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P0AAB4

- UBID_ECOLI

UniProt

P0AAB4 - UBID_ECOLI

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Protein

3-octaprenyl-4-hydroxybenzoate carboxy-lyase

Gene

ubiD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol.1 Publication

Cofactori

Mn2+1 PublicationNote: Divalent metal ions. Preferably manganese.1 Publication

Enzyme regulationi

Requires phospholipid, a metal ion, dithiothreitol and at least one other so far unidentified soluble cofactor for maximal activity. Inhibited by EDTA.1 Publication

Pathwayi

GO - Molecular functioni

  1. 3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity Source: EcoCyc
  2. FMN binding Source: InterPro
  3. identical protein binding Source: EcoCyc
  4. oxidoreductase activity Source: InterPro

GO - Biological processi

  1. ubiquinone biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Ubiquinone biosynthesis

Keywords - Ligandi

Manganese

Enzyme and pathway databases

BioCyciEcoCyc:EG11396-MONOMER.
ECOL316407:JW3819-MONOMER.
MetaCyc:EG11396-MONOMER.
UniPathwayiUPA00232.

Names & Taxonomyi

Protein namesi
Recommended name:
3-octaprenyl-4-hydroxybenzoate carboxy-lyase (EC:4.1.1.-)
Alternative name(s):
Polyprenyl p-hydroxybenzoate decarboxylase
Gene namesi
Name:ubiD
Synonyms:yigC, yigY
Ordered Locus Names:b3843, JW3819
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11396. ubiD.

Subcellular locationi

Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4974973-octaprenyl-4-hydroxybenzoate carboxy-lyasePRO_0000157357Add
BLAST

Proteomic databases

PaxDbiP0AAB4.
PRIDEiP0AAB4.

Expressioni

Gene expression databases

GenevestigatoriP0AAB4.

Interactioni

Subunit structurei

Homohexamer.1 Publication

Protein-protein interaction databases

DIPiDIP-48249N.
IntActiP0AAB4. 4 interactions.
STRINGi511145.b3843.

Structurei

Secondary structure

1
497
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1810Combined sources
Beta strandi22 – 254Combined sources
Helixi34 – 4310Combined sources
Beta strandi49 – 535Combined sources
Beta strandi62 – 643Combined sources
Helixi70 – 756Combined sources
Turni76 – 783Combined sources
Helixi82 – 843Combined sources
Helixi85 – 9612Combined sources
Beta strandi123 – 1275Combined sources
Helixi129 – 1313Combined sources
Beta strandi132 – 1365Combined sources
Helixi137 – 1393Combined sources
Helixi142 – 1443Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi174 – 1774Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi185 – 1917Combined sources
Beta strandi195 – 1973Combined sources
Helixi198 – 20912Combined sources
Beta strandi215 – 2228Combined sources
Helixi225 – 2328Combined sources
Helixi241 – 2499Combined sources
Beta strandi254 – 2574Combined sources
Beta strandi259 – 2624Combined sources
Beta strandi264 – 2663Combined sources
Beta strandi270 – 28516Combined sources
Beta strandi293 – 2964Combined sources
Beta strandi299 – 31113Combined sources
Beta strandi324 – 3263Combined sources
Helixi328 – 34720Combined sources
Beta strandi351 – 3555Combined sources
Helixi358 – 3603Combined sources
Turni361 – 3633Combined sources
Beta strandi364 – 3707Combined sources
Helixi377 – 38711Combined sources
Helixi390 – 3923Combined sources
Beta strandi397 – 4026Combined sources
Helixi410 – 41910Combined sources
Helixi423 – 4264Combined sources
Beta strandi427 – 4348Combined sources
Beta strandi442 – 4443Combined sources
Beta strandi447 – 4548Combined sources
Beta strandi463 – 4653Combined sources
Helixi475 – 48410Combined sources
Turni485 – 4873Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IDBX-ray2.90A/B/C1-497[»]
ProteinModelPortaliP0AAB4.
SMRiP0AAB4. Positions 6-491.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AAB4.

Family & Domainsi

Sequence similaritiesi

Belongs to the UbiD family.Curated

Phylogenomic databases

eggNOGiCOG0043.
InParanoidiP0AAB4.
KOiK03182.
OMAiSKMGMDA.
OrthoDBiEOG6QZMM7.
PhylomeDBiP0AAB4.

