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Q58MU6

- PEBS_BPPRM

UniProt

Q58MU6 - PEBS_BPPRM

Protein

Phycoerythrobilin synthase

Gene

pebS

Organism
Prochlorococcus phage P-SSM2
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 32 (01 Oct 2014)
      Sequence version 1 (26 Apr 2005)
      Previous versions | rss
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    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

    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 – 3410
    Beta strandi39 – 4911
    Beta strandi59 – 6810
    Beta strandi71 – 8111
    Beta strandi84 – 9310
    Beta strandi95 – 973
    Beta strandi101 – 11010
    Beta strandi113 – 1219
    Beta strandi139 – 1413
    Beta strandi142 – 1443
    Beta strandi148 – 1503
    Beta strandi155 – 1595
    Helixi161 – 1677
    Helixi168 – 18518
    Helixi192 – 1954
    Helixi196 – 2049
    Helixi210 – 2167
    Helixi218 – 22710
    Turni228 – 2325

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MTKNPRNNKP KKILDSSYKS KTIWQNYIDA LFETFPQLEI SEVWAKWDGG    50
    NVTKDGGDAK LTANIRTGEH FLKAREAHIV DPNSDIYNTI LYPKTGADLP 100
    CFGMDLMKFS DKKVIIVFDF QHPREKYLFS VDGLPEDDGK YRFFEMGNHF 150
    SKNIFVRYCK PDEVDQYLDT FKLYLTKYKE MIDNNKPVGE DTTVYSDFDT 200
    YMTELDPVRG YMKNKFGEGR SEAFVNDFLF SYK 233
    Length:233
    Mass (Da):27,256
    Last modified:April 26, 2005 - v1
    Checksum:i4DAABD1CCF307137
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY939844 Genomic DNA. Translation: AAX44436.1 .
    RefSeqi YP_214290.1. NC_006883.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VCK X-ray 1.80 A/B/C/D 1-233 [» ]
    2VCL X-ray 1.55 A 1-233 [» ]
    2VGR X-ray 2.10 A/B/C/D 1-233 [» ]
    2X9I X-ray 2.20 A/B/C/D 1-233 [» ]
    2X9J X-ray 1.85 A/B 1-233 [» ]
    ProteinModelPortali Q58MU6.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3294481.

    Miscellaneous databases

    EvolutionaryTracei Q58MU6.

    Family and domain databases

    InterProi IPR009249. Ferredoxin-dep_bilin_Rdtase.
    [Graphical view ]
    Pfami PF05996. Fe_bilin_red. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 32 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