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Protein

Light-independent protochlorophyllide reductase subunit N

Gene

bchN

Organism
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Status
Reviewed-Annotation score: Annotation score: 4 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 (BchN-BchB) is the catalytic component of the complex.UniRule annotation2 Publications

Catalytic activityi

Protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate.UniRule annotation1 Publication

Cofactori

[4Fe-4S] clusterUniRule annotation1 PublicationNote: Binds 1 [4Fe-4S] cluster per heterodimer (PubMed:20400946). The cluster is bound at the heterodimer interface by residues from both subunits (PubMed:20400946).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 bindingi26Iron-sulfur (4Fe-4S); shared with heterodimeric partner1 Publication1
Metal bindingi51Iron-sulfur (4Fe-4S); shared with heterodimeric partner1 Publication1
Metal bindingi112Iron-sulfur (4Fe-4S); shared with heterodimeric partner1 Publication1

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, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13269.
BRENDAi1.3.7.7. 5381.
UniPathwayiUPA00671.

Names & Taxonomyi

Protein namesi
Recommended name:
Light-independent protochlorophyllide reductase subunit NUniRule annotation (EC:1.3.7.7UniRule annotation1 Publication)
Short name:
DPOR subunit NUniRule annotation
Short name:
LI-POR subunit NUniRule annotation
Gene namesi
Name:bchNUniRule annotation
Ordered Locus Names:RCAP_rcc00665
OrganismiRhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Taxonomic identifieri272942 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000002361 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi25F → A: Retains 50% activity. 1 Publication1
Mutagenesisi26C → A: Does not form heterotetramers. 1 Publication1
Mutagenesisi51C → A: Does not form heterotetramers. 1 Publication1
Mutagenesisi112C → A: Does not form heterotetramers. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002085961 – 424Light-independent protochlorophyllide reductase subunit NAdd BLAST424

Interactioni

Subunit structurei

Protochlorophyllide reductase is composed of three subunits; BchL, BchN and BchB. Forms a heterotetramer of two BchB and two BchN subunits (PubMed:20400946).UniRule annotation1 Publication

Protein-protein interaction databases

DIPiDIP-59277N.
STRINGi272942.RCAP_rcc00665.

Structurei

Secondary structure

1424
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Beta strandi15 – 18Combined sources4
Helixi27 – 30Combined sources4
Helixi31 – 37Combined sources7
Beta strandi41 – 47Combined sources7
Helixi49 – 59Combined sources11
Helixi60 – 64Combined sources5
Beta strandi68 – 73Combined sources6
Helixi76 – 79Combined sources4
Beta strandi80 – 82Combined sources3
Helixi85 – 98Combined sources14
Beta strandi105 – 110Combined sources6
Helixi112 – 116Combined sources5
Helixi121 – 131Combined sources11
Turni133 – 135Combined sources3
Beta strandi137 – 142Combined sources6
Turni145 – 147Combined sources3
Helixi152 – 161Combined sources10
Helixi162 – 164Combined sources3
Beta strandi173 – 177Combined sources5
Helixi181 – 193Combined sources13
Beta strandi199 – 203Combined sources5
Helixi207 – 209Combined sources3
Beta strandi218 – 223Combined sources6
Helixi227 – 235Combined sources9
Beta strandi239 – 241Combined sources3
Helixi248 – 262Combined sources15
Helixi267 – 286Combined sources20
Helixi289 – 292Combined sources4
Beta strandi296 – 299Combined sources4
Beta strandi301 – 304Combined sources4
Helixi306 – 315Combined sources10
Beta strandi320 – 327Combined sources8
Helixi331 – 338Combined sources8
Beta strandi346 – 350Combined sources5
Helixi353 – 363Combined sources11
Beta strandi366 – 370Combined sources5
Helixi372 – 379Combined sources8
Turni380 – 382Combined sources3
Beta strandi385 – 387Combined sources3
Helixi388 – 391Combined sources4
Beta strandi397 – 399Combined sources3
Helixi402 – 420Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AEKX-ray2.30A/C2-424[»]
3AEQX-ray2.90A/C2-424[»]
3AERX-ray2.80A/C2-424[»]
3AESX-ray2.50A/C2-424[»]
3AETX-ray2.91A/C2-424[»]
3AEUX-ray2.90A/C2-424[»]
ProteinModelPortaliP26164.
SMRiP26164.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26164.