Family and domain databases

HAMAPiMF_01636. UbiD.
InterProiIPR023677. OPHB_Carboxy-lyase.
IPR012349. Split_barrel_FMN-bd.
IPR002830. UbiD.
[Graphical view]
PfamiPF01977. UbiD. 1 hit.
[Graphical view]
SUPFAMiSSF50475. SSF50475. 1 hit.
TIGRFAMsiTIGR00148. TIGR00148. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AAB4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDAMKYNDLR DFLTLLEQQG ELKRITLPVD PHLEITEIAD RTLRAGGPAL
60 70 80 90 100
LFENPKGYSM PVLCNLFGTP KRVAMGMGQE DVSALREVGK LLAFLKEPEP
110 120 130 140 150
PKGFRDLFDK LPQFKQVLNM PTKRLRGAPC QQKIVSGDDV DLNRIPIMTC
160 170 180 190 200
WPEDAAPLIT WGLTVTRGPH KERQNLGIYR QQLIGKNKLI MRWLSHRGGA
210 220 230 240 250
LDYQEWCAAH PGERFPVSVA LGADPATILG AVTPVPDTLS EYAFAGLLRG
260 270 280 290 300
TKTEVVKCIS NDLEVPASAE IVLEGYIEQG ETAPEGPYGD HTGYYNEVDS
310 320 330 340 350
FPVFTVTHIT QREDAIYHST YTGRPPDEPA VLGVALNEVF VPILQKQFPE
360 370 380 390 400
IVDFYLPPEG CSYRLAVVTI KKQYAGHAKR VMMGVWSFLR QFMYTKFVIV
410 420 430 440 450
CDDDVNARDW NDVIWAITTR MDPARDTVLV ENTPIDYLDF ASPVSGLGSK
460 470 480 490
MGLDATNKWP GETQREWGRP IKKDPDVVAH IDAIWDELAI FNNGKSA
Length:497
Mass (Da):55,604
Last modified:September 13, 2005 - v1
Checksum:i5432A3BEBE81ECC5
GO

Sequence cautioni

The sequence AAA67639.1 differs from that shown. Reason: Frameshift at position 380. Curated
The sequence CAA46146.1 differs from that shown. Reason: Frameshift at position 376. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti452 – 4521G → R in AN66; inactive protein. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiD65189.
S20905.
S30734.
RefSeqiNP_418285.1. NC_000913.3.
YP_491601.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76846; AAC76846; b3843.
BAE77460; BAE77460; BAE77460.
GeneIDi12932472.
948326.
KEGGiecj:Y75_p3337.
eco:b3843.
PATRICi32123183. VBIEscCol129921_3957.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi D65189.
S20905.
S30734.
RefSeqi NP_418285.1. NC_000913.3.
YP_491601.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2IDB X-ray 2.90 A/B/C 1-497 [» ]
ProteinModelPortali P0AAB4.
SMRi P0AAB4. Positions 6-491.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48249N.
IntActi P0AAB4. 4 interactions.
STRINGi 511145.b3843.

Proteomic databases

PaxDbi P0AAB4.
PRIDEi P0AAB4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76846 ; AAC76846 ; b3843 .
BAE77460 ; BAE77460 ; BAE77460 .
GeneIDi 12932472.
948326.
KEGGi ecj:Y75_p3337.
eco:b3843.
PATRICi 32123183. VBIEscCol129921_3957.

Organism-specific databases

EchoBASEi EB1369.
EcoGenei EG11396. ubiD.

Phylogenomic databases

eggNOGi COG0043.
InParanoidi P0AAB4.
KOi K03182.
OMAi SKMGMDA.
OrthoDBi EOG6QZMM7.
PhylomeDBi P0AAB4.

Enzyme and pathway databases

UniPathwayi UPA00232 .
BioCyci EcoCyc:EG11396-MONOMER.
ECOL316407:JW3819-MONOMER.
MetaCyc:EG11396-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AAB4.
PROi P0AAB4.

Gene expression databases

Genevestigatori P0AAB4.

Family and domain databases

HAMAPi MF_01636. UbiD.
InterProi IPR023677. OPHB_Carboxy-lyase.
IPR012349. Split_barrel_FMN-bd.
IPR002830. UbiD.
[Graphical view ]
Pfami PF01977. UbiD. 1 hit.
[Graphical view ]
SUPFAMi SSF50475. SSF50475. 1 hit.
TIGRFAMsi TIGR00148. TIGR00148. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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: FUNCTION, COFACTOR, ENZYME REGULATION, PATHWAY, SUBUNIT, SUBCELLULAR LOCATION.
    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.

Entry informationi

Entry nameiUBID_ECOLI
AccessioniPrimary (citable) accession number: P0AAB4
Secondary accession number(s): P26615
, P27861, P76767, Q2M8E6, Q47265, Q47714
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: November 26, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3