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Protein

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

Gene

bchL

Organism
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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: bacteriochlorophyll biosynthesis (light-independent)

This protein is involved in the pathway bacteriochlorophyll 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 bacteriochlorophyll biosynthesis (light-independent) and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451MagnesiumUniRule annotation
Binding sitei70 – 701ATPUniRule annotation
Metal bindingi126 – 1261Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation
Metal bindingi160 – 1601Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi41 – 466ATPUniRule annotation
Nucleotide bindingi211 – 2122ATPUniRule annotation
Nucleotide bindingi235 – 2373ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Bacteriochlorophyll biosynthesis, Chlorophyll biosynthesis, Photosynthesis

Keywords - Ligandi

4Fe-4S, ATP-binding, Iron, Iron-sulfur, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciRSPH349102:GHE1-2335-MONOMER.
UniPathwayiUPA00671.

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:bchLUniRule annotation
Ordered Locus Names:Rsph17025_1007
OrganismiRhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Taxonomic identifieri349102 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000000234 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297Light-independent protochlorophyllide reductase iron-sulfur ATP-binding proteinPRO_1000048467Add
BLAST

Interactioni

Subunit structurei

Homodimer. Protochlorophyllide reductase is composed of three subunits; BchL, BchN and BchB.UniRule annotation

Protein-protein interaction databases

STRINGi349102.Rsph17025_1007.

Structurei

3D structure databases

ProteinModelPortaliA4WR94.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DSM. Bacteria.
COG1348. LUCA.
HOGENOMiHOG000228825.
KOiK04037.
OMAiTSCNISV.
OrthoDBiPOG091H0230.

Family and domain databases

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.

A4WR94-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPKDLTIPT GEDGEGSVQV HLDESDKITG AKVFAVYGKG GIGKSTTSSN
60 70 80 90 100
LSAAFSILGK RVLQIGCDPK HDSTFTLTGS LVPTVIDVLK DVDFHPEELR
110 120 130 140 150
PEDFVFEGFN GVMCVEAGGP PAGTGCGGYV VGQTVKLLKQ HHLLDDTDVV
160 170 180 190 200
IFDVLGDVVC GGFAAPLQHA DQAVVVTAND FDSIYAMNRI IAAVQAKSKN
210 220 230 240 250
YKVRLAGCVA NRSRATDEVD RFCEASDFRR LAHMPDLDAI RRSRLKKKTL
260 270 280 290
FAMDEDPDVL VARAEYLRLA QSLWDGLPPM SPHSLPDREI FELLGFD
Length:297
Mass (Da):32,182
Last modified:May 29, 2007 - v1
Checksum:i7E20961C6CB28A4C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000661 Genomic DNA. Translation: ABP69908.1.
RefSeqiWP_011908046.1. NC_009428.1.

Genome annotation databases

EnsemblBacteriaiABP69908; ABP69908; Rsph17025_1007.
KEGGirsq:Rsph17025_1007.
PATRICi23160195. VBIRhoSph94549_1031.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000661 Genomic DNA. Translation: ABP69908.1.
RefSeqiWP_011908046.1. NC_009428.1.

3D structure databases

ProteinModelPortaliA4WR94.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi349102.Rsph17025_1007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP69908; ABP69908; Rsph17025_1007.
KEGGirsq:Rsph17025_1007.
PATRICi23160195. VBIRhoSph94549_1031.

Phylogenomic databases

eggNOGiENOG4105DSM. Bacteria.
COG1348. LUCA.
HOGENOMiHOG000228825.
KOiK04037.
OMAiTSCNISV.
OrthoDBiPOG091H0230.

Enzyme and pathway databases

UniPathwayiUPA00671.
BioCyciRSPH349102:GHE1-2335-MONOMER.

Family and domain databases

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 nameiBCHL_RHOS5
AccessioniPrimary (citable) accession number: A4WR94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: September 7, 2016
This is version 66 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

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.