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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: 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 bindingi17Iron-sulfur (4Fe-4S); shared with heterodimeric partnerUniRule annotation1
Metal bindingi42Iron-sulfur (4Fe-4S); shared with heterodimeric partnerUniRule annotation1
Metal bindingi103Iron-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:Pro_0546
OrganismiProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
Taxonomic identifieri167539 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000001420 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003240081 – 418Light-independent protochlorophyllide reductase subunit NAdd BLAST418

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

1418
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi18 – 21Combined sources4
Helixi22 – 28Combined sources7
Beta strandi32 – 38Combined sources7
Helixi40 – 50Combined sources11
Beta strandi60 – 64Combined sources5
Helixi67 – 70Combined sources4
Helixi76 – 90Combined sources15
Beta strandi95 – 101Combined sources7
Helixi103 – 107Combined sources5
Helixi112 – 123Combined sources12
Beta strandi124 – 126Combined sources3
Beta strandi128 – 133Combined sources6
Turni136 – 138Combined sources3
Helixi143 – 152Combined sources10
Helixi153 – 155Combined sources3
Beta strandi163 – 168Combined sources6
Helixi172 – 184Combined sources13
Beta strandi190 – 194Combined sources5
Beta strandi208 – 214Combined sources7
Helixi218 – 226Combined sources9
Helixi239 – 253Combined sources15
Helixi258 – 283Combined sources26
Beta strandi287 – 290Combined sources4
Beta strandi292 – 295Combined sources4
Helixi297 – 306Combined sources10
Beta strandi311 – 318Combined sources8
Turni322 – 324Combined sources3
Helixi326 – 331Combined sources6
Beta strandi337 – 341Combined sources5
Helixi344 – 354Combined sources11
Beta strandi357 – 361Combined sources5
Turni363 – 365Combined sources3
Helixi366 – 371Combined sources6
Beta strandi376 – 378Combined sources3
Helixi379 – 384Combined sources6
Helixi390 – 392Combined sources3
Helixi393 – 410Combined sources18

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the BchN/ChlN family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C78. Bacteria.
COG2710. LUCA.
KOiK04038.
OMAiREVFCGL.
OrthoDBiPOG091H13ZK.

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.

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.
WP_011124700.1. 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.
WP_011124700.1. NC_005042.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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

eggNOGiENOG4105C78. Bacteria.
COG2710. LUCA.
KOiK04038.
OMAiREVFCGL.
OrthoDBiPOG091H13ZK.

Enzyme and pathway databases

UniPathwayiUPA00670.

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_PROMA
AccessioniPrimary (citable) accession number: Q7VD37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 1, 2003
Last modified: November 2, 2016
This is version 68 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.