Reviewed, UniProtKB/Swiss-Prot P80213 (SDHB_CLOPR)

Names and origin

Protein names	Recommended name:     L-serine dehydratase, beta chain       Short name=SDH     EC=4.3.1.17 Alternative name(s):     L-serine deaminase       Short name=L-SD
Organism	Clostridium propionicum
Taxonomic identifier	28446 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	29 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-serine = pyruvate + NH3.
Cofactor	Binds 1 4Fe-4S cluster.
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Subunit structure	Heterodimer of an alpha chain and a beta chain.
Sequence similarities	Belongs to the iron-sulfur dependent L-serine dehydratase family.

Ontologies

Keywords
Biological process	Gluconeogenesis
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW L-serine ammonia-lyase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›29	›29	L-serine dehydratase, beta chain		PRO_0000171917
Experimental info
	Non-terminal residue	29	1

Sequences

	Sequence		Length	Mass (Da)
	P80213-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: B1D75B67EAB83FC2	FASTA	29	3,082
	10 20 MLQVFDIIGP IMIGPSESIT AGAVRIXKI

References

[1]

"L-serine and L-threonine dehydratase from Clostridium propionicum. Two enzymes with different prosthetic groups." Hofmeister A.E.M., Grabowski R., Linder D., Buckel W. Eur. J. Biochem. 215:341-349(1993) [PubMed: 8344301] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: ATCC 25522 / DSM 1682 / NCIB 10656 / VPI 5303.

Cross-references

Sequence databases
PIR	S34762.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.3.1.17. 20911.
Family and domain databases
InterPro	IPR005131. Ser_deHydtase_bsu. [Graphical view]
Pfam	PF03315. SDH_beta. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SDHB_CLOPR

Accession

Primary (citable) accession number: P80213

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)