P50846 (ALKH_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	196 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate. 2-dehydro-3-deoxy-D-gluconate 6-phosphate = 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 component	Cytoplasm
Ligand	Schiff base
Molecular function	Lyase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	2-dehydro-3-deoxy-phosphogluconate aldolase activity Inferred from electronic annotation. Source: EC 4-hydroxy-2-oxoglutarate aldolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 196	196	KHG/KDPG aldolase		PRO_0000201036
Sites
	Active site	43	1	By similarity
	Active site	47	1	By similarity
	Active site	130	1	Schiff-base intermediate with KHG or pyruvate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P50846 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: EB0B597FD1102CC4	FASTA	196	20,865
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	H69647.
RefSeq	NP_390092.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P50846.
SMR	P50846. Positions 2-193.
ModBase	Search...
Protein-protein interaction databases
STRING	224308.BSU22100.
Proteomic databases
PaxDb	P50846.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB14127; CAB14127; BSU22100.
GeneID	939066.
KEGG	bsu:BSU22100.
PATRIC	18976227. VBIBacSub10457_2304.
Organism-specific databases
GenoList	BSU22100. [Micado]
Phylogenomic databases
eggNOG	COG0800.
HOGENOM	HOG000233113.
KO	K01625.
OMA	KGLMAPM.
ProtClustDB	CLSK887480.
Enzyme and pathway databases
BioCyc	BSUB:BSU22100-MONOMER.
UniPathway	UPA00227. UPA00856; UER00829.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR000887. Aldlse_KDPG_KHG. IPR013785. Aldolase_TIM. [Graphical view]
Pfam	PF01081. Aldolase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01182. eda. 1 hit.
PROSITE	PS00159. ALDOLASE_KDPG_KHG_1. False negative. PS00160. ALDOLASE_KDPG_KHG_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALKH_BACSU

Accession

Primary (citable) accession number: P50846

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program