Reviewed, UniProtKB/Swiss-Prot P17725 (CITE_KLEPN)

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

Klebsiella pneumoniae

Taxonomic identifier

573 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella

Protein attributes

Sequence length	289 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Direct protein sequencing
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 – 289	289	Citrate lyase subunit beta		PRO_0000089759
Sites
	Metal binding	129	1	Magnesium By similarity
	Metal binding	156	1	Magnesium By similarity
	Binding site	66	1	Substrate By similarity
	Binding site	129	1	Substrate By similarity
Experimental info
	Sequence conflict	216	1	N → D AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P17725-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: C70A92DCAC3EABC2	FASTA	289	31,352
	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

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 / IFO 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 / IFO 13541 / NCTC 8172.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X79817 Genomic DNA. Translation: CAA56216.1.
PIR	S60775.
3D structure databases
SMR	P17725. Positions 2-234.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.1.3.34. 758. 4.1.3.6. 758.
Family and domain databases
InterPro	IPR011206. Citrate_lyase_beta. IPR006475. Citrate_lyase_beta_bac. IPR005000. HpcH_HpaI. 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_KLEPN

Accession

Primary (citable) accession number: P17725

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	November 1, 1995
Last modified:	February 9, 2010
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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