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P44460 (CITE_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Ordered Locus Names:HI_0023
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length291 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 – 291291Citrate lyase subunit beta
PRO_0000089758

Sites

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

Sequences

Sequence LengthMass (Da)Tools
P44460 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 9DB1B9D202CF221F

FASTA29131,855
        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

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42023 Genomic DNA. Translation: AAC21701.1.
PIRD64043.
RefSeqNP_438196.2. NC_000907.1.

3D structure databases

ProteinModelPortalP44460.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID950915.
GenomeReviewsGene locus HI_0023 in contig L42023_GR.
KEGGhin:HI0023.
NMPDRfig|71421.1.peg.22.
PATRIC20188497. VBIHaeInf48452_0023.
TIGRHI_0023.

Phylogenomic databases

HOGENOMHBG676713.
OMATDMKTHR.
ProtClustDBCLSK874112.

Enzyme and pathway databases

BioCycHINF71421:HI_0023-MONOMER.

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.
KOK01644.
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_HAEIN
AccessionPrimary (citable) accession number: P44460
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

SIMILARITY comments

Index of protein domains and families

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