3-octaprenyl-4-hydroxybenzoate carboxy-lyase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P0AAB4 (UBID_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 76. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	497 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Ubiquinone biosynthesis
Cellular component	Cell membrane Membrane
Ligand	Manganese
Molecular function	Decarboxylase Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ubiquinone biosynthetic process Inferred from mutant phenotype PubMed 4897112. Source: EcoCyc
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity Inferred from direct assay Ref.5. Source: EcoCyc FMN binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 497

497

3-octaprenyl-4-hydroxybenzoate carboxy-lyase HAMAP-Rule MF_01636

PRO_0000157357

Natural variations

Natural variant

452

G → R in AN66; inactive protein. Ref.6

Secondary structure

497

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AAB4 [UniParc].

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

FASTA

497

55,604

        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' referencesShow '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 277:1453-1474(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.

PIR

D65189.
S20905.
S30734.

RefSeq

NP_418285.1. NC_000913.2.
YP_491601.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IDB	X-ray	2.90	A/B/C	1-497	[»]

ProteinModelPortal

P0AAB4.

SMR

P0AAB4. Positions 6-491.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48249N.

IntAct

P0AAB4. 3 interactions.

STRING

511145.b3843.

Proteomic databases

PaxDb

P0AAB4.

PRIDE

P0AAB4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76846; AAC76846; b3843.
BAE77460; BAE77460; BAE77460.

GeneID

12932472.
948326.

KEGG

ecj:Y75_p3337.
eco:b3843.

PATRIC

32123183. VBIEscCol129921_3957.

Organism-specific databases

EchoBASE

EB1369.

EcoGene

EG11396. ubiD.

Phylogenomic databases

eggNOG

COG0043.

K03182.

OMA

MGIDATN.

ProtClustDB

PRK10922.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11396-MONOMER.
ECOL316407:JW3819-MONOMER.
MetaCyc:EG11396-MONOMER.

UniPathway

UPA00232.

Gene expression databases

Genevestigator

P0AAB4.

Family and domain databases

HAMAP

MF_01636. UbiD.

InterPro

IPR023677. OPHB_Carboxy-lyase.
IPR012349. Split_barrel_FMN-bd.
IPR002830. UbiD.
[Graphical view]

Pfam

PF01977. UbiD. 1 hit.
[Graphical view]

SUPFAM

SSF50475. FMN_binding. 1 hit.

TIGRFAMs

TIGR00148. TIGR00148. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0AAB4.

Entry information

Entry name

UBID_ECOLI

Accession

Primary (citable) accession number: P0AAB4
Secondary accession number(s): P26615

Q47714

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	September 13, 2005
Last modified:	May 29, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents