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Q7VD39

- CHLL_PROMA

UniProt

Q7VD39 - CHLL_PROMA

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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

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

[4Fe-4S] clusterUniRule annotationNote: 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
Complete GO annotation...

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 – 378Combined sources
Helixi42 – 5514Combined sources
Beta strandi60 – 667Combined sources
Helixi73 – 764Combined sources
Helixi83 – 897Combined sources
Turni90 – 923Combined sources
Helixi94 – 963Combined sources
Helixi99 – 1024Combined sources
Helixi107 – 1093Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi122 – 1243Combined sources
Helixi125 – 13814Combined sources
Turni139 – 1435Combined sources
Beta strandi144 – 1529Combined sources
Helixi159 – 1613Combined sources
Helixi163 – 1664Combined sources
Beta strandi169 – 1757Combined sources
Helixi179 – 19517Combined sources
Turni196 – 1983Combined sources
Beta strandi202 – 2109Combined sources
Helixi215 – 22410Combined sources
Beta strandi228 – 2325Combined sources
Helixi236 – 2438Combined sources
Helixi248 – 2503Combined sources
Helixi258 – 27417Combined sources
Helixi286 – 2927Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MTTTLANRPD GEGSVQVKLD PKVNIEEGAL VIAVYGKGGI GKSTTSSNLS
60 70 80 90 100
AAFSKLGKKV LQIGCDPKHD STFTLTHKMV PTVIDILEEV DFHSEELRPQ
110 120 130 140 150
DFMFEGFNGV QCVESGGPPA GTGCGGYVTG QTVKLLKEHH LLEDTDVVIF
160 170 180 190 200
DVLGDVVCGG FAAPLQHANY CLIVTANDFD SIFAMNRIVA AINAKAKNYK
210 220 230 240 250
VRLGGVIANR SAELDQIEKF NEKTGLKTMA HFRNVDAIRR SRLKKCTIFE
260 270 280 290
MDPEEEGVLE VQNEYLSLAK KMIDNVEPLE AEPLKDREIF DLLGFD
Length:296
Mass (Da):32,395
Last modified:October 1, 2003 - v1
Checksum:iD46A27CE10432012
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAP99589.1 .
RefSeqi NP_874937.1. NC_005042.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 80 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