Q3Z233 (SUFS_SHISS) 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:	SSON_1476

Organism

Shigella sonnei (strain Ss046) [Complete proteome] [HAMAP]

Taxonomic identifier

300269 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella › Shigella sonnei

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_1000070431
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)
	Q3Z233 [UniParc]. Last modified September 27, 2005. Version 1. Checksum: DFB0AC19707DA6CF	FASTA	406	44,404
	10 20 30 40 50 60 MTFSVDKVRA 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 NPLAEIITLA 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]

"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery." Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q. Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ss046.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000038 Genomic DNA. Translation: AAZ88179.1.
RefSeq	YP_310414.1. NC_007384.1.
3D structure databases
HSSP	HSSP built from PDB template 1T3I based on UniProtKB Q55793.
ProteinModelPortal	Q3Z233.
SMR	Q3Z233. Positions 3-406.
ModBase	Search...
Protein-protein interaction databases
STRING	300269.SSON_1476.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAZ88179; AAZ88179; SSON_1476.
GeneID	3667121.
KEGG	ssn:SSON_1476.
PATRIC	18736836. VBIShiSon107113_1768.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0520.
HOGENOM	HOG000017511.
KO	K11717.
OMA	GKHHAFD.
ProtClustDB	PRK09295.
Enzyme and pathway databases
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_SHISS

Accession

Primary (citable) accession number: Q3Z233

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 27, 2005
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program