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Protein

Light-independent protochlorophyllide reductase subunit N

Gene

chlN

Organism
Thermosynechococcus elongatus (strain BP-1)
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: chlorophyll biosynthesis (light-independent)

This protein is involved in the pathway chlorophyll biosynthesis (light-independent), which is part of Porphyrin-containing compound metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway chlorophyll biosynthesis (light-independent) and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi22Iron-sulfur (4Fe-4S); shared with heterodimeric partnerUniRule annotation1
Metal bindingi47Iron-sulfur (4Fe-4S); shared with heterodimeric partnerUniRule annotation1
Metal bindingi107Iron-sulfur (4Fe-4S); shared with heterodimeric partnerUniRule annotation1

GO - Molecular functioni

GO - Biological processi

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

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:tll2345
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeThermosynechococcus
Proteomesi
  • UP000000440 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002086021 – 460Light-independent protochlorophyllide reductase subunit NAdd BLAST460

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

STRINGi197221.tll2345.

Structurei

Secondary structure

1460
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 13Combined sources4
Helixi23 – 25Combined sources3
Helixi26 – 33Combined sources8
Beta strandi37 – 43Combined sources7
Helixi45 – 54Combined sources10
Helixi56 – 60Combined sources5
Beta strandi64 – 69Combined sources6
Helixi72 – 75Combined sources4
Helixi81 – 96Combined sources16
Beta strandi99 – 105Combined sources7
Helixi107 – 111Combined sources5
Helixi116 – 127Combined sources12
Beta strandi131 – 135Combined sources5
Turni138 – 140Combined sources3
Helixi145 – 155Combined sources11
Beta strandi199 – 203Combined sources5
Helixi207 – 217Combined sources11
Helixi218 – 220Combined sources3
Beta strandi224 – 229Combined sources6
Helixi233 – 235Combined sources3
Beta strandi244 – 249Combined sources6
Helixi253 – 261Combined sources9
Beta strandi266 – 268Combined sources3
Helixi275 – 289Combined sources15
Helixi298 – 306Combined sources9
Helixi309 – 315Combined sources7
Beta strandi319 – 322Combined sources4
Helixi329 – 338Combined sources10
Beta strandi342 – 349Combined sources8
Helixi353 – 369Combined sources17
Beta strandi376 – 380Combined sources5
Helixi383 – 393Combined sources11
Beta strandi396 – 400Combined sources5
Helixi402 – 409Combined sources8
Beta strandi415 – 417Combined sources3
Helixi420 – 423Combined sources4
Helixi429 – 431Combined sources3
Helixi432 – 448Combined sources17
Beta strandi451 – 453Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XDQX-ray2.40A1-460[»]
ProteinModelPortaliQ8DGH2.
SMRiQ8DGH2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8DGH2.

Family & Domainsi

Sequence similaritiesi

Belongs to the BchN/ChlN family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C78. Bacteria.
COG2710. LUCA.
HOGENOMiHOG000265994.
KOiK04038.
OMAiREVFCGL.
OrthoDBiPOG091H14P2.

Family and domain databases

HAMAPiMF_00352. ChlN_BchN. 1 hit.
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.

Q8DGH2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVTAPNALN FECETGNYHT FCPISCVAWL YQKIEDSFFL VIGTKTCGYF
60 70 80 90 100
LQNAMGVMIF AEPRYAMAEL EEGDISAQLN DYEELKRLCL EIKRDRNPSV
110 120 130 140 150
IVWIGTCTTE IIKMDLEGLA PKLEAEIGIP IVVARANGLD YAFTQGEDTV
160 170 180 190 200
LAAMAARCPT STAISDPEER NPIQRLLNFG KKKEEVQAQS SQYHPHPPLV
210 220 230 240 250
LFGSLPDPVV TQLTLELKKQ GIKVSGWLPA KRYTELPVID EGYYVAGVNP
260 270 280 290 300
FLSRTATTLI RRRKCQLITA PFPIGPDGTR TWIEQICATF GIQPQGLAER
310 320 330 340 350
EAETWQKLSD YLELVRGKSV FFMGDNLLEI SLARFLIRCG MRVLEIGIPY
360 370 380 390 400
MDKRYQAAEL ALLSQTCAEM GHPLPTIVEK PDNYNQLQRI KALQPDLVIT
410 420 430 440 450
GMAHANPLEA RGISTKWSVE FTFAQIHGFG NARDILELVT RPLRRNQALA
460
GLGWQKLVAH
Length:460
Mass (Da):51,509
Last modified:March 1, 2003 - v1
Checksum:i9D3ED2EAF8ED4774
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC09897.1.
RefSeqiNP_683135.1. NC_004113.1.
WP_011058178.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC09897; BAC09897; BAC09897.
GeneIDi1011794.
KEGGitel:tll2345.
PATRICi23930158. VBITheElo119873_2458.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC09897.1.
RefSeqiNP_683135.1. NC_004113.1.
WP_011058178.1. NC_004113.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XDQX-ray2.40A1-460[»]
ProteinModelPortaliQ8DGH2.
SMRiQ8DGH2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi197221.tll2345.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC09897; BAC09897; BAC09897.
GeneIDi1011794.
KEGGitel:tll2345.
PATRICi23930158. VBITheElo119873_2458.

Phylogenomic databases

eggNOGiENOG4105C78. Bacteria.
COG2710. LUCA.
HOGENOMiHOG000265994.
KOiK04038.
OMAiREVFCGL.
OrthoDBiPOG091H14P2.

Enzyme and pathway databases

UniPathwayiUPA00670.

Miscellaneous databases

EvolutionaryTraceiQ8DGH2.

Family and domain databases

HAMAPiMF_00352. ChlN_BchN. 1 hit.
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...

Entry informationi

Entry nameiCHLN_THEEB
AccessioniPrimary (citable) accession number: Q8DGH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 78 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

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 one 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.