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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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

BRENDAi1.3.7.6. 10990.

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]
Proteomesi
  • UP000000991 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003540641 – 233Phycoerythrobilin synthaseAdd BLAST233

Structurei

Secondary structure

1233
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi25 – 34Combined sources10
Beta strandi39 – 49Combined sources11
Beta strandi59 – 68Combined sources10
Beta strandi71 – 81Combined sources11
Beta strandi84 – 93Combined sources10
Beta strandi95 – 97Combined sources3
Beta strandi101 – 110Combined sources10
Beta strandi113 – 121Combined sources9
Beta strandi139 – 141Combined sources3
Beta strandi142 – 144Combined sources3
Beta strandi148 – 150Combined sources3
Beta strandi155 – 159Combined sources5
Helixi161 – 167Combined sources7
Helixi168 – 185Combined sources18
Helixi192 – 195Combined sources4
Helixi196 – 204Combined sources9
Helixi210 – 216Combined sources7
Helixi218 – 227Combined sources10
Turni228 – 232Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiQ58MU6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ58MU6.

Family & Domainsi

Sequence similaritiesi

Belongs to the HY2 family.Curated

Phylogenomic databases

KOiK05369.

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.
KEGGiag:AAX44436.
vg:3294481.

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
PDB 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.
SMRiQ58MU6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3294481.
KEGGiag:AAX44436.
vg:3294481.

Phylogenomic databases

KOiK05369.

Enzyme and pathway databases

BRENDAi1.3.7.6. 10990.

Miscellaneous databases

EvolutionaryTraceiQ58MU6.

Family and domain databases

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

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: November 30, 2016
This is version 41 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.