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Protein

Phycoerythrobilin synthase

Gene

pebS

Organism
Prochlorococcus phage P-SSM2
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in phycoerythrobilin biosynthesis, the red pigment chromophore photosynthetically active biliproteins of the host cyanobacteria. Uses a four-electron reduction to carry out the reactions catalyzed by two enzymes (EC 1.3.7.2 and EC 1.3.7.3) in host.

Catalytic activityi

(3Z)-phycoerythrobilin + 2 oxidized ferredoxin = biliverdin IX-alpha + 2 reduced ferredoxin.1 Publication

GO - Molecular functioni

  1. cobalt ion binding Source: InterPro
  2. oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor Source: InterPro

GO - Biological processi

  1. phytochromobilin biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Names & Taxonomyi

Protein namesi
Recommended name:
Phycoerythrobilin synthase (EC:1.3.7.6)
Alternative name(s):
(3Z)-phycoerythrobilin:ferredoxin oxidoreductase
Gene namesi
Name:pebS
ORF Names:PSSM2_058
OrganismiProchlorococcus phage P-SSM2
Taxonomic identifieri268746 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostiProchlorococcus [TaxID: 1218]
ProteomesiUP000000991: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 233233Phycoerythrobilin synthasePRO_0000354064Add
BLAST

Structurei

Secondary structure

1
233
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 3410Combined sources
Beta strandi39 – 4911Combined sources
Beta strandi59 – 6810Combined sources
Beta strandi71 – 8111Combined sources
Beta strandi84 – 9310Combined sources
Beta strandi95 – 973Combined sources
Beta strandi101 – 11010Combined sources
Beta strandi113 – 1219Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi155 – 1595Combined sources
Helixi161 – 1677Combined sources
Helixi168 – 18518Combined sources
Helixi192 – 1954Combined sources
Helixi196 – 2049Combined sources
Helixi210 – 2167Combined sources
Helixi218 – 22710Combined sources
Turni228 – 2325Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VCKX-ray1.80A/B/C/D1-233[»]
2VCLX-ray1.55A1-233[»]
2VGRX-ray2.10A/B/C/D1-233[»]
2X9IX-ray2.20A/B/C/D1-233[»]
2X9JX-ray1.85A/B1-233[»]
ProteinModelPortaliQ58MU6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ58MU6.

Family & Domainsi

Sequence similaritiesi

Belongs to the HY2 family.Curated

Family and domain databases

InterProiIPR009249. Ferredoxin-dep_bilin_Rdtase.
[Graphical view]
PfamiPF05996. Fe_bilin_red. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q58MU6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKNPRNNKP KKILDSSYKS KTIWQNYIDA LFETFPQLEI SEVWAKWDGG
60 70 80 90 100
NVTKDGGDAK LTANIRTGEH FLKAREAHIV DPNSDIYNTI LYPKTGADLP
110 120 130 140 150
CFGMDLMKFS DKKVIIVFDF QHPREKYLFS VDGLPEDDGK YRFFEMGNHF
160 170 180 190 200
SKNIFVRYCK PDEVDQYLDT FKLYLTKYKE MIDNNKPVGE DTTVYSDFDT
210 220 230
YMTELDPVRG YMKNKFGEGR SEAFVNDFLF SYK
Length:233
Mass (Da):27,256
Last modified:April 26, 2005 - v1
Checksum:i4DAABD1CCF307137
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY939844 Genomic DNA. Translation: AAX44436.1.
RefSeqiYP_214290.1. NC_006883.2.

Genome annotation databases

GeneIDi3294481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY939844 Genomic DNA. Translation: AAX44436.1.
RefSeqiYP_214290.1. NC_006883.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VCKX-ray1.80A/B/C/D1-233[»]
2VCLX-ray1.55A1-233[»]
2VGRX-ray2.10A/B/C/D1-233[»]
2X9IX-ray2.20A/B/C/D1-233[»]
2X9JX-ray1.85A/B1-233[»]
ProteinModelPortaliQ58MU6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3294481.

Miscellaneous databases

EvolutionaryTraceiQ58MU6.

Family and domain databases

InterProiIPR009249. Ferredoxin-dep_bilin_Rdtase.
[Graphical view]
PfamiPF05996. Fe_bilin_red. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Three Prochlorococcus cyanophage genomes: signature features and ecological interpretations."
    Sullivan M.B., Coleman M.L., Weigele P., Rohwer F., Chisholm S.W.
    PLoS Biol. 3:E144-E144(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Efficient phage-mediated pigment biosynthesis in oceanic cyanobacteria."
    Dammeyer T., Bagby S.C., Sullivan M.B., Chisholm S.W., Frankenberg-Dinkel N.
    Curr. Biol. 18:442-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, CHARACTERIZATION.

Entry informationi

Entry nameiPEBS_BPPRM
AccessioniPrimary (citable) accession number: Q58MU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: April 26, 2005
Last modified: January 7, 2015
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.