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Protein

Light-independent protochlorophyllide reductase subunit B

Gene

chlB

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Iron-sulfur (4Fe-4S); shared with heterodimeric partnerUniRule annotation
Active sitei294 – 2941Proton donorUniRule annotation

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 BUniRule annotation (EC:1.3.7.7UniRule annotation)
Short name:
DPOR subunit BUniRule annotation
Short name:
LI-POR subunit BUniRule annotation
Gene namesi
Name:chlBUniRule annotation
Ordered Locus Names:tll2392
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
Proteomesi
  • UP000000440 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508Light-independent protochlorophyllide reductase subunit BPRO_0000219805Add
BLAST

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.tll2392.

Structurei

Secondary structure

1
508
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Helixi12 – 209Combined sources
Beta strandi26 – 327Combined sources
Turni34 – 374Combined sources
Helixi38 – 469Combined sources
Beta strandi54 – 596Combined sources
Turni62 – 676Combined sources
Beta strandi69 – 713Combined sources
Helixi72 – 8413Combined sources
Beta strandi87 – 926Combined sources
Helixi95 – 984Combined sources
Helixi104 – 11411Combined sources
Beta strandi116 – 1216Combined sources
Turni126 – 1283Combined sources
Helixi131 – 15323Combined sources
Beta strandi165 – 1717Combined sources
Helixi178 – 19215Combined sources
Beta strandi195 – 2017Combined sources
Turni206 – 2083Combined sources
Helixi209 – 2146Combined sources
Beta strandi215 – 2195Combined sources
Helixi227 – 23711Combined sources
Helixi249 – 26416Combined sources
Turni265 – 2673Combined sources
Helixi273 – 28210Combined sources
Helixi286 – 2916Combined sources
Helixi293 – 2964Combined sources
Turni297 – 3004Combined sources
Beta strandi302 – 3076Combined sources
Helixi309 – 32315Combined sources
Beta strandi326 – 3338Combined sources
Helixi335 – 3373Combined sources
Helixi338 – 3458Combined sources
Turni346 – 3483Combined sources
Beta strandi349 – 3546Combined sources
Helixi358 – 36811Combined sources
Beta strandi371 – 3755Combined sources
Helixi377 – 38610Combined sources
Beta strandi390 – 3923Combined sources
Beta strandi394 – 3963Combined sources
Helixi399 – 4013Combined sources
Helixi411 – 43828Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XDQX-ray2.40B1-508[»]
ProteinModelPortaliQ8DGC6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8DGC6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni429 – 4302Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the ChlB/BchB/BchZ family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105EVY. Bacteria.
COG2710. LUCA.
HOGENOMiHOG000032963.
KOiK04039.
OMAiIPCAVIS.
OrthoDBiEOG6WX4K1.

Family and domain databases

HAMAPiMF_00353. ChlB_BchB.
InterProiIPR000510. Nase/OxRdtase_comp1.
IPR013580. P-CP/CP_red_C.
IPR005969. Protochl_reductB.
IPR016209. Protochlorophyllide_Rdtase.
[Graphical view]
PfamiPF00148. Oxidored_nitro. 1 hit.
PF08369. PCP_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000163. PCP_ChlB. 1 hit.
TIGRFAMsiTIGR01278. DPOR_BchB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8DGC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLAYWMYAG PAHIGTLRIA SSFKNVHGIM HAPLGDDYFN VMRSMLERER
60 70 80 90 100
DFTPVTASIV DRHVLARGSQ EKVVDNIIRK DTEEHPDLIV LTPTCTSSIL
110 120 130 140 150
QEDLQNFVRR ASLSTTADVL LADVNHYRVN ELQAADRTLE QIVQFYIDKA
160 170 180 190 200
RRQGTLGTSK TPTPSVNIIG ITTLGFHNQH DCRELKQLMA DLGIQVNLVI
210 220 230 240 250
PAAATVHDLQ RLPQAWFNLV PYREIGGLTA QYLEREFGQP SVRITPMGVV
260 270 280 290 300
ETARCIRAIQ GVLNAQGAGV NYEAFIEQQT REVSQAAWFS RSIDCQNLTG
310 320 330 340 350
KKAVVFGDNT HAAAMTKILS REMGIHVVWA GTYCKYDADW FRAEVAGFCD
360 370 380 390 400
EVLITDDHTV VGDAIARVEP AAIFGTQMER HVGKRLNIPC GVIAAPIHIQ
410 420 430 440 450
DFPVGYRPFL GYEGTNQLVD LIYNSFTLGM EDHLLEIFGG HDTKAVIHKG
460 470 480 490 500
LSADSDLTWT AAGLAELNKI PGFVRGKVKR NTEKFAREQG ISEITVEVLY

AAKEAVGA
Length:508
Mass (Da):56,317
Last modified:March 1, 2003 - v1
Checksum:i90C9BFCF89DD0789
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC09944.1.
RefSeqiNP_683182.1. NC_004113.1.
WP_011058224.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC09944; BAC09944; BAC09944.
GeneIDi1010370.
KEGGitel:tll2392.
PATRICi23930268. VBITheElo119873_2512.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC09944.1.
RefSeqiNP_683182.1. NC_004113.1.
WP_011058224.1. NC_004113.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XDQX-ray2.40B1-508[»]
ProteinModelPortaliQ8DGC6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi197221.tll2392.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC09944; BAC09944; BAC09944.
GeneIDi1010370.
KEGGitel:tll2392.
PATRICi23930268. VBITheElo119873_2512.

Phylogenomic databases

eggNOGiENOG4105EVY. Bacteria.
COG2710. LUCA.
HOGENOMiHOG000032963.
KOiK04039.
OMAiIPCAVIS.
OrthoDBiEOG6WX4K1.

Enzyme and pathway databases

UniPathwayiUPA00670.

Miscellaneous databases

EvolutionaryTraceiQ8DGC6.

Family and domain databases

HAMAPiMF_00353. ChlB_BchB.
InterProiIPR000510. Nase/OxRdtase_comp1.
IPR013580. P-CP/CP_red_C.
IPR005969. Protochl_reductB.
IPR016209. Protochlorophyllide_Rdtase.
[Graphical view]
PfamiPF00148. Oxidored_nitro. 1 hit.
PF08369. PCP_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000163. PCP_ChlB. 1 hit.
TIGRFAMsiTIGR01278. DPOR_BchB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BP-1.

Entry informationi

Entry nameiCHLB_THEEB
AccessioniPrimary (citable) accession number: Q8DGC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: March 1, 2003
Last modified: November 11, 2015
This is version 79 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.