B1XFY8 (SUFS_ECODH) 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
Ordered Locus Names:	ECDH10B_1814

Organism

Escherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP]

Taxonomic identifier

316385 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli › Escherichia coli (strain K12)

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Protein existence	Inferred 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. HAMAP-Rule MF_01831 L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor. HAMAP-Rule MF_01831
Cofactor	Pyridoxal phosphate By similarity.
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.
Subcellular location	Cytoplasm By similarity.
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	Complete proteome
Gene Ontology (GO)
Biological_process	cysteine metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cysteine desulfurase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro selenocysteine lyase activity Inferred from electronic annotation. Source: HAMAP
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_1000188298
Sites
	Active site	364	1	Cysteine persulfide intermediate By similarity
Amino acid modifications
	Modified residue	226	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	B1XFY8 [UniParc]. Last modified May 20, 2008. 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

[1]

"The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse." Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R. J. Bacteriol. 190:2597-2606(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / DH10B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000948 Genomic DNA. Translation: ACB02882.1.
RefSeq	YP_001730660.1. NC_010473.1.
3D structure databases
ProteinModelPortal	B1XFY8.
SMR	B1XFY8. Positions 2-406.
ModBase	Search...
Protein-protein interaction databases
STRING	316385.ECDH10B_1814.
Proteomic databases
PRIDE	B1XFY8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACB02882; ACB02882; ECDH10B_1814.
GeneID	6062160.
KEGG	ecd:ECDH10B_1814.
PATRIC	18463486. VBIEscCol59506_1838.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0520.
HOGENOM	HOG000017511.
KO	K11717.
OMA	GKHHAFD.
ProtClustDB	PRK09295.
Enzyme and pathway databases
BioCyc	ECOL316385:GJ8B-1766-MONOMER.
UniPathway	UPA00266.
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...

Entry information

Entry name

SUFS_ECODH

Accession

Primary (citable) accession number: B1XFY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	May 20, 2008
Last modified:	May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program