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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)DescriptionActionsGraphical viewLength
Metal bindingi36Iron-sulfur (4Fe-4S); shared with heterodimeric partnerUniRule annotation1
Active sitei294Proton donorUniRule 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 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 lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeThermosynechococcus
Proteomesi
  • UP000000440 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002198051 – 508Light-independent protochlorophyllide reductase subunit BAdd BLAST508

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

1508
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Helixi12 – 20Combined sources9
Beta strandi26 – 32Combined sources7
Turni34 – 37Combined sources4
Helixi38 – 46Combined sources9
Beta strandi54 – 59Combined sources6
Turni62 – 67Combined sources6
Beta strandi69 – 71Combined sources3
Helixi72 – 84Combined sources13
Beta strandi87 – 92Combined sources6
Helixi95 – 98Combined sources4
Helixi104 – 114Combined sources11
Beta strandi116 – 121Combined sources6
Turni126 – 128Combined sources3
Helixi131 – 153Combined sources23
Beta strandi165 – 171Combined sources7
Helixi178 – 192Combined sources15
Beta strandi195 – 201Combined sources7
Turni206 – 208Combined sources3
Helixi209 – 214Combined sources6
Beta strandi215 – 219Combined sources5
Helixi227 – 237Combined sources11
Helixi249 – 264Combined sources16
Turni265 – 267Combined sources3
Helixi273 – 282Combined sources10
Helixi286 – 291Combined sources6
Helixi293 – 296Combined sources4
Turni297 – 300Combined sources4
Beta strandi302 – 307Combined sources6
Helixi309 – 323Combined sources15
Beta strandi326 – 333Combined sources8
Helixi335 – 337Combined sources3
Helixi338 – 345Combined sources8
Turni346 – 348Combined sources3
Beta strandi349 – 354Combined sources6
Helixi358 – 368Combined sources11
Beta strandi371 – 375Combined sources5
Helixi377 – 386Combined sources10
Beta strandi390 – 392Combined sources3
Beta strandi394 – 396Combined sources3
Helixi399 – 401Combined sources3
Helixi411 – 438Combined sources28

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ8DGC6.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni429 – 430Substrate bindingUniRule annotation2

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105EVY. Bacteria.
COG2710. LUCA.
HOGENOMiHOG000032963.
KOiK04039.
OMAiIPCAVIS.
OrthoDBiPOG091H00BO.

Family and domain databases

HAMAPiMF_00353. ChlB_BchB. 1 hit.
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
PDB 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.
OrthoDBiPOG091H00BO.

Enzyme and pathway databases

UniPathwayiUPA00670.

Miscellaneous databases

EvolutionaryTraceiQ8DGC6.

Family and domain databases

HAMAPiMF_00353. ChlB_BchB. 1 hit.
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...

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 2, 2016
This is version 81 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.