Reviewed, UniProtKB/Swiss-Prot O53078 (CITE_LEUMC)

Names and origin

Protein names

Recommended 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

Organism

Leuconostoc mesenteroides subsp. cremoris

Taxonomic identifier

33965 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Leuconostoc

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Gene Ontology (GO)
Biological process	acetyl-CoA metabolic process Inferred from electronic annotation. Source: InterPro cellular aromatic compound metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	citrate lyase complex Inferred from electronic annotation. Source: InterPro
Molecular function	citrate (pro-3S)-lyase activity Inferred from electronic annotation. Source: EC citryl-CoA lyase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 302	302	Citrate lyase subunit beta		PRO_0000089760
Sites
	Metal binding	132	1	Magnesium By similarity
	Metal binding	159	1	Magnesium By similarity
	Binding site	69	1	Substrate By similarity
	Binding site	132	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O53078-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: E79C6D73DEDA1F7E	FASTA	302	33,376
	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

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
SMR	O53078. Positions 4-238.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.1.3.34. 190084. 4.1.3.6. 190084.
Family and domain databases
InterPro	IPR011206. Citrate_lyase_beta. IPR006475. Citrate_lyase_beta_bac. IPR005000. HpcH_HpaI. IPR011076. Malate_synth-like_core. IPR015813. Pyrv/PenolPyrv_Kinase_cat. [Graphical view]
Gene3D	G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
Pfam	PF03328. HpcH_HpaI. 1 hit. [Graphical view]
PIRSF	PIRSF015582. Cit_lyase_B. 1 hit.
TIGRFAMs	TIGR01588. citE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CITE_LEUMC

Accession

Primary (citable) accession number: O53078

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 1, 1998
Last modified:	February 9, 2010
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)