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C6UIM0 (C6UIM0_ECOBR) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cysteine desulfurase RuleBase RU004506 HAMAP-Rule MF_01831
EC=2.8.1.7 RuleBase RU004506 HAMAP-Rule MF_01831
Alternative name(s):
Selenocysteine beta-lyase HAMAP-Rule MF_01831
Selenocysteine lyase HAMAP-Rule MF_01831
Selenocysteine reductase HAMAP-Rule MF_01831
Gene names
Name:sufS HAMAP-Rule MF_01831
Ordered Locus Names:ECB_01649
OrganismEscherichia coli (strain B / REL606) [Complete proteome] [HAMAP] EMBL ACT39313.1
Taxonomic identifier413997 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo By similarity. HAMAP-Rule MF_01831

Catalytic activity

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. SAAS SAAS010970 RuleBase RU004506 HAMAP-Rule MF_01831

L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor. HAMAP-Rule MF_01831

Cofactor

Pyridoxal phosphate By similarity. SAAS SAAS010970 HAMAP-Rule MF_01831 RuleBase RU004504

Pathway

Cofactor biosynthesis; iron-sulfur cluster biosynthesis. HAMAP-Rule MF_01831

Subunit structure

Homodimer. Interacts with SufE and the SufBCD complex composed of SufB, SufC and SufD. The interaction with SufE is required to mediate the direct transfer of the sulfur atom from the S-sulfanylcysteine By similarity. HAMAP-Rule MF_01831

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01831.

Sequence similarities

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily. HAMAP-Rule MF_01831

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site3641Cysteine persulfide intermediate By similarity HAMAP-Rule MF_01831

Amino acid modifications

Modified residue2261N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01831

Sequences

Sequence LengthMass (Da)Tools
C6UIM0 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: C9038728B22AC51D

FASTA40644,380
        10         20         30         40         50         60 
MTFSVDKVRA DFPVLSREVN GLPLAYLDSA ASAQKPGQVI DAEAEFYRHG YAAVHRGIHT 

        70         80         90        100        110        120 
LSAQATEKME NVRKQASLFI NARSAEELVF VRGTTEGINL VANSWGNSNV RAGDNIIISQ 

       130        140        150        160        170        180 
MEHHANIVPW QMLCARVGAE LRVIPLNPDG TLQLETLPTL FDEKTRLLAI THVSNVLGTE 

       190        200        210        220        230        240 
NPLAEMITLA HQHGAKVLVD GAQAVMHHLV DVQALDCDFY VFSGHKLYGP TGIGILYVKE 

       250        260        270        280        290        300 
ALLQEMPPWE GGGSMIATVS LSEGTTWTKA PWRFEAGTPN TGGIIGLGAA LEYVSALGLN 

       310        320        330        340        350        360 
NIAEYEQNLM HYALSQLESV PDLTLYGPQN RLGVIAFNLG KHHAYDVGSF LDNYGIAVRT 

       370        380        390        400 
GHHCAMPLMA YYNVPAMCRA SLAMYNTHEE VDRLVTGLQR IHRLLG

« Hide

References

[1]"Genome sequences of Escherichia coli B strains REL606 and BL21(DE3)."
Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A., Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B., Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F.
J. Mol. Biol. 394:644-652(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / REL606.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000819 Genomic DNA. Translation: ACT39313.1.
RefSeqYP_003044849.1. NC_012967.1.

3D structure databases

ProteinModelPortalC6UIM0.
SMRC6UIM0. Positions 3-406.
ModBaseSearch...

Protein-protein interaction databases

STRING413997.ECB_01649.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT39313; ACT39313; ECB_01649.
GeneID8176275.
KEGGebr:ECB_01649.
PATRIC18235390. VBIEscCol118196_1724.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0520.
HOGENOMHOG000017511.
KOK11717.
OMAGKHHAFD.
ProtClustDBPRK09295.

Enzyme and pathway databases

UniPathwayUPA00266.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01831. SufS_aminotrans_5.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR010970. Cys_dSase_SufS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01979. sufS. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC6UIM0_ECOBR
AccessionPrimary (citable) accession number: C6UIM0
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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