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Protein

Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein

Gene

chlL

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 L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.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 dimer.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 bindingi43MagnesiumUniRule annotation1
Binding sitei68ATPUniRule annotation1
Metal bindingi124Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation1
Metal bindingi158Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi39 – 44ATPUniRule annotation6
Nucleotide bindingi209 – 210ATPUniRule annotation2

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, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi1.3.1.33. 5023.
1.3.7.7. 5023.
UniPathwayiUPA00670.

Names & Taxonomyi

Protein namesi
Recommended name:
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding proteinUniRule annotation (EC:1.3.7.7UniRule annotation)
Short name:
DPOR subunit LUniRule annotation
Short name:
LI-POR subunit LUniRule annotation
Gene namesi
Name:chlLUniRule annotation
Ordered Locus Names:Pro_0544
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_00003240571 – 296Light-independent protochlorophyllide reductase iron-sulfur ATP-binding proteinAdd BLAST296

Interactioni

Subunit structurei

Homodimer. Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB.UniRule annotation

Protein-protein interaction databases

STRINGi167539.Pro0544.

Structurei

Secondary structure

1296
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 37Combined sources8
Helixi42 – 55Combined sources14
Beta strandi60 – 66Combined sources7
Helixi73 – 76Combined sources4
Helixi83 – 89Combined sources7
Turni90 – 92Combined sources3
Helixi94 – 96Combined sources3
Helixi99 – 102Combined sources4
Helixi107 – 109Combined sources3
Beta strandi111 – 114Combined sources4
Beta strandi122 – 124Combined sources3
Helixi125 – 138Combined sources14
Turni139 – 143Combined sources5
Beta strandi144 – 152Combined sources9
Helixi159 – 161Combined sources3
Helixi163 – 166Combined sources4
Beta strandi169 – 175Combined sources7
Helixi179 – 195Combined sources17
Turni196 – 198Combined sources3
Beta strandi202 – 210Combined sources9
Helixi215 – 224Combined sources10
Beta strandi228 – 232Combined sources5
Helixi236 – 243Combined sources8
Helixi248 – 250Combined sources3
Helixi258 – 274Combined sources17
Helixi286 – 292Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YNMX-ray2.10A/B1-296[»]
ProteinModelPortaliQ7VD39.
SMRiQ7VD39.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NifH/BchL/ChlL family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DSM. Bacteria.
COG1348. LUCA.
KOiK04037.
OMAiTSCNISV.
OrthoDBiPOG091H0230.

Family and domain databases

CDDicd02032. Bchl_like. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00355. ChlL_BchL. 1 hit.
InterProiIPR030655. NifH/chlL_CS.
IPR000392. Nitogenase_NifH/Reductase_ChlL.
IPR027417. P-loop_NTPase.
IPR005971. Protochlorophyllide_ATP-bd.
[Graphical view]
PIRSFiPIRSF000363. Nitrogenase_iron. 1 hit.
PRINTSiPR00091. NITROGNASEII.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01281. DPOR_bchL. 1 hit.
PROSITEiPS00746. NIFH_FRXC_1. 1 hit.
PS00692. NIFH_FRXC_2. 1 hit.
PS51026. NIFH_FRXC_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7VD39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTTLANRPD GEGSVQVKLD PKVNIEEGAL VIAVYGKGGI GKSTTSSNLS
60 70 80 90 100
AAFSKLGKKV LQIGCDPKHD STFTLTHKMV PTVIDILEEV DFHSEELRPQ
110 120 130 140 150
DFMFEGFNGV QCVESGGPPA GTGCGGYVTG QTVKLLKEHH LLEDTDVVIF
160 170 180 190 200
DVLGDVVCGG FAAPLQHANY CLIVTANDFD SIFAMNRIVA AINAKAKNYK
210 220 230 240 250
VRLGGVIANR SAELDQIEKF NEKTGLKTMA HFRNVDAIRR SRLKKCTIFE
260 270 280 290
MDPEEEGVLE VQNEYLSLAK KMIDNVEPLE AEPLKDREIF DLLGFD
Length:296
Mass (Da):32,395
Last modified:October 1, 2003 - v1
Checksum:iD46A27CE10432012
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAP99589.1.
RefSeqiNP_874937.1. NC_005042.1.
WP_011124698.1. NC_005042.1.

Genome annotation databases

EnsemblBacteriaiAAP99589; AAP99589; Pro_0544.
GeneIDi1461926.
KEGGipma:Pro_0544.
PATRICi23027721. VBIProMar8617_0559.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAP99589.1.
RefSeqiNP_874937.1. NC_005042.1.
WP_011124698.1. NC_005042.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YNMX-ray2.10A/B1-296[»]
ProteinModelPortaliQ7VD39.
SMRiQ7VD39.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi167539.Pro0544.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP99589; AAP99589; Pro_0544.
GeneIDi1461926.
KEGGipma:Pro_0544.
PATRICi23027721. VBIProMar8617_0559.

Phylogenomic databases

eggNOGiENOG4105DSM. Bacteria.
COG1348. LUCA.
KOiK04037.
OMAiTSCNISV.
OrthoDBiPOG091H0230.

Enzyme and pathway databases

UniPathwayiUPA00670.
BRENDAi1.3.1.33. 5023.
1.3.7.7. 5023.

Family and domain databases

CDDicd02032. Bchl_like. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00355. ChlL_BchL. 1 hit.
InterProiIPR030655. NifH/chlL_CS.
IPR000392. Nitogenase_NifH/Reductase_ChlL.
IPR027417. P-loop_NTPase.
IPR005971. Protochlorophyllide_ATP-bd.
[Graphical view]
PIRSFiPIRSF000363. Nitrogenase_iron. 1 hit.
PRINTSiPR00091. NITROGNASEII.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01281. DPOR_bchL. 1 hit.
PROSITEiPS00746. NIFH_FRXC_1. 1 hit.
PS00692. NIFH_FRXC_2. 1 hit.
PS51026. NIFH_FRXC_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCHLL_PROMA
AccessioniPrimary (citable) accession number: Q7VD39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 1, 2003
Last modified: November 2, 2016
This is version 88 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.