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Q7VD37 (CHLN_PROMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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 subunit N

Short name=DPOR subunit N
Short name=LI-POR subunit N
EC=1.3.7.7
Gene names
Name:chlN
Ordered Locus Names:Pro_0546
OrganismProchlorococcus marinus (strain SARG / CCMP1375 / SS120) [Reference proteome] [HAMAP]
Taxonomic identifier167539 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length418 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 NB-protein (ChlN-ChlB) is the catalytic component of the complex By similarity. HAMAP-Rule MF_00352

Catalytic activity

Protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate. HAMAP-Rule MF_00352

Cofactor

Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits By similarity.

Pathway

Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent). HAMAP-Rule MF_00352

Subunit structure

Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN subunits By similarity.

Sequence similarities

Belongs to the BchN/ChlN family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418Light-independent protochlorophyllide reductase subunit N HAMAP-Rule MF_00352
PRO_0000324008

Sites

Metal binding171Iron-sulfur (4Fe-4S); shared with heterodimeric partner By similarity
Metal binding421Iron-sulfur (4Fe-4S); shared with heterodimeric partner By similarity
Metal binding1031Iron-sulfur (4Fe-4S); shared with heterodimeric partner By similarity

Secondary structure

....................................................................... 418
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7VD37 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 02458DD9AD581EE5

FASTA41846,199
        10         20         30         40         50         60 
MSGSTLLKET GPREVFCGLT SIVWLHRRMP DAFFLVVGSR TCAHLIQSAA GVMIFAEPRF 

        70         80         90        100        110        120 
GTAILEERDL AGLADAHEEL DRVVKSLLKR RPEIRTLFLV GSCPSEVIKI DLSRAAERLS 

       130        140        150        160        170        180 
SQFNGQVRIL NYSGSGIETT FTQGEDGALK ALVPLMPSSQ EEQLLLAGTL ANPVEDRLKT 

       190        200        210        220        230        240 
IFNRLGIQKV ESFPPRESTK LPAIGPGTKV LLAQPYLTDT ARELKDRGAE ILQAPFPLGV 

       250        260        270        280        290        300 
EGSQLWIEAA ANAFKIKKTL VDATLEPLIT RAHKALKPYV EQLSGKKLFL LPESQLEIPL 

       310        320        330        340        350        360 
ARFLSNECGM KLIEVGVPYL NREMMGPELD LLPQNTRIVE GQHVEKQLDR VREHHPDLVV 

       370        380        390        400        410 
CGMGLANPLE AEGISTKWSI EMVFSPIHGI DQASDLAELF ARPLHRQNLL NKKTLEAV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017126 Genomic DNA. Translation: AAP99591.1.
RefSeqNP_874939.1. NC_005042.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YNMX-ray2.10C1-418[»]
ProteinModelPortalQ7VD37.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167539.Pro0546.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP99591; AAP99591; Pro_0546.
GeneID1461928.
KEGGpma:Pro_0546.
PATRIC23027725. VBIProMar8617_0561.

Phylogenomic databases

eggNOGCOG2710.
KOK04038.
OMAIFAEPRF.
OrthoDBEOG6PZX7T.
ProtClustDBPRK02842.

Enzyme and pathway databases

BioCycPMAR167539:GJN2-564-MONOMER.
UniPathwayUPA00670.

Family and domain databases

HAMAPMF_00352. ChlN_BchN.
InterProIPR000510. Nase/OxRdtase_comp1.
IPR005970. Protochl_reductN.
[Graphical view]
PfamPF00148. Oxidored_nitro. 1 hit.
[Graphical view]
PIRSFPIRSF000162. P_chlorophyll_rd. 1 hit.
TIGRFAMsTIGR01279. DPOR_bchN. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCHLN_PROMA
AccessionPrimary (citable) accession number: Q7VD37
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 59 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