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Protein

Light-independent protochlorophyllide reductase subunit N

Gene

chlN

Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Status
Reviewed-Annotation score: 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 NB-protein (ChlN-ChlB) is the catalytic component of the complex.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 heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi17 – 171Iron-sulfur (4Fe-4S); shared with heterodimeric partnerUniRule annotation
Metal bindingi42 – 421Iron-sulfur (4Fe-4S); shared with heterodimeric partnerUniRule annotation
Metal bindingi103 – 1031Iron-sulfur (4Fe-4S); shared with heterodimeric partnerUniRule 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, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciPMAR167539:GJN2-564-MONOMER.
UniPathwayiUPA00670.

Names & Taxonomyi

Protein namesi
Recommended name:
Light-independent protochlorophyllide reductase subunit NUniRule annotation (EC:1.3.7.7UniRule annotation)
Short name:
DPOR subunit NUniRule annotation
Short name:
LI-POR subunit NUniRule annotation
Gene namesi
Name:chlNUniRule annotation
Ordered Locus Names:Pro_0546
OrganismiProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
Taxonomic identifieri167539 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001420 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Light-independent protochlorophyllide reductase subunit NPRO_0000324008Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi167539.Pro0546.

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi18 – 214Combined sources
Helixi22 – 287Combined sources
Beta strandi32 – 387Combined sources
Helixi40 – 5011Combined sources
Beta strandi60 – 645Combined sources
Helixi67 – 704Combined sources
Helixi76 – 9015Combined sources
Beta strandi95 – 1017Combined sources
Helixi103 – 1075Combined sources
Helixi112 – 12312Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1336Combined sources
Turni136 – 1383Combined sources
Helixi143 – 15210Combined sources
Helixi153 – 1553Combined sources
Beta strandi163 – 1686Combined sources
Helixi172 – 18413Combined sources
Beta strandi190 – 1945Combined sources
Beta strandi208 – 2147Combined sources
Helixi218 – 2269Combined sources
Helixi239 – 25315Combined sources
Helixi258 – 28326Combined sources
Beta strandi287 – 2904Combined sources
Beta strandi292 – 2954Combined sources
Helixi297 – 30610Combined sources
Beta strandi311 – 3188Combined sources
Turni322 – 3243Combined sources
Helixi326 – 3316Combined sources
Beta strandi337 – 3415Combined sources
Helixi344 – 35411Combined sources
Beta strandi357 – 3615Combined sources
Turni363 – 3653Combined sources
Helixi366 – 3716Combined sources
Beta strandi376 – 3783Combined sources
Helixi379 – 3846Combined sources
Helixi390 – 3923Combined sources
Helixi393 – 41018Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YNMX-ray2.10C1-418[»]
ProteinModelPortaliQ7VD37.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the BchN/ChlN family.UniRule annotation

Phylogenomic databases

eggNOGiCOG2710.
KOiK04038.
OMAiIFAEPRF.
OrthoDBiEOG6PZX7T.

Family and domain databases

HAMAPiMF_00352. ChlN_BchN.
InterProiIPR000510. Nase/OxRdtase_comp1.
IPR005970. Protochl_reductN.
[Graphical view]
PfamiPF00148. Oxidored_nitro. 1 hit.
[Graphical view]
PIRSFiPIRSF000162. P_chlorophyll_rd. 1 hit.
TIGRFAMsiTIGR01279. DPOR_bchN. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7VD37-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGSTLLKET GPREVFCGLT SIVWLHRRMP DAFFLVVGSR TCAHLIQSAA
60 70 80 90 100
GVMIFAEPRF GTAILEERDL AGLADAHEEL DRVVKSLLKR RPEIRTLFLV
110 120 130 140 150
GSCPSEVIKI DLSRAAERLS SQFNGQVRIL NYSGSGIETT FTQGEDGALK
160 170 180 190 200
ALVPLMPSSQ EEQLLLAGTL ANPVEDRLKT IFNRLGIQKV ESFPPRESTK
210 220 230 240 250
LPAIGPGTKV LLAQPYLTDT ARELKDRGAE ILQAPFPLGV EGSQLWIEAA
260 270 280 290 300
ANAFKIKKTL VDATLEPLIT RAHKALKPYV EQLSGKKLFL LPESQLEIPL
310 320 330 340 350
ARFLSNECGM KLIEVGVPYL NREMMGPELD LLPQNTRIVE GQHVEKQLDR
360 370 380 390 400
VREHHPDLVV CGMGLANPLE AEGISTKWSI EMVFSPIHGI DQASDLAELF
410
ARPLHRQNLL NKKTLEAV
Length:418
Mass (Da):46,199
Last modified:October 1, 2003 - v1
Checksum:i02458DD9AD581EE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAP99591.1.
RefSeqiNP_874939.1. NC_005042.1.

Genome annotation databases

EnsemblBacteriaiAAP99591; AAP99591; Pro_0546.
GeneIDi1461928.
KEGGipma:Pro_0546.
PATRICi23027725. VBIProMar8617_0561.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAP99591.1.
RefSeqiNP_874939.1. NC_005042.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YNMX-ray2.10C1-418[»]
ProteinModelPortaliQ7VD37.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi167539.Pro0546.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP99591; AAP99591; Pro_0546.
GeneIDi1461928.
KEGGipma:Pro_0546.
PATRICi23027725. VBIProMar8617_0561.

Phylogenomic databases

eggNOGiCOG2710.
KOiK04038.
OMAiIFAEPRF.
OrthoDBiEOG6PZX7T.

Enzyme and pathway databases

UniPathwayiUPA00670.
BioCyciPMAR167539:GJN2-564-MONOMER.

Family and domain databases

HAMAPiMF_00352. ChlN_BchN.
InterProiIPR000510. Nase/OxRdtase_comp1.
IPR005970. Protochl_reductN.
[Graphical view]
PfamiPF00148. Oxidored_nitro. 1 hit.
[Graphical view]
PIRSFiPIRSF000162. P_chlorophyll_rd. 1 hit.
TIGRFAMsiTIGR01279. DPOR_bchN. 1 hit.
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiCHLN_PROMA
AccessioniPrimary (citable) accession number: Q7VD37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 1, 2003
Last modified: January 7, 2015
This is version 64 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.