Family & Domainsi

Sequence similaritiesi

Belongs to the BchN/ChlN family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C78. Bacteria.
COG2710. LUCA.
HOGENOMiHOG000265994.
KOiK04038.
OMAiREVFCGL.
OrthoDBiPOG091H13ZK.

Family and domain databases

HAMAPiMF_00352. ChlN_BchN. 1 hit.
InterProiIPR000510. Nase/OxRdtase_comp1.
IPR005970. Protochl_reductN.
[Graphical view]
PfamiPF00148. Oxidored_nitro. 1 hit.
[Graphical view]
PIRSFiPIRSF000162. P_chlorophyll_rd. 1 hit.
TIGRFAMsiTIGR01279. DPOR_bchN. 1 hit.

Sequencei

Sequence statusi: Complete.

P26164-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLDSPTFGC TDSPVRRERG QKAVFCGLTS IVWLHRKMQD AFFLVVGSRT
60 70 80 90 100
CAHLLQAAAG VMIFAEPRFG TAVLEEQDLA GLADAHKELD REVAKLLERR
110 120 130 140 150
PDIRQLFLVG SCPSEVLKLD LDRAAERLSG LHAPHVRVYS YTGSGLDTTF
160 170 180 190 200
TQGEDTCLAA MVPTLDTTEA AELIVVGALP DVVEDQCLSL LTQLGVGPVR
210 220 230 240 250
MLPARRSDIE PAVGPNTRFI LAQPFLGETT GALERRGAKR IAAPFPFGEE
260 270 280 290 300
GTTLWLKAVA DAYGVSAEKF EAVTAAPRAR AKKAIAAHLE TLTGKSLFMF
310 320 330 340 350
PDSQLEIPLA RFLARECGMK TTEIATPFLH KAIMAPDLAL LPSNTALTEG
360 370 380 390 400
QDLEAQLDRH EAINPDLTVC GLGLANPLEA KGHATKWAIE LVFTPVHFYE
410 420
QAGDLAGLFS RPLRRRALLN GGAA
Length:424
Mass (Da):45,830
Last modified:May 1, 1992 - v1
Checksum:iC90C75233802834D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11165 Genomic DNA. Translation: CAA77526.1.
CP001312 Genomic DNA. Translation: ADE84430.1.
PIRiB49851.
RefSeqiWP_013066409.1. NC_014034.1.

Genome annotation databases

EnsemblBacteriaiADE84430; ADE84430; RCAP_rcc00665.
KEGGircp:RCAP_rcc00665.
PATRICi35501398. VBIRhoCap134200_0676.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11165 Genomic DNA. Translation: CAA77526.1.
CP001312 Genomic DNA. Translation: ADE84430.1.
PIRiB49851.
RefSeqiWP_013066409.1. NC_014034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AEKX-ray2.30A/C2-424[»]
3AEQX-ray2.90A/C2-424[»]
3AERX-ray2.80A/C2-424[»]
3AESX-ray2.50A/C2-424[»]
3AETX-ray2.91A/C2-424[»]
3AEUX-ray2.90A/C2-424[»]
ProteinModelPortaliP26164.
SMRiP26164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59277N.
STRINGi272942.RCAP_rcc00665.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADE84430; ADE84430; RCAP_rcc00665.
KEGGircp:RCAP_rcc00665.
PATRICi35501398. VBIRhoCap134200_0676.

Phylogenomic databases

eggNOGiENOG4105C78. Bacteria.
COG2710. LUCA.
HOGENOMiHOG000265994.
KOiK04038.
OMAiREVFCGL.
OrthoDBiPOG091H13ZK.

Enzyme and pathway databases

UniPathwayiUPA00671.
BioCyciMetaCyc:MONOMER-13269.
BRENDAi1.3.7.7. 5381.

Miscellaneous databases

EvolutionaryTraceiP26164.

Family and domain databases

HAMAPiMF_00352. ChlN_BchN. 1 hit.
InterProiIPR000510. Nase/OxRdtase_comp1.
IPR005970. Protochl_reductN.
[Graphical view]
PfamiPF00148. Oxidored_nitro. 1 hit.
[Graphical view]
PIRSFiPIRSF000162. P_chlorophyll_rd. 1 hit.
TIGRFAMsiTIGR01279. DPOR_bchN. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiBCHN_RHOCB
AccessioniPrimary (citable) accession number: P26164
Secondary accession number(s): D5ANS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 2, 2016
This is version 91 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.