Reviewed, UniProtKB/Swiss-Prot P44460 (CITE_HAEIN)

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
Ordered Locus Names:	HI0023

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	291 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
Technical term	Complete proteome
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 – 291	291	Citrate lyase subunit beta		PRO_0000089758
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

Sequences

	Sequence		Length	Mass (Da)
	P44460-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 9DB1B9D202CF221F	FASTA	291	31,855
	10 20 30 40 50 60 MKLRRSMLFV PGSNAAMLSN SFIYKPDSIM FDLEDAVALK EKDSARLLVA HALQHPLYKE 70 80 90 100 110 120 IETVVRVNPL DSEFGLLDLN SVVRAGVDVV RMPKTESAQD VLDMDHAITE IEKACGREAG 130 140 150 160 170 180 STKMLAAIES PLGITQANQI AFASKRLIGI ALGAEDYVRN LKTERSPEGI ELLFARCSIL 190 200 210 220 230 240 QAARAAGIQA FDTVYSNANN EEGFLKEAAL IKQLGFDGKS LINPRQIELL HNLFAPTQKD 250 260 270 280 290 VEQAKRIIEA AVEAERQGAG VVSLNGKMID APIIDRAKLV LERAKSGIRE E

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42023 Genomic DNA. Translation: AAC21701.1.
PIR	D64043.
RefSeq	NP_438196.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	950915.
GenomeReviews	Gene locus HI0023 in contig L42023_GR.
KEGG	hin:HI0023.
NMPDR	fig|71421.1.peg.22.
TIGR	HI0023.
Phylogenomic databases
HOGENOM	P44460.
OMA	IELLFAR.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0023-MON.
BRENDA	4.1.3.34. 109. 4.1.3.6. 109.
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_HAEIN

Accession

Primary (citable) accession number: P44460

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 62 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)