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O53078 (CITE_LEUMC) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 57. 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
OrganismLeuconostoc mesenteroides subsp. cremoris
Taxonomic identifier33965 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLeuconostoc

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Represents a citryl-ACP lyase By similarity.

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 By similarity.

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 – 302302Citrate lyase subunit beta
PRO_0000089760

Sites

Metal binding1321Magnesium By similarity
Metal binding1591Magnesium By similarity
Binding site691Substrate By similarity
Binding site1321Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O53078 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: E79C6D73DEDA1F7E

FASTA30233,376
        10         20         30         40         50         60 
MNNERLRRTM MFVPGNNPAM VKDAGIFGAD SIMFDLEDAV SLAEKDSARY LVYEALQTVD 

        70         80         90        100        110        120 
YGSSELVVRI NGLDTPFYKN DIKAMVKAGI DVIRLPKVET AAMMHELESL ITDAEKEFGR 

       130        140        150        160        170        180 
PVGTTHMMAA IESALGVVNA VEIANASDRM IGIALSAEDY TTDMKTHRYP DGQELLYARN 

       190        200        210        220        230        240 
VILHAARAAG IAAFDTVFTN LNDEEGFYRE TQLIHQLGFD GKSLINPRQI EMVNKVYAPT 

       250        260        270        280        290        300 
EKEINNAQNV IAAIEEAKQK GSGVISMNGQ MVDRPVVLRA QRVMKLANAN HLVDSEGNYI 


EK 

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References

[1]"Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster."
Bekal S., van Beeumen J., Samyn B., Garmyn D., Henini S., Divies C., Prevost H.
J. Bacteriol. 180:647-654(1998) [PubMed: 9457870] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 195.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y10621 Genomic DNA. Translation: CAA71632.1.

3D structure databases

ProteinModelPortalO53078.
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_LEUMC
AccessionPrimary (citable) accession number: O53078
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: October 19, 2011
This is version 57 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