C6DKM6 (SUFS_PECCP) 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:	PC1_2446

Organism

Pectobacterium carotovorum subsp. carotovorum (strain PC1) [Complete proteome] [HAMAP]

Taxonomic identifier

561230 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium › Erwinia carotovora › Pectobacterium carotovorum subsp. carotovorum

Protein attributes

Sequence length	407 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 – 407	407	Cysteine desulfurase HAMAP-Rule MF_01831		PRO_1000216076
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)
	C6DKM6 [UniParc]. Last modified September 1, 2009. Version 1. Checksum: 6A49BBED2E8B38FE	FASTA	407	44,415
	10 20 30 40 50 60 MSYPIERVRA DFPLLASEVN GQPLAYLDSA ASAQKPQSVI EREAEFYRHE YAAVHRGIHT 70 80 90 100 110 120 LSAQATSAME AVREQVAAFI NAASVEEIVF VRGTTEAINL VANSYGRTFI QPGDNLIITE 130 140 150 160 170 180 MEHHANIVPW QMLAEARGVE VRVLPLAEDG SLDVAQLPGL LDERTRLLAV TQISNVLGAL 190 200 210 220 230 240 NPVKTMIAQA KAVGAVTLVD GAQSIMHQTV DVQDLDCDFF VFSGHKIYGP SGIGVLYGKR 250 260 270 280 290 300 DLLQAMPPWE GGGAMIRQVS LRTGTTYADS PWRFEAGSPN TGGIMGLGAA LDYVTALGRE 310 320 330 340 350 360 EIQRYESSLM KYALEALKQV PDLTLYGPAE RHGVIAFNLG QHHAYDVGSF LDRYGIAIRT 370 380 390 400 GHHCAMPLME HYGVPSMCRA SLAVYTTREE IDRLVAGLQR IHRLLGS

References

[1]

"Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. , Balakrishnan V., Glasner J., Perna N.T. Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PC1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001657 Genomic DNA. Translation: ACT13477.1.
RefSeq	YP_003018013.1. NC_012917.1.
3D structure databases
ProteinModelPortal	C6DKM6.
ModBase	Search...
Protein-protein interaction databases
STRING	561230.PC1_2446.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACT13477; ACT13477; PC1_2446.
GeneID	8133392.
KEGG	pct:PC1_2446.
PATRIC	20489556. VBIPecCar70489_2462.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0520.
HOGENOM	HOG000017511.
KO	K11717.
OMA	NDAKERG.
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_PECCP

Accession

Primary (citable) accession number: C6DKM6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	September 1, 2009
Last modified:	May 1, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program