P77444 (SUFS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cysteine desulfurase
EC=2.8.1.7

Alternative name(s):
Selenocysteine beta-lyase
Short name=SCL
Selenocysteine lyase
EC=4.4.1.16
Selenocysteine reductase

Gene names

Name:	sufS
Synonyms:	csdB, ynhB
Ordered Locus Names:	b1680, JW1670

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	406 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11
Catalytic activity	L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. HAMAP-Rule MF_01831 L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor. HAMAP-Rule MF_01831
Cofactor	Pyridoxal phosphate.
Enzyme regulation	Displays a strong preference for selenocysteine as a substrate in vitro and is only very sightly active using cysteine. The interactions with SufE and the SufBCD complex act synergistically to enhance, up to 50-fold, its cysteine desulfurase activity. Ref.10 Ref.11 Ref.12
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. Ref.10 Ref.11 Ref.12
Subcellular location	Cytoplasm By similarity.
Induction	Suf operon is under both the Fe-dependent Fur repressor and the oxidative stress dependent OxyR activator. Ref.10 Ref.11 Ref.12
Sequence similarities	Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Lyase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cysteine metabolic process Inferred from electronic annotation. Source: InterPro iron-sulfur cluster assembly Inferred from direct assay PubMed 12686149. Source: EcoCyc selenium compound metabolic process Inferred from genetic interaction Ref.6. Source: EcoCyc sulfur compound metabolic process Inferred from direct assay PubMed 23068614. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cysteine desulfurase activity Inferred from direct assay Ref.1. Source: EcoCyc pyridoxal phosphate binding Inferred from direct assay Ref.1. Source: EcoCyc selenocysteine lyase activity Inferred from direct assay Ref.1. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 406

406

Cysteine desulfurase HAMAP-Rule MF_01831

PRO_0000150329

Sites

Active site

364

1

Cysteine persulfide intermediate

Amino acid modifications

Modified residue

226

1

N6-(pyridoxal phosphate)lysine HAMAP-Rule MF_01831

Experimental info

Mutagenesis

55

1

H → A: No effect. Ref.14

Mutagenesis

123

1

H → A: Loss of function; possibly due to destabilization of PLP in the active site. Ref.14

Mutagenesis

364

1

C → A: Abolishes activity towards L-cysteine but not towards selenocysteine. Ref.7

Mutagenesis

379

1

R → A: Loss of function. Ref.14

Secondary structure

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406

Helix Strand Turn

Details...

