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P17725 (CITE_KLEPN) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Citrate lyase subunit beta

Short name=Citrase beta chain
EC=4.1.3.6
Alternative name(s):
Citrate (pro-3S)-lyase subunit beta
Citryl-CoA lyase subunit
EC=4.1.3.34
Gene names
Name:citE
OrganismKlebsiella pneumoniae
Taxonomic identifier573 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Represents a citryl-ACP lyase.

Catalytic activity

Citrate = acetate + oxaloacetate.

(3S)-citryl-CoA = acetyl-CoA + oxaloacetate.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Subunit structure

Oligomer with a subunit composition of (alpha,beta, gamma)6.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the HpcH/HpaI aldolase family. Citrate lyase beta subunit subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 289289Citrate lyase subunit beta
PRO_0000089759

Sites

Metal binding1291Magnesium By similarity
Metal binding1561Magnesium By similarity
Binding site661Substrate By similarity
Binding site1291Substrate By similarity

Experimental info

Sequence conflict2161N → D AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P17725 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: C70A92DCAC3EABC2

FASTA28931,352
        10         20         30         40         50         60 
MKPRRSMLFI PGANAAMLST SFVYGADAVM FDLEDAVSLR EKDTARLLVY QALQHPLYQD 

        70         80         90        100        110        120 
IETVVRINPL NTPFGLADLE AVVRAGVDMV RLPKTDSKED IHELEAHVER IERECGREVG 

       130        140        150        160        170        180 
STKLMAAIES ALGVVNAVEI ARASPRLAAI ALAAFDYVMD MGTSRGDGTE LFYARCAVLH 

       190        200        210        220        230        240 
AARVAGIAAY DVVWSDINNE EGFLAEANLA KNLGFNGKSL VNPRQIELLH QVYAPTRKEV 

       250        260        270        280 
DHALEVIAAA EEAETRGLGV VSLNGKMIDG PIIDHARKVV ALSASGIRD 

« Hide

References

[1]"Citrate lyase from Klebsiella pneumoniae. The complete primary structure of the acyl lyase subunit."
Hupperich M., Henschen A., Eggerer H.
Eur. J. Biochem. 192:161-166(1990) [PubMed: 2205500] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: ATCC 13882 / NBRC 13541 / NCTC 8172.
[2]"Klebsiella pneumoniae genes for citrate lyase and citrate lyase ligase: localization, sequencing, and expression."
Bott M., Dimroth P.
Mol. Microbiol. 14:347-356(1994) [PubMed: 7830578] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13882 / NBRC 13541 / NCTC 8172.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79817 Genomic DNA. Translation: CAA56216.1.
PIRS60775.

3D structure databases

ProteinModelPortalP17725.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR005000. Aldehyde-lyase_domain.
IPR011206. Citrate_lyase_beta.
IPR006475. Citrate_lyase_beta_bac.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
Gene3DG3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
PANTHERPTHR11105. PTHR11105. 1 hit.
PfamPF03328. HpcH_HpaI. 1 hit.
[Graphical view]
PIRSFPIRSF015582. Cit_lyase_B. 1 hit.
SUPFAMSSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR01588. CitE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCITE_KLEPN
AccessionPrimary (citable) accession number: P17725
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1995
Last modified: October 19, 2011
This is version 67 of the entry and version 2 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