P76194 (SUFE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cysteine desulfuration protein SufE

Gene names

Name:	sufE
Synonyms:	ynhA
Ordered Locus Names:	b1679, JW1669

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	138 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Participates in cysteine desulfuration mediated by SufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for SufS, by mediating the direct transfer of the sulfur atom from the S-sulfanylcysteine of SufS, an intermediate product of cysteine desulfuration process. Together with the SufBCD complex, it thereby enhances up to 50-fold, the cysteine desulfurase activity of SufS. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Does not affect the selenocysteine lyase activity of SufS. Ref.4 Ref.5 Ref.6
Pathway	Cofactor biosynthesis; iron-sulfur cluster biosynthesis. HAMAP-Rule MF_01832
Subunit structure	Homodimer. Interacts with SufS. Ref.4 Ref.5 Ref.6
Subcellular location	Cytoplasm By similarity.
Induction	Suf operon is under both the Fe-dependent Fur repressor and the oxidative stress dependent OxyR activator. HAMAP-Rule MF_01832
Sequence similarities	Belongs to the SufE family.

Ontologies

Keywords
Cellular component	Cytoplasm
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	iron-sulfur cluster assembly Inferred from direct assay Ref.5. Source: EcoCyc sulfur compound metabolic process Inferred from direct assay Ref.5. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	enzyme activator activity Inferred from direct assay Ref.4. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 138

138

Cysteine desulfuration protein SufE HAMAP-Rule MF_01832

PRO_0000202124

Sites

Active site

51

1

Cysteine persulfide intermediate Probable

Experimental info

Mutagenesis

51

1

C → S: Abolishes cysteine desulfurase activity. Ref.4 Ref.5 Ref.6

Secondary structure

1

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138

Helix Strand Turn

Details...

Helix

7 – 16

10

Helix

20 – 33

14

Turn

39 – 41

3

Helix

44 – 46

3

Beta strand

50 – 53

4

Beta strand

55 – 61

7

Beta strand

63 – 65

3

Beta strand

67 – 75

9

Helix

76 – 88

13

Turn

89 – 91

3

Helix

94 – 99

6

Helix

103 – 109

7

Helix

111 – 114

4

Helix

117 – 138

22

Sequences

	Sequence		Length	Mass (Da)
	P76194 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: AD7B89A74C946772	FASTA	138	15,800
	10 20 30 40 50 60 MALLPDKEKL LRNFLRCANW EEKYLYIIEL GQRLPELRDE DRSPQNSIQG CQSQVWIVMR 70 80 90 100 110 120 QNAQGIIELQ GDSDAAIVKG LIAVVFILYD QMTPQDIVNF DVRPWFEKMA LTQHLTPSRS 130 QGLEAMIRAI RAKAAALS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"SufS is a NifS-like protein, and SufD is necessary for stability of the 2Fe-2S FhuF protein in Escherichia coli." Patzer S.I., Hantke K. J. Bacteriol. 181:3307-3309(1999) [PubMed] [Europe PMC] [Abstract] Cited for: GENE NAME. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase." Loiseau L., Ollagnier-de-Choudens S., Nachin L., Fontecave M., Barras F. J. Biol. Chem. 278:38352-38359(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SUFS, MUTAGENESIS OF CYS-51. Strain: K12 / TG1.
[5]	"The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli." Outten F.W., Wood M.J., Munoz F.M., Storz G. J. Biol. Chem. 278:45713-45719(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SUFS, MUTAGENESIS OF CYS-51. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Mechanistic studies of the SufS-SufE cysteine desulfurase: evidence for sulfur transfer from SufS to SufE." Ollagnier-de-Choudens S., Lascoux D., Loiseau L., Barras F., Forest E., Fontecave M. FEBS Lett. 555:263-267(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SUFS, MUTAGENESIS OF CYS-51.
[7]	"The SufE sulfur-acceptor protein contains a conserved core structure that mediates interdomain interactions in a variety of redox protein complexes." Goldsmith-Fischman S., Kuzin A., Edstrom W.C., Benach J., Shastry R., Xiao R., Acton T.B., Honig B., Montelione G.T., Hunt J.F. J. Mol. Biol. 344:549-565(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00096 Genomic DNA. Translation: AAC74749.1.
AP009048 Genomic DNA. Translation: BAE76500.1.

PIR

G64925.

RefSeq

NP_416194.1. NC_000913.2.
YP_489941.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MZG	X-ray	2.00	A/B	1-138	[»]

ProteinModelPortal

P76194.

SMR

P76194. Positions 2-126.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10941N.

IntAct

P76194. 4 interactions.

STRING

511145.b1679.

Proteomic databases

PaxDb

P76194.

PRIDE

P76194.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74749; AAC74749; b1679.
BAE76500; BAE76500; BAE76500.

GeneID

12931284.
946173.

KEGG

ecj:Y75_p1654.
eco:b1679.

PATRIC

32118664. VBIEscCol129921_1750.

Organism-specific databases

EchoBASE

EB3719.

EcoGene

EG13961. sufE.

Phylogenomic databases

eggNOG

COG2166.

HOGENOM

HOG000285040.

KO

K02426.

OMA

KVQGCAS.

ProtClustDB

PRK09296.

Enzyme and pathway databases

BioCyc

EcoCyc:G6905-MONOMER.
ECOL316407:JW1669-MONOMER.

UniPathway

UPA00266.

Gene expression databases

Genevestigator

P76194.

Family and domain databases

HAMAP

MF_01832. SufE.

InterPro

IPR023939. Cysteine_desulfuration_SufE.
IPR003808. Fe-S_metab-assoc_dom.
[Graphical view]

Pfam

PF02657. SufE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P76194.

Entry information

Entry name

SUFE_ECOLI

Accession

Primary (citable) accession number: P76194
Secondary accession number(s): Q2MB56

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program