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P0AAB4 (UBID_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-octaprenyl-4-hydroxybenzoate carboxy-lyase

EC=4.1.1.-
Alternative name(s):
Polyprenyl p-hydroxybenzoate decarboxylase
Gene names
Name:ubiD
Synonyms:yigC, yigY
Ordered Locus Names:b3843, JW3819
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol. HAMAP-Rule MF_01636

Cofactor

Divalent metal ions. Preferably manganese.

Enzyme regulation

Requires phospholipid, a metal ion, dithiothreitol and at least one other so far unidentified soluble cofactor for maximal activity. Inhibited by EDTA. HAMAP-Rule MF_01636

Pathway

Cofactor biosynthesis; ubiquinone biosynthesis. HAMAP-Rule MF_01636

Subunit structure

Homohexamer Probable.

Subcellular location

Cell membrane; Peripheral membrane protein Probable HAMAP-Rule MF_01636.

Sequence similarities

Belongs to the UbiD family.

Sequence caution

The sequence AAA67639.1 differs from that shown. Reason: Frameshift at position 380.

The sequence CAA46146.1 differs from that shown. Reason: Frameshift at position 376.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4974973-octaprenyl-4-hydroxybenzoate carboxy-lyase HAMAP-Rule MF_01636
PRO_0000157357

Natural variations

Natural variant4521G → R in AN66; inactive protein. Ref.6

Secondary structure

.................................................................................... 497
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AAB4 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 5432A3BEBE81ECC5

FASTA49755,604
        10         20         30         40         50         60 
MDAMKYNDLR DFLTLLEQQG ELKRITLPVD PHLEITEIAD RTLRAGGPAL LFENPKGYSM 

        70         80         90        100        110        120 
PVLCNLFGTP KRVAMGMGQE DVSALREVGK LLAFLKEPEP PKGFRDLFDK LPQFKQVLNM 

       130        140        150        160        170        180 
PTKRLRGAPC QQKIVSGDDV DLNRIPIMTC WPEDAAPLIT WGLTVTRGPH KERQNLGIYR 

       190        200        210        220        230        240 
QQLIGKNKLI MRWLSHRGGA LDYQEWCAAH PGERFPVSVA LGADPATILG AVTPVPDTLS 

       250        260        270        280        290        300 
EYAFAGLLRG TKTEVVKCIS NDLEVPASAE IVLEGYIEQG ETAPEGPYGD HTGYYNEVDS 

       310        320        330        340        350        360 
FPVFTVTHIT QREDAIYHST YTGRPPDEPA VLGVALNEVF VPILQKQFPE IVDFYLPPEG 

       370        380        390        400        410        420 
CSYRLAVVTI KKQYAGHAKR VMMGVWSFLR QFMYTKFVIV CDDDVNARDW NDVIWAITTR 

       430        440        450        460        470        480 
MDPARDTVLV ENTPIDYLDF ASPVSGLGSK MGLDATNKWP GETQREWGRP IKKDPDVVAH 

       490 
IDAIWDELAI FNNGKSA 

« Hide

References

« Hide 'large scale' references
[1]"Escherichia coli HlyT protein, a transcriptional activator of haemolysin synthesis and secretion, is encoded by the rfaH (sfrB) locus required for expression of sex factor and lipopolysaccharide genes."
Bailey M.J.A., Koronakis V., Schmoll T., Hughes C.
Mol. Microbiol. 6:1003-1012(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 5KC.
[2]"Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Membrane-associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase."
Leppik R.A., Young I.G., Gibson F.
Biochim. Biophys. Acta 436:800-810(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: K12.
[6]"Identification of the ubiD gene on the Escherichia coli chromosome."
Zhang H., Javor G.T.
J. Bacteriol. 182:6243-6246(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS UBID, VARIANT AN66 ARG-452.
Strain: K12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65013 Genomic DNA. Translation: CAA46146.1. Frameshift.
M87049 Genomic DNA. Translation: AAA67639.1. Frameshift.
M87049 Genomic DNA. Translation: AAA67640.1.
U00096 Genomic DNA. Translation: AAC76846.1.
AP009048 Genomic DNA. Translation: BAE77460.1.
PIRD65189.
S20905.
S30734.
RefSeqNP_418285.1. NC_000913.3.
YP_491601.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IDBX-ray2.90A/B/C1-497[»]
ProteinModelPortalP0AAB4.
SMRP0AAB4. Positions 6-491.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48249N.
IntActP0AAB4. 4 interactions.
STRING511145.b3843.

Proteomic databases

PaxDbP0AAB4.
PRIDEP0AAB4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76846; AAC76846; b3843.
BAE77460; BAE77460; BAE77460.
GeneID12932472.
948326.
KEGGecj:Y75_p3337.
eco:b3843.
PATRIC32123183. VBIEscCol129921_3957.

Organism-specific databases

EchoBASEEB1369.
EcoGeneEG11396. ubiD.

Phylogenomic databases

eggNOGCOG0043.
KOK03182.
OMAKMGMDAT.
OrthoDBEOG6QZMM7.
PhylomeDBP0AAB4.
ProtClustDBPRK10922.

Enzyme and pathway databases

BioCycEcoCyc:EG11396-MONOMER.
ECOL316407:JW3819-MONOMER.
MetaCyc:EG11396-MONOMER.
UniPathwayUPA00232.

Gene expression databases

GenevestigatorP0AAB4.

Family and domain databases

HAMAPMF_01636. UbiD.
InterProIPR023677. OPHB_Carboxy-lyase.
IPR012349. Split_barrel_FMN-bd.
IPR002830. UbiD.
[Graphical view]
PfamPF01977. UbiD. 1 hit.
[Graphical view]
SUPFAMSSF50475. SSF50475. 1 hit.
TIGRFAMsTIGR00148. TIGR00148. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0AAB4.
PROP0AAB4.

Entry information

Entry nameUBID_ECOLI
AccessionPrimary (citable) accession number: P0AAB4
Secondary accession number(s): P26615 expand/collapse secondary AC list , P27861, P76767, Q2M8E6, Q47265, Q47714
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: April 16, 2014
This is version 82 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene