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Protein

1,4-dihydroxy-2-naphthoyl-CoA hydrolase

Gene

PMT_2055

Organism
Prochlorococcus marinus (strain MIT 9313)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA), a reaction involved in phylloquinone (vitamin K1) biosynthesis.UniRule annotation

Catalytic activityi

1,4-dihydroxy-2-naphthoyl-CoA + H2O = 1,4-dihydroxy-2-naphthoate + CoA.UniRule annotation

Pathwayi: phylloquinone biosynthesis

This protein is involved in the pathway phylloquinone biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway phylloquinone biosynthesis and in Cofactor biosynthesis.

Pathwayi: 1,4-dihydroxy-2-naphthoate biosynthesis

This protein is involved in step 7 of the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate.UniRule annotation
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (menD)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. 1,4-dihydroxy-2-naphthoyl-CoA synthase (menB)
  7. 1,4-dihydroxy-2-naphthoyl-CoA hydrolase (PMT_2055)
This subpathway is part of the pathway 1,4-dihydroxy-2-naphthoate biosynthesis, which is itself part of Quinol/quinone metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate, the pathway 1,4-dihydroxy-2-naphthoate biosynthesis and in Quinol/quinone metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei19 – 191UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

UniPathwayiUPA00995.
UPA01057; UER01033.

Names & Taxonomyi

Protein namesi
Recommended name:
1,4-dihydroxy-2-naphthoyl-CoA hydrolaseUniRule annotation (EC:3.1.2.28UniRule annotation)
Short name:
DHNA-CoA hydrolaseUniRule annotation
Alternative name(s):
DHNA-CoA thioesteraseUniRule annotation
Gene namesi
Ordered Locus Names:PMT_2055
OrganismiProchlorococcus marinus (strain MIT 9313)
Taxonomic identifieri74547 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
Proteomesi
  • UP000001423 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1511511,4-dihydroxy-2-naphthoyl-CoA hydrolasePRO_0000377022Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi74547.PMT2055.

Structurei

Secondary structure

1
151
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 74Combined sources
Beta strandi8 – 125Combined sources
Helixi15 – 173Combined sources
Beta strandi22 – 243Combined sources
Helixi28 – 4417Combined sources
Helixi48 – 514Combined sources
Beta strandi63 – 653Combined sources
Beta strandi68 – 758Combined sources
Beta strandi84 – 9512Combined sources
Beta strandi98 – 10710Combined sources
Beta strandi110 – 12011Combined sources
Turni124 – 1263Combined sources
Helixi134 – 1429Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HX5X-ray1.50A1-151[»]
ProteinModelPortaliQ7V4A7.
SMRiQ7V4A7. Positions 1-144.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7V4A7.

Family & Domainsi

Sequence similaritiesi

Belongs to the 4-hydroxybenzoyl-CoA thioesterase family. DHNA-CoA hydrolase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105WGP. Bacteria.
COG0824. LUCA.
OMAiHEAWEES.
OrthoDBiEOG6KWXZW.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
HAMAPiMF_02101. DHNA_CoA_hydrolase.
InterProiIPR022829. DHNA_CoA_hydrolase.
IPR029069. HotDog_dom.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7V4A7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPENWLLLR RVVRFGDTDA AGVMHFHQLF RWCHESWEES LESYGLNPAD
60 70 80 90 100
IFPGSRKSEV TPEVALPIIH CQADFRRPIH TGDALAMELR PERLNPNSFQ
110 120 130 140 150
VHFEFRCEEQ IAAHALIRHL AINAQTRHRC ALPEGIDRWL EASGVGKIGS

I
Length:151
Mass (Da):17,304
Last modified:October 1, 2003 - v1
Checksum:iEA9F48E141EBB974
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX548175 Genomic DNA. Translation: CAE22229.1.
RefSeqiWP_011131420.1. NC_005071.1.

Genome annotation databases

EnsemblBacteriaiCAE22229; CAE22229; PMT_2055.
PATRICi23012961. VBIProMar135351_2603.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX548175 Genomic DNA. Translation: CAE22229.1.
RefSeqiWP_011131420.1. NC_005071.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HX5X-ray1.50A1-151[»]
ProteinModelPortaliQ7V4A7.
SMRiQ7V4A7. Positions 1-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi74547.PMT2055.

Protocols and materials databases

DNASUi1729478.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE22229; CAE22229; PMT_2055.
PATRICi23012961. VBIProMar135351_2603.

Phylogenomic databases

eggNOGiENOG4105WGP. Bacteria.
COG0824. LUCA.
OMAiHEAWEES.
OrthoDBiEOG6KWXZW.

Enzyme and pathway databases

UniPathwayiUPA00995.
UPA01057; UER01033.

Miscellaneous databases

EvolutionaryTraceiQ7V4A7.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
HAMAPiMF_02101. DHNA_CoA_hydrolase.
InterProiIPR022829. DHNA_CoA_hydrolase.
IPR029069. HotDog_dom.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MIT 9313.

Entry informationi

Entry nameiDNCH_PROMM
AccessioniPrimary (citable) accession number: Q7V4A7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: October 1, 2003
Last modified: November 11, 2015
This is version 77 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.