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P80213 (SDHB_CLOPR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-serine dehydratase, beta chain

Short name=SDH
EC=4.3.1.17
Alternative name(s):
L-serine deaminase
Short name=L-SD
OrganismClostridium propionicum
Taxonomic identifier28446 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length29 AA.
Sequence statusFragment.
Protein existenceEvidence 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 processGluconeogenesis
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
   Molecular functionLyase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

L-serine ammonia-lyase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›29›29L-serine dehydratase, beta chain
PRO_0000171917

Experimental info

Non-terminal residue291

Sequences

Sequence LengthMass (Da)Tools
P80213 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: B1D75B67EAB83FC2

FASTA293,082
        10         20 
MLQVFDIIGP IMIGPSESIT AGAVRIXKI 

« Hide

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

PIRS34762.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR005131. Ser_deHydtase_bsu.
[Graphical view]
PfamPF03315. SDH_beta. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSDHB_CLOPR
AccessionPrimary (citable) accession number: P80213
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 31, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families