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Q7VD39 (CHLL_PROMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein

Short name=DPOR subunit L
Short name=LI-POR subunit L
EC=1.3.7.7
Gene names
Name:chlL
Ordered Locus Names:Pro_0544
OrganismProchlorococcus marinus (strain SARG / CCMP1375 / SS120) [Reference proteome] [HAMAP]
Taxonomic identifier167539 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00355

Catalytic activity

Protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate. HAMAP-Rule MF_00355

Cofactor

Binds 1 4Fe-4S cluster per dimer By similarity. HAMAP-Rule MF_00355

Pathway

Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent). HAMAP-Rule MF_00355

Subunit structure

Homodimer. Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB By similarity.

Sequence similarities

Belongs to the NifH/BchL/ChlL family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 296296Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein HAMAP-Rule MF_00355
PRO_0000324057

Regions

Nucleotide binding39 – 446ATP By similarity
Nucleotide binding209 – 2102ATP By similarity

Sites

Metal binding431Magnesium By similarity
Metal binding1241Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity
Metal binding1581Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity
Binding site681ATP By similarity

Secondary structure

................................................ 296
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7VD39 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: D46A27CE10432012

FASTA29632,395
        10         20         30         40         50         60 
MTTTLANRPD GEGSVQVKLD PKVNIEEGAL VIAVYGKGGI GKSTTSSNLS AAFSKLGKKV 

        70         80         90        100        110        120 
LQIGCDPKHD STFTLTHKMV PTVIDILEEV DFHSEELRPQ DFMFEGFNGV QCVESGGPPA 

       130        140        150        160        170        180 
GTGCGGYVTG QTVKLLKEHH LLEDTDVVIF DVLGDVVCGG FAAPLQHANY CLIVTANDFD 

       190        200        210        220        230        240 
SIFAMNRIVA AINAKAKNYK VRLGGVIANR SAELDQIEKF NEKTGLKTMA HFRNVDAIRR 

       250        260        270        280        290 
SRLKKCTIFE MDPEEEGVLE VQNEYLSLAK KMIDNVEPLE AEPLKDREIF DLLGFD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017126 Genomic DNA. Translation: AAP99589.1.
RefSeqNP_874937.1. NC_005042.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YNMX-ray2.10A/B1-296[»]
ProteinModelPortalQ7VD39.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167539.Pro0544.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP99589; AAP99589; Pro_0544.
GeneID1461926.
KEGGpma:Pro_0544.
PATRIC23027721. VBIProMar8617_0559.

Phylogenomic databases

eggNOGCOG1348.
KOK04037.
OMATSCNISV.
OrthoDBEOG69SK8Q.

Enzyme and pathway databases

BioCycPMAR167539:GJN2-562-MONOMER.
UniPathwayUPA00670.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00355. ChlL_BchL.
InterProIPR000392. Nitogenase_NifH/Reductase_ChlL.
IPR027417. P-loop_NTPase.
IPR005971. Protochlorophyllide_ATP-bd.
[Graphical view]
PfamPF00142. Fer4_NifH. 1 hit.
[Graphical view]
PIRSFPIRSF000363. Nitrogenase_iron. 1 hit.
PRINTSPR00091. NITROGNASEII.
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01281. DPOR_bchL. 1 hit.
PROSITEPS00746. NIFH_FRXC_1. 1 hit.
PS00692. NIFH_FRXC_2. 1 hit.
PS51026. NIFH_FRXC_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHLL_PROMA
AccessionPrimary (citable) accession number: Q7VD39
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways