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P33073 (SDHA_PEPAS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 62. 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, alpha chain

Short name=SDH
EC=4.3.1.17
Alternative name(s):
L-serine deaminase
Short name=L-SD
Gene names
Name:sdhA
OrganismPeptostreptococcus asaccharolyticus (Peptococcus asaccharolyticus)
Taxonomic identifier1258 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiales Family XI. Incertae SedisPeptoniphilus

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
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

Heterooctamer of four alpha chains and four beta chains.

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-UniPathway

   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 – 292292L-serine dehydratase, alpha chain
PRO_0000171915

Experimental info

Sequence conflict61Missing AA sequence Ref.2
Sequence conflict121C → Q AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P33073 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 4247702EEC932AE0

FASTA29230,770
        10         20         30         40         50         60 
MLNTAREIID VCNERGIKIY DLVLEEEIKN SHTTEEEIRK KLDAVIDVMH ASATKNLTQS 

        70         80         90        100        110        120 
DVTEYKMIDG FAKRTYEYAN SGKSIVGDFL AKAMAMAFST SEVNASMGKI VAAPTAGSSG 

       130        140        150        160        170        180 
IMPAMLVAAT EKYNFDRTTI QNGFLTSIGI GQVITKYATF AGAEGGCQAE CGSASAMAAA 

       190        200        210        220        230        240 
ALVEMLGGTV EQALHAASIT IINVLGLVCD PIAGLVQYPC TFRNASGVIN AFISADLALA 

       250        260        270        280        290 
GVESLVPFDE VVIAMGEVGN SMIEALRETG LGGLAGSKTG QKIRRDFLKE GD 

« Hide

References

[1]"Cloning and expression of the two genes coding for L-serine dehydratase from Peptostreptococcus asaccharolyticus: relationship of the iron-sulfur protein to both L-serine dehydratases from Escherichia coli."
Hofmeister A.E., Textor S., Buckel W.
J. Bacteriol. 179:4937-4941(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 14963 / DSM 20463 / NCIB 10074 / NCTC 11461.
[2]"Purification and properties of an iron-sulfur-containing and pyridoxal-phosphate-independent L-serine dehydratase from Peptostreptococcus asaccharolyticus."
Grabowski R., Buckel W.
Eur. J. Biochem. 199:89-94(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-23.
Strain: ATCC 14963 / DSM 20463 / NCIB 10074 / NCTC 11461.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U76260 Genomic DNA. Translation: AAC45546.1.
PIRS16224.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00138.

Family and domain databases

InterProIPR005130. Ser_deHydtase-like_asu.
IPR004642. Ser_deHydtase_asu.
[Graphical view]
PfamPF03313. SDH_alpha. 1 hit.
[Graphical view]
TIGRFAMsTIGR00718. sda_alpha. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSDHA_PEPAS
AccessionPrimary (citable) accession number: P33073
Secondary accession number(s): O33922
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: July 15, 1999
Last modified: April 3, 2013
This is version 62 of the entry and version 2 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