Helix

5 – 10

6

Helix

13 – 16

4

Turn

29 – 31

3

Helix

37 – 49

13

Helix

60 – 79

20

Helix

85 – 87

3

Beta strand

88 – 93

6

Helix

94 – 109

16

Beta strand

115 – 119

5

Helix

124 – 126

3

Helix

128 – 137

10

Beta strand

140 – 144

5

Helix

154 – 156

3

Helix

157 – 160

4

Beta strand

165 – 173

9

Turn

175 – 177

3

Helix

183 – 192

10

Beta strand

196 – 200

5

Turn

202 – 207

6

Helix

212 – 215

4

Beta strand

218 – 223

6

Helix

224 – 226

3

Beta strand

234 – 238

5

Helix

240 – 243

4

Beta strand

252 – 258

7

Turn

261 – 263

3

Beta strand

264 – 267

4

Helix

272 – 274

3

Helix

281 – 297

17

Helix

299 – 317

19

Beta strand

323 – 327

5

Beta strand

333 – 339

7

Helix

344 – 353

10

Beta strand

359 – 361

3

Helix

366 – 371

6

Beta strand

377 – 381

5

Helix

388 – 405

18

Sequences

	Sequence		Length	Mass (Da)
	P77444 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 9374C43C3AD9D8E3	FASTA	406	44,434
	10 20 30 40 50 60 MIFSVDKVRA DFPVLSREVN GLPLAYLDSA ASAQKPSQVI DAEAEFYRHG YAAVHRGIHT 70 80 90 100 110 120 LSAQATEKME NVRKRASLFI NARSAEELVF VRGTTEGINL VANSWGNSNV RAGDNIIISQ 130 140 150 160 170 180 MEHHANIVPW QMLCARVGAE LRVIPLNPDG TLQLETLPTL FDEKTRLLAI THVSNVLGTE 190 200 210 220 230 240 NPLAEMITLA HQHGAKVLVD GAQAVMHHPV 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary X-ray crystallographic studies." Mihara H., Maeda M., Fujii T., Kurihara T., Hata Y., Esaki N. J. Biol. Chem. 274:14768-14772(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, CHARACTERIZATION, X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). Strain: K12.
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"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.
[4]	"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.
[5]	"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.
[6]	"Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate." Lacourciere G.M., Mihara H., Kurihara T., Esaki N., Stadtman T.C. J. Biol. Chem. 275:23769-23773(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions." Mihara H., Kurihara T., Yoshimura T., Esaki N. J. Biochem. 127:559-567(2000) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-364.
[8]	"A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids." Takahashi Y., Tokumoto U. J. Biol. Chem. 277:28380-28383(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN FE-S CLUSTER SYSTEM.
[9]	"The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H." Mihara H., Kato S., Lacourciere G.M., Stadtman T.C., Kennedy R.A.J.D., Kurihara T., Tokumoto U., Takahashi Y., Esaki N. Proc. Natl. Acad. Sci. U.S.A. 99:6679-6683(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"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, ENZYME REGULATION, INTERACTION WITH SUFE AND SUFBCD COMPLEX. Strain: K12 / TG1.
[11]	"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, ENZYME REGULATION, INTERACTION WITH SUFE AND SUFBCD COMPLEX. Strain: K12 / MG1655 / ATCC 47076.
[12]	"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: ENZYME REGULATION, INTERACTION WITH SUFE.
[13]	"Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase." Fujii T., Maeda M., Mihara H., Kurihara T., Esaki N., Hata Y. Biochemistry 39:1263-1273(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[14]	"Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine." Mihara H., Fujii T., Kato S., Kurihara T., Hata Y., Esaki N. J. Biochem. 131:679-685(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), MUTAGENESIS OF HIS-55; HIS-123 AND ARG-379.
[15]	"Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural basis for perselenide and persulfide intermediate formation." Lima C.D. J. Mol. Biol. 315:1199-1208(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH L-CYSTEINE AND L-SELENOCYSTEINE, PYRIDOXAL PHOSPHATE AT LYS-226.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB055108 Genomic DNA. Translation: BAB21542.1.
U00096 Genomic DNA. Translation: AAC74750.1.
AP009048 Genomic DNA. Translation: BAA15457.1.

PIR

H64925.

RefSeq

NP_416195.1. NC_000913.2.
YP_489942.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C0N	X-ray	2.80	A	1-406	[»]
1I29	X-ray	2.80	A	1-406	[»]
1JF9	X-ray	2.00	A	1-406	[»]
1KMJ	X-ray	2.00	A	1-406	[»]
1KMK	X-ray	2.20	A	1-406	[»]

ProteinModelPortal

P77444.

SMR

P77444. Positions 2-406.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9324N.

IntAct

P77444. 7 interactions.

STRING

511145.b1680.

Proteomic databases

PaxDb

P77444.

PRIDE

P77444.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74750; AAC74750; b1680.
BAA15457; BAA15457; BAA15457.

GeneID

12931287.
946185.

KEGG

ecj:Y75_p1655.
eco:b1680.

PATRIC

32118666. VBIEscCol129921_1751.

Organism-specific databases

EchoBASE

EB3720.

EcoGene

EG13962. sufS.

Phylogenomic databases

eggNOG

COG0520.

HOGENOM

HOG000017511.

KO

K11717.

OMA

GKHHAFD.

ProtClustDB

PRK09295.

Enzyme and pathway databases

BioCyc

EcoCyc:G6906-MONOMER.
ECOL316407:JW1670-MONOMER.
MetaCyc:G6906-MONOMER.

UniPathway

UPA00266.

Gene expression databases

Genevestigator

P77444.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

HAMAP

MF_01831. SufS_aminotrans_5.

InterPro

IPR000192. 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]

Pfam

PF00266. Aminotran_5. 1 hit.
[Graphical view]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

TIGRFAMs

TIGR01979. sufS. 1 hit.

PROSITE

PS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P77444.

Entry information

Entry name

SUFS_ECOLI

Accession

Primary (citable) accession number: P77444

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program