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P38947 (SUCD_CLOK5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. Feed History...

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

Protein namesRecommended name:
Succinate-semialdehyde dehydrogenase (acetylating)
EC=1.2.1.76
Gene names
Name:sucD
Ordered Locus Names:CKL_3015
OrganismClostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680) [Complete proteome] [HAMAP]
Taxonomic identifier431943 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reduction of succinate semialdehyde to succinyl-CoA. The enzyme is specific for succinate semialdehyde and succinyl-CoA, and only shows low activity with palmitoyl-CoA. There is no activity with NAD+ as cosubstrate.

Catalytic activity

Succinate semialdehyde + coenzyme A + NADP+ = succinyl-CoA + NADPH.

Subunit structure

Homodimer.

Biophysicochemical properties

Kinetic parameters:

KM=4.3 mM for NADPH

KM=3.2 mM for succinyl-CoA

KM=2.7 mM for succinate semialdehyde

KM=2.9 mM for CoA

KM=4.0 mM for NADP+

Vmax=28.9 µmol/min/mg enzyme toward NADPH

Vmax=28.9 µmol/min/mg enzyme toward succinyl-CoA

Vmax=28.3 µmol/min/mg enzyme toward succinate semialdehyde

Vmax=27.3 µmol/min/mg enzyme toward CoA

Vmax=31.2 µmol/min/mg enzyme toward NADP+

pH dependence:

Optimum pH is 7.0 for the reduction reaction and 8.5 for the oxidation reaction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 453453Succinate-semialdehyde dehydrogenase (acetylating)
PRO_0000072297

Regions

Nucleotide binding188 – 1936NADP By similarity

Sites

Active site2421 By similarity

Experimental info

Sequence conflict161V → A in AAA92347. Ref.1
Sequence conflict3791A → ARTVLPISRLVVNQPATTAG in AAA92347. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P38947 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: 61706F0AEBC865D7

FASTA45348,968
        10         20         30         40         50         60 
MSNEVSIKEL IEKAKVAQKK LEAYSQEQVD VLVKALGKVV YDNAEMFAKE AVEETEMGVY 

        70         80         90        100        110        120 
EDKVAKCHLK SGAIWNHIKD KKTVGIIKEE PERALVYVAK PKGVVAATTP ITNPVVTPMC 

       130        140        150        160        170        180 
NAMAAIKGRN TIIVAPHPKA KKVSAHTVEL MNAELKKLGA PENIIQIVEA PSREAAKELM 

       190        200        210        220        230        240 
ESADVVIATG GAGRVKAAYS SGRPAYGVGP GNSQVIVDKG YDYNKAAQDI ITGRKYDNGI 

       250        260        270        280        290        300 
ICSSEQSVIA PAEDYDKVIA AFVENGAFYV EDEETVEKFR STLFKDGKIN SKIIGKSVQI 

       310        320        330        340        350        360 
IADLAGVKVP EGTKVIVLKG KGAGEKDVLC KEKMCPVLVA LKYDTFEEAV EIAMANYMYE 

       370        380        390        400        410        420 
GAGHTAGIHS DNDENIRYAG TVLPISRLVV NQPATTAGGS FNNGFNPTTT LGCGSWGRNS 

       430        440        450 
ISENLTYEHL INVSRIGYFN KEAKVPSYEE IWG

« Hide

References

« Hide 'large scale' references
[1]"Molecular analysis of the anaerobic succinate degradation pathway in Clostridium kluyveri."
Soehling B., Gottschalk G.
J. Bacteriol. 178:871-880(1996) [PubMed: 8550525] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-24.
[2]"The genome of Clostridium kluyveri, a strict anaerobe with unique metabolic features."
Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H., Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F., Hagemeier C., Thauer R.K., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008) [PubMed: 18218779] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8527 / DSM 555 / NCIMB 10680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L21902 Genomic DNA. Translation: AAA92347.1.
CP000673 Genomic DNA. Translation: EDK35023.1.
RefSeqYP_001396394.1. NC_009706.1.

3D structure databases

ProteinModelPortalP38947.
ModBaseSearch...

Protein-protein interaction databases

STRINGP38947.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5394466.
GenomeReviewsGene locus CKL_3015 in contig CP000673_GR.
KEGGckl:CKL_3015.
PATRIC19467578. VBICloKlu111549_3119.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHBG373091.
OMASLSMGCG.
ProtClustDBCLSK922707.

Enzyme and pathway databases

BioCycCKLU431943:CKL_3015-MONOMER.
MetaCyc:MONOMER-13462.

Family and domain databases

InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 2 hits.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSUCD_CLOK5
AccessionPrimary (citable) accession number: P38947
Secondary accession number(s): A5N1M7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info