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Q7VD39

- CHLL_PROMA

UniProt

Q7VD39 - CHLL_PROMA

Protein

Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein

Gene

chlL

Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.UniRule annotation

    Catalytic activityi

    Protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate.UniRule annotation

    Cofactori

    Binds 1 4Fe-4S cluster per dimer.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi43 – 431MagnesiumUniRule annotation
    Binding sitei68 – 681ATPUniRule annotation
    Metal bindingi124 – 1241Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation
    Metal bindingi158 – 1581Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi39 – 446ATPUniRule annotation
    Nucleotide bindingi209 – 2102ATPUniRule annotation

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
    2. ATP binding Source: UniProtKB-HAMAP
    3. metal ion binding Source: UniProtKB-KW
    4. oxidoreductase activity, acting on iron-sulfur proteins as donors Source: InterPro
    5. oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor Source: UniProtKB-HAMAP

    GO - Biological processi

    1. light-independent chlorophyll biosynthetic process Source: UniProtKB-UniPathway
    2. photosynthesis, dark reaction Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Chlorophyll biosynthesis, Photosynthesis

    Keywords - Ligandi

    4Fe-4S, ATP-binding, Iron, Iron-sulfur, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciPMAR167539:GJN2-562-MONOMER.
    UniPathwayiUPA00670.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Light-independent protochlorophyllide reductase iron-sulfur ATP-binding proteinUniRule annotation (EC:1.3.7.7UniRule annotation)
    Short name:
    DPOR subunit LUniRule annotation
    Short name:
    LI-POR subunit LUniRule annotation
    Gene namesi
    Name:chlLUniRule annotation
    Ordered Locus Names:Pro_0544
    OrganismiProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
    Taxonomic identifieri167539 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000001420: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 296296Light-independent protochlorophyllide reductase iron-sulfur ATP-binding proteinPRO_0000324057Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer. Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB.UniRule annotation

    Protein-protein interaction databases

    STRINGi167539.Pro0544.

    Structurei

    Secondary structure

    1
    296
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 378
    Helixi42 – 5514
    Beta strandi60 – 667
    Helixi73 – 764
    Helixi83 – 897
    Turni90 – 923
    Helixi94 – 963
    Helixi99 – 1024
    Helixi107 – 1093
    Beta strandi111 – 1144
    Beta strandi122 – 1243
    Helixi125 – 13814
    Turni139 – 1435
    Beta strandi144 – 1529
    Helixi159 – 1613
    Helixi163 – 1664
    Beta strandi169 – 1757
    Helixi179 – 19517
    Turni196 – 1983
    Beta strandi202 – 2109
    Helixi215 – 22410
    Beta strandi228 – 2325
    Helixi236 – 2438
    Helixi248 – 2503
    Helixi258 – 27417
    Helixi286 – 2927

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YNMX-ray2.10A/B1-296[»]
    ProteinModelPortaliQ7VD39.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the NifH/BchL/ChlL family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1348.
    KOiK04037.
    OMAiTSCNISV.
    OrthoDBiEOG69SK8Q.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00355. ChlL_BchL.
    InterProiIPR000392. Nitogenase_NifH/Reductase_ChlL.
    IPR027417. P-loop_NTPase.
    IPR005971. Protochlorophyllide_ATP-bd.
    [Graphical view]
    PfamiPF00142. Fer4_NifH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000363. Nitrogenase_iron. 1 hit.
    PRINTSiPR00091. NITROGNASEII.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR01281. DPOR_bchL. 1 hit.
    PROSITEiPS00746. NIFH_FRXC_1. 1 hit.
    PS00692. NIFH_FRXC_2. 1 hit.
    PS51026. NIFH_FRXC_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7VD39-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTTLANRPD GEGSVQVKLD PKVNIEEGAL VIAVYGKGGI GKSTTSSNLS    50
    AAFSKLGKKV LQIGCDPKHD STFTLTHKMV PTVIDILEEV DFHSEELRPQ 100
    DFMFEGFNGV QCVESGGPPA GTGCGGYVTG QTVKLLKEHH LLEDTDVVIF 150
    DVLGDVVCGG FAAPLQHANY CLIVTANDFD SIFAMNRIVA AINAKAKNYK 200
    VRLGGVIANR SAELDQIEKF NEKTGLKTMA HFRNVDAIRR SRLKKCTIFE 250
    MDPEEEGVLE VQNEYLSLAK KMIDNVEPLE AEPLKDREIF DLLGFD 296
    Length:296
    Mass (Da):32,395
    Last modified:October 1, 2003 - v1
    Checksum:iD46A27CE10432012
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017126 Genomic DNA. Translation: AAP99589.1.
    RefSeqiNP_874937.1. NC_005042.1.

    Genome annotation databases

    EnsemblBacteriaiAAP99589; AAP99589; Pro_0544.
    GeneIDi1461926.
    KEGGipma:Pro_0544.
    PATRICi23027721. VBIProMar8617_0559.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017126 Genomic DNA. Translation: AAP99589.1 .
    RefSeqi NP_874937.1. NC_005042.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YNM X-ray 2.10 A/B 1-296 [» ]
    ProteinModelPortali Q7VD39.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 167539.Pro0544.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAP99589 ; AAP99589 ; Pro_0544 .
    GeneIDi 1461926.
    KEGGi pma:Pro_0544.
    PATRICi 23027721. VBIProMar8617_0559.

    Phylogenomic databases

    eggNOGi COG1348.
    KOi K04037.
    OMAi TSCNISV.
    OrthoDBi EOG69SK8Q.

    Enzyme and pathway databases

    UniPathwayi UPA00670 .
    BioCyci PMAR167539:GJN2-562-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_00355. ChlL_BchL.
    InterProi IPR000392. Nitogenase_NifH/Reductase_ChlL.
    IPR027417. P-loop_NTPase.
    IPR005971. Protochlorophyllide_ATP-bd.
    [Graphical view ]
    Pfami PF00142. Fer4_NifH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000363. Nitrogenase_iron. 1 hit.
    PRINTSi PR00091. NITROGNASEII.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR01281. DPOR_bchL. 1 hit.
    PROSITEi PS00746. NIFH_FRXC_1. 1 hit.
    PS00692. NIFH_FRXC_2. 1 hit.
    PS51026. NIFH_FRXC_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SARG / CCMP1375 / SS120.

    Entry informationi

    Entry nameiCHLL_PROMA
    AccessioniPrimary (citable) accession number: Q7VD39
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 79 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

    External Data

    Dasty 3