxal phosphate1 Publication

GO - Molecular functioni

  • cysteine synthase activity Source: EcoCyc
  • L-cysteine desulfhydrase activity Source: EcoCyc
  • pyridoxal phosphate binding Source: GO_Central
  • transferase activity Source: UniProtKB-KW

GO - Biological processi

  • cysteine biosynthetic process from serine Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:ACSERLYB-MONOMER.
ECOL316407:JW2414-MONOMER.
MetaCyc:ACSERLYB-MONOMER.
BRENDAi2.5.1.47. 2026.
SABIO-RKP16703.
UniPathwayiUPA00136; UER00200.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine synthase B (EC:2.5.1.47)
Short name:
CSase B
Alternative name(s):
O-acetylserine (thiol)-lyase B
Short name:
OAS-TL B
O-acetylserine sulfhydrylase B
Gene namesi
Name:cysM
Ordered Locus Names:b2421, JW2414
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10193. cysM.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Cysteine synthase BPRO_0000167108Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411N6-(pyridoxal phosphate)lysine

Proteomic databases

PaxDbiP16703.

2D gel databases

SWISS-2DPAGEP16703.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4259326. 6 interactions.
DIPiDIP-9383N.
IntActiP16703. 21 interactions.
MINTiMINT-1300981.
STRINGi511145.b2421.

Structurei

Secondary structure

1
303
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 74Combined sources
Beta strandi13 – 153Combined sources
Beta strandi17 – 204Combined sources
Beta strandi22 – 243Combined sources
Beta strandi26 – 316Combined sources
Helixi32 – 343Combined sources
Helixi41 – 5414Combined sources
Beta strandi63 – 675Combined sources
Helixi71 – 8313Combined sources
Beta strandi86 – 927Combined sources
Helixi97 – 1059Combined sources
Beta strandi109 – 1135Combined sources
Turni115 – 1173Combined sources
Helixi118 – 13114Combined sources
Beta strandi134 – 1374Combined sources
Turni140 – 1423Combined sources
Helixi145 – 1528Combined sources
Helixi154 – 1618Combined sources
Turni162 – 1643Combined sources
Beta strandi168 – 1725Combined sources
Beta strandi174 – 1763Combined sources
Helixi177 – 18711Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi194 – 2007Combined sources
Helixi214 – 2163Combined sources
Helixi223 – 2253Combined sources
Beta strandi227 – 2326Combined sources
Helixi234 – 24815Combined sources
Helixi254 – 26916Combined sources
Beta strandi274 – 2796Combined sources
Beta strandi281 – 2833Combined sources
Helixi284 – 2896Combined sources
Turni290 – 2923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BHSX-ray2.67A/B/C/D1-303[»]
2BHTX-ray2.10A/B/C/D1-303[»]
2V03X-ray1.33A1-303[»]
ProteinModelPortaliP16703.
SMRiP16703. Positions 2-293.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16703.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni174 – 1785Pyridoxal phosphate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C6T. Bacteria.
COG0031. LUCA.
HOGENOMiHOG000217394.
InParanoidiP16703.
KOiK12339.
OMAiFTTTGPE.
PhylomeDBiP16703.

Family and domain databases

InterProiIPR005856. Cys_synth.
IPR005858. CysM.
IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01136. cysKM. 1 hit.
TIGR01138. cysM. 1 hit.
PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16703-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTLEQTIGN TPLVKLQRMG PDNGSEVWLK LEGNNPAGSV KDRAALSMIV
60 70 80 90 100
EAEKRGEIKP GDVLIEATSG NTGIALAMIA ALKGYRMKLL MPDNMSQERR
110 120 130 140 150
AAMRAYGAEL ILVTKEQGME GARDLALEMA NRGEGKLLDQ FNNPDNPYAH
160 170 180 190 200
YTTTGPEIWQ QTGGRITHFV SSMGTTGTIT GVSRFMREQS KPVTIVGLQP
210 220 230 240 250
EEGSSIPGIR RWPTEYLPGI FNASLVDEVL DIHQRDAENT MRELAVREGI
260 270 280 290 300
FCGVSSGGAV AGALRVAKAN PDAVVVAIIC DRGDRYLSTG VFGEEHFSQG

AGI
Length:303
Mass (Da):32,664
Last modified:August 1, 1990 - v1
Checksum:i1C7FBCB943FCFE39
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32101 Genomic DNA. Translation: AAA23640.1.
U00096 Genomic DNA. Translation: AAC75474.1.
AP009048 Genomic DNA. Translation: BAA16295.1.
PIRiD35402. SYECBC.
RefSeqiNP_416916.1. NC_000913.3.
WP_001336044.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75474; AAC75474; b2421.
BAA16295; BAA16295; BAA16295.
GeneIDi946888.
KEGGiecj:JW2414.
eco:b2421.
PATRICi32120227. VBIEscCol129921_2516.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32101 Genomic DNA. Translation: AAA23640.1.
U00096 Genomic DNA. Translation: AAC75474.1.
AP009048 Genomic DNA. Translation: BAA16295.1.
PIRiD35402. SYECBC.
RefSeqiNP_416916.1. NC_000913.3.
WP_001336044.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BHSX-ray2.67A/B/C/D1-303[»]
2BHTX-ray2.10A/B/C/D1-303[»]
2V03X-ray1.33A1-303[»]
ProteinModelPortaliP16703.
SMRiP16703. Positions 2-293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259326. 6 interactions.
DIPiDIP-9383N.
IntActiP16703. 21 interactions.
MINTiMINT-1300981.
STRINGi511145.b2421.

2D gel databases

SWISS-2DPAGEP16703.

Proteomic databases

PaxDbiP16703.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75474; AAC75474; b2421.
BAA16295; BAA16295; BAA16295.
GeneIDi946888.
KEGGiecj:JW2414.
eco:b2421.
PATRICi32120227. VBIEscCol129921_2516.

Organism-specific databases

EchoBASEiEB0190.
EcoGeneiEG10193. cysM.

Phylogenomic databases

eggNOGiENOG4105C6T. Bacteria.
COG0031. LUCA.
HOGENOMiHOG000217394.
InParanoidiP16703.
KOiK12339.
OMAiFTTTGPE.
PhylomeDBiP16703.

Enzyme and pathway databases

UniPathwayiUPA00136; UER00200.
BioCyciEcoCyc:ACSERLYB-MONOMER.
ECOL316407:JW2414-MONOMER.
MetaCyc:ACSERLYB-MONOMER.
BRENDAi2.5.1.47. 2026.
SABIO-RKP16703.

Miscellaneous databases

EvolutionaryTraceiP16703.
PROiP16703.

Family and domain databases

InterProiIPR005856. Cys_synth.
IPR005858. CysM.
IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01136. cysKM. 1 hit.
TIGR01138. cysM. 1 hit.
PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCYSM_ECOLI
AccessioniPrimary (citable) accession number: P16703
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: September 7, 2016
This is version 154 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, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.