1,4-dihydroxy-2-naphthoate octaprenyltransferase

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P32166 (MENA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. History...

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

Documents (3) |

Third-party data

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

Names and origin

Protein names

Recommended name:
1,4-dihydroxy-2-naphthoate octaprenyltransferase
Short name=DHNA-octaprenyltransferase
EC=2.5.1.74

Gene names

Name:	menA
Synonyms:	yiiW
Ordered Locus Names:	b3930, JW3901

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	308 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to dimethylmenaquinone (DMK). Attaches octaprenylpyrophosphate, a membrane-bound 40-carbon side chain to DHNA. The conversion of DHNA to DMK proceeds in three stages: the removal of the carboxyl group of DHNA as CO₂, the attachment of the isoprenoid side chain, and a quinol-to-quinone oxidation, which is thought to be spontaneous.
Catalytic activity	An all-trans-polyprenyl diphosphate + 1,4-dihydroxy-2-naphthoate = a demethylmenaquinol + diphosphate + CO₂.
Pathway	Cofactor biosynthesis; menaquinone biosynthesis; menaquinone-2 from chorismate: step 7/8.
Subcellular location	Cell inner membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the MenA family.

Ontologies

Keywords
Biological process	Menaquinone biosynthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	menaquinone biosynthetic process Inferred from mutant phenotype PubMed 1091286. Source: EcoCyc
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	1,4-dihydroxy-2-naphthoate octaprenyltransferase activity Inferred from direct assay Ref.1. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 308

308

1,4-dihydroxy-2-naphthoate octaprenyltransferase

PRO_0000096414

Regions

Topological domain

1 – 20

Periplasmic Potential

Transmembrane

21 – 41

Helical; Potential

Topological domain

Cytoplasmic Potential

Transmembrane

43 – 63

Helical; Potential

Topological domain

64 – 97

Periplasmic Potential

Transmembrane

98 – 118

Helical; Potential

Topological domain

119 – 123

Cytoplasmic Potential

Transmembrane

124 – 144

Helical; Potential

Topological domain

145 – 148

Periplasmic Potential

Transmembrane

149 – 169

Helical; Potential

Topological domain

170 – 176

Cytoplasmic Potential

Transmembrane

177 – 197

Helical; Potential

Topological domain

198 – 237

Periplasmic Potential

Transmembrane

238 – 258

Helical; Potential

Topological domain

259 – 286

Cytoplasmic Potential

Transmembrane

287 – 307

Helical; Potential

Topological domain

308

Periplasmic Potential

Sequences

Sequence

Length

Mass (Da)

Tools

P32166 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: FECD9E85BAA40E2E
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FASTA

308

33,594

        10         20         30         40         50         60 
MTEQQISRTQ AWLESLRPKT LPLAFAAIIV GTALAWWQGH FDPLVALLAL ITAGLLQILS 

        70         80         90        100        110        120 
NLANDYGDAV KGSDKPDRIG PLRGMQKGVI TQQEMKRALI ITVVLICLSG LALVAVACHT 

       130        140        150        160        170        180 
LADFVGFLIL GGLSIIAAIT YTVGNRPYGY IGLGDISVLV FFGWLSVMGS WYLQAHTLIP 

       190        200        210        220        230        240 
ALILPATACG LLATAVLNIN NLRDINSDRE NGKNTLVVRL GEVNARRYHA CLLMGSLVCL 

       250        260        270        280        290        300 
ALFNLFSLHS LWGWLFLLAA PLLVKQARYV MREMDPVAMR PMLERTVKGA LLTNLLFVLG 


IFLSQWAA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menA gene from Escherichia coli." Suvarna K., Stevenson D., Meganathan R., Hudspeth M.E.S. J. Bacteriol. 180:2782-2787(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: K12.
[2]	"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Plunkett G. III, Burland V., Daniels D.L., Blattner F.R. Nucleic Acids Res. 21:3391-3398(1993) [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]. 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]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U56082 Genomic DNA. Translation: AAB01207.1. L19201 Genomic DNA. Translation: AAB03062.1. U00096 Genomic DNA. Translation: AAC76912.1. AP009048 Genomic DNA. Translation: BAE77380.1.
PIR	S40873.
RefSeq	NP_418365.1. NC_000913.2. YP_491521.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P32166.
ModBase	Search...
Protein-protein interaction databases
STRING	511145.b3930.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC76912; AAC76912; b3930. BAE77380; BAE77380; BAE77380.
GeneID	12932784. 948418.
KEGG	ecj:Y75_p3257. eco:b3930.
PATRIC	32123375. VBIEscCol129921_4048.
Organism-specific databases
EchoBASE	EB1826.
EcoGene	EG11880. menA.
Phylogenomic databases
eggNOG	COG1575.
HOGENOM	HOG000028297.
KO	K02548.
OMA	ICMAAGY.
ProtClustDB	PRK06080.
Enzyme and pathway databases
BioCyc	EcoCyc:DMK-MONOMER. ECOL316407:JW3901-MONOMER. MetaCyc:DMK-MONOMER.
UniPathway	UPA00079; UER00168.
Gene expression databases
Genevestigator	P32166.
Family and domain databases
InterPro	IPR004657. DHNA_octaprenyltransferase. IPR000537. UbiA_prenyltransferase. IPR026046. UBIAD1. [Graphical view]
Pfam	PF01040. UbiA. 1 hit. [Graphical view]
PIRSF	PIRSF005355. UBIAD1. 1 hit.
TIGRFAMs	TIGR00751. menA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MENA_ECOLI

Accession

Primary (citable) accession number: P32166
Secondary accession number(s): Q2M8M6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 106 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

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

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents