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P50846 (ALKH_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
KHG/KDPG aldolase

Including the following 2 domains:

  1. 4-hydroxy-2-oxoglutarate aldolase
    EC=4.1.3.16
    Alternative name(s):
    2-keto-4-hydroxyglutarate aldolase
    Short name=KHG-aldolase
  2. 2-dehydro-3-deoxy-phosphogluconate aldolase
    EC=4.1.2.14
    Alternative name(s):
    2-keto-3-deoxy-6-phosphogluconate aldolase
    Short name=KDPG-aldolase
    Phospho-2-dehydro-3-deoxygluconate aldolase
    Phospho-2-keto-3-deoxygluconate aldolase
Gene names
Name:kdgA
Ordered Locus Names:BSU22100
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate.

2-dehydro-3-deoxy-6-phosphate-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate.

Pathway

Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate: step 2/2.

Carbohydrate metabolism; glyoxylate and dicarboxylate metabolism.

Subunit structure

Homotrimer By similarity.

Subcellular location

Cytoplasm.

Induction

Induced by galacturonate and negatively regulated by the KdgR repressor. Is subject to catabolite repression by glucose involving the ccpA gene. Ref.3

Sequence similarities

Belongs to the KHG/KDPG aldolase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function2-dehydro-3-deoxy-phosphogluconate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

4-hydroxy-2-oxoglutarate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196KHG/KDPG aldolase
PRO_0000201036

Sites

Active site431 By similarity
Active site471 By similarity
Active site1301Schiff-base intermediate with KHG or pyruvate By similarity

Sequences

Sequence LengthMass (Da)Tools
P50846 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: EB0B597FD1102CC4

FASTA19620,865
        10         20         30         40         50         60 
MESKVVENRL KEAKLIAVIR SKDKQEACQQ IESLLDKGIR AVEVTYTTPG ASDIIESFRN 

        70         80         90        100        110        120 
REDILIGAGT VISAQQAGEA AKAGAQFIVS PGFSADLAEH LSFVKTHYIP GVLTPSEIME 

       130        140        150        160        170        180 
ALTFGFTTLK LFPSGVFGIP FMKNLAGPFP QVTFIPTGGI HPSEVPDWLR AGAGAVGVGS 

       190 
QLGSCSKEDL QAVFQV 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome."
Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D., Serror P.
Microbiology 142:2005-2016(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"The kdgRKAT operon of Bacillus subtilis: detection of the transcript and regulation by the kdgR and ccpA genes."
Pujic P., Dervyn R., Sorokin A., Ehrlich S.D.
Microbiology 144:3111-3118(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L47838 Genomic DNA. Translation: AAB38480.1.
AL009126 Genomic DNA. Translation: CAB14127.1.
PIRH69647.
RefSeqNP_390092.1. NC_000964.3.

3D structure databases

ProteinModelPortalP50846.
SMRP50846. Positions 2-193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU22100.

Proteomic databases

PaxDbP50846.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14127; CAB14127; BSU22100.
GeneID939066.
KEGGbsu:BSU22100.
PATRIC18976227. VBIBacSub10457_2304.

Organism-specific databases

GenoListBSU22100. [Micado]

Phylogenomic databases

eggNOGCOG0800.
HOGENOMHOG000233113.
KOK01625.
OMAQALACIE.
OrthoDBEOG6K9QNZ.
PhylomeDBP50846.

Enzyme and pathway databases

BioCycBSUB:BSU22100-MONOMER.
UniPathwayUPA00227.
UPA00856; UER00829.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR000887. Aldlse_KDPG_KHG.
IPR013785. Aldolase_TIM.
[Graphical view]
PfamPF01081. Aldolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01182. eda. 1 hit.
PROSITEPS00160. ALDOLASE_KDPG_KHG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALKH_BACSU
AccessionPrimary (citable) accession number: P50846
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList