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P26164 (BCHN_RHOCB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Light-independent protochlorophyllide reductase subunit N

Short name=DPOR subunit N
Short name=LI-POR subunit N
EC=1.18.-.-
Gene names
Name:bchN
Ordered Locus Names:RCAP_rcc00665
OrganismRhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) [Complete proteome] [HAMAP]
Taxonomic identifier272942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). The BchN-BchB pair binds Pchlide. This reaction is light-independent. HAMAP-Rule MF_00352

Pathway

Porphyrin biosynthesis; bacteriochlorophyll biosynthesis (light-independent). HAMAP-Rule MF_00352

Subunit structure

Protochlorophyllide reductase is thought to be composed of three subunits; BchL, BchN and BchB. Could form a heterotetramer of two BchB and two BchN subunits.

Sequence similarities

Belongs to the BchN/ChlN family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424Light-independent protochlorophyllide reductase subunit N HAMAP-Rule MF_00352
PRO_0000208596

Secondary structure

................................................................................. 424
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26164 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: C90C75233802834D

FASTA42445,830
        10         20         30         40         50         60 
MSLDSPTFGC TDSPVRRERG QKAVFCGLTS IVWLHRKMQD AFFLVVGSRT CAHLLQAAAG 

        70         80         90        100        110        120 
VMIFAEPRFG TAVLEEQDLA GLADAHKELD REVAKLLERR PDIRQLFLVG SCPSEVLKLD 

       130        140        150        160        170        180 
LDRAAERLSG LHAPHVRVYS YTGSGLDTTF TQGEDTCLAA MVPTLDTTEA AELIVVGALP 

       190        200        210        220        230        240 
DVVEDQCLSL LTQLGVGPVR MLPARRSDIE PAVGPNTRFI LAQPFLGETT GALERRGAKR 

       250        260        270        280        290        300 
IAAPFPFGEE GTTLWLKAVA DAYGVSAEKF EAVTAAPRAR AKKAIAAHLE TLTGKSLFMF 

       310        320        330        340        350        360 
PDSQLEIPLA RFLARECGMK TTEIATPFLH KAIMAPDLAL LPSNTALTEG QDLEAQLDRH 

       370        380        390        400        410        420 
EAINPDLTVC GLGLANPLEA KGHATKWAIE LVFTPVHFYE QAGDLAGLFS RPLRRRALLN 


GGAA 

« Hide

References

« Hide 'large scale' references
[1]"bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter capsulatus and identification of the third subunit of light-independent protochlorophyllide reductase in bacteria and plants."
Burke D.H., Alberti M., Hearst J.E.
J. Bacteriol. 175:2414-2422(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
[2]"Complete genome sequence of the photosynthetic purple nonsulfur bacterium Rhodobacter capsulatus SB 1003."
Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., Haselkorn R.
J. Bacteriol. 192:3545-3546(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
[3]"Reconstitution of light-independent protochlorophyllide reductase from purified bchL and bchN-bchB subunits. In vitro confirmation of nitrogenase-like features of a bacteriochlorophyll biosynthesis enzyme."
Fujita Y., Bauer C.E.
J. Biol. Chem. 275:23583-23588(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: SB1003 / CB