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Protein

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

Gene

bchL

Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Status
Reviewed-Annotation score: Annotation score: 5 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 annotation1 Publication

Catalytic activityi

Protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotation1 PublicationNote: Binds 1 [4Fe-4S] cluster per dimer.UniRule annotation1 Publication

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)DescriptionActionsGraphical viewLength
Metal bindingi45Magnesium1 Publication1
Binding sitei70ATP1 Publication1
Metal bindingi126Iron-sulfur (4Fe-4S); shared with homodimeric partner1 Publication1
Metal bindingi160Iron-sulfur (4Fe-4S); shared with homodimeric partner1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi41 – 46ATP1 Publication6
Nucleotide bindingi211 – 212ATP1 Publication2
Nucleotide bindingi235 – 237ATP1 Publication3

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

BRENDAi1.3.7.7. 5383.
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:RHOS4_18930
ORF Names:RSP_0288
OrganismiRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Taxonomic identifieri272943 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000002703 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001395821 – 297Light-independent protochlorophyllide reductase iron-sulfur ATP-binding proteinAdd BLAST297

Interactioni

Subunit structurei

Homodimer (PubMed:19006326). Protochlorophyllide reductase is composed of three subunits; BchL, BchN and BchB.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi272943.RSP_0288.

Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 37Combined sources6
Helixi44 – 57Combined sources14
Beta strandi62 – 70Combined sources9
Helixi75 – 78Combined sources4
Helixi85 – 91Combined sources7
Helixi96 – 98Combined sources3
Helixi101 – 104Combined sources4
Helixi109 – 111Combined sources3
Beta strandi113 – 116Combined sources4
Helixi129 – 140Combined sources12
Turni141 – 144Combined sources4
Beta strandi148 – 154Combined sources7
Helixi161 – 168Combined sources8
Beta strandi171 – 177Combined sources7
Helixi181 – 195Combined sources15
Turni196 – 200Combined sources5
Beta strandi204 – 212Combined sources9
Helixi217 – 226Combined sources10
Beta strandi230 – 234Combined sources5
Helixi238 – 245Combined sources8
Turni250 – 252Combined sources3
Helixi257 – 275Combined sources19
Helixi287 – 293Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FWYX-ray1.63A/B2-297[»]
ProteinModelPortaliQ9RFD6.
SMRiQ9RFD6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RFD6.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DSM. Bacteria.
COG1348. LUCA.
HOGENOMiHOG000228825.
KOiK04037.
OMAiTSCNISV.
OrthoDBiPOG091H0230.
PhylomeDBiQ9RFD6.

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.

Q9RFD6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPKDLTIPT GADGEGSVQV HLDEADKITG 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 RFCKETNFRR LAHMPDLDAI RRSRLKKKTL
260 270 280 290
FEMDEDQDVL AARAEYIRLA ESLWRGLDPI DPHSLPDRDI FELLGFD
Length:297
Mass (Da):32,295
Last modified:January 24, 2006 - v2
Checksum:iBDDE6F40A21952CE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14G → V in AAF24272 (PubMed:10648776).Curated1
Sequence conflicti194V → A in CAB38722 (Ref. 2) Curated1
Sequence conflicti261 – 262AA → VV in AAF24272 (PubMed:10648776).Curated2
Sequence conflicti269L → V in CAB38722 (Ref. 2) Curated1
Sequence conflicti273L → F in AAF24272 (PubMed:10648776).Curated1
Sequence conflicti278D → Y in AAF24272 (PubMed:10648776).Curated1
Sequence conflicti284S → R in AAF24272 (PubMed:10648776).Curated1
Sequence conflicti289D → E in AAF24272 (PubMed:10648776).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195122 Genomic DNA. Translation: AAF24272.1.
AJ010302 Genomic DNA. Translation: CAB38722.1.
CP000143 Genomic DNA. Translation: ABA79461.1.
PIRiT50728.
RefSeqiWP_011338126.1. NZ_AKVW01000001.1.
YP_353362.1. NC_007493.2.

Genome annotation databases

EnsemblBacteriaiABA79461; ABA79461; RSP_0288.
GeneIDi3719200.
KEGGirsp:RSP_0288.
PATRICi23153714. VBIRhoSph57909_2232.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195122 Genomic DNA. Translation: AAF24272.1.
AJ010302 Genomic DNA. Translation: CAB38722.1.
CP000143 Genomic DNA. Translation: ABA79461.1.
PIRiT50728.
RefSeqiWP_011338126.1. NZ_AKVW01000001.1.
YP_353362.1. NC_007493.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FWYX-ray1.63A/B2-297[»]
ProteinModelPortaliQ9RFD6.
SMRiQ9RFD6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272943.RSP_0288.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA79461; ABA79461; RSP_0288.
GeneIDi3719200.
KEGGirsp:RSP_0288.
PATRICi23153714. VBIRhoSph57909_2232.

Phylogenomic databases

eggNOGiENOG4105DSM. Bacteria.
COG1348. LUCA.
HOGENOMiHOG000228825.
KOiK04037.
OMAiTSCNISV.
OrthoDBiPOG091H0230.
PhylomeDBiQ9RFD6.

Enzyme and pathway databases

UniPathwayiUPA00671.
BRENDAi1.3.7.7. 5383.

Miscellaneous databases

EvolutionaryTraceiQ9RFD6.

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 nameiBCHL_RHOS4
AccessioniPrimary (citable) accession number: Q9RFD6
Secondary accession number(s): Q3J173, Q9Z5E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 24, 2006
Last modified: November 2, 2016
This is version 115 of the entry and version 2 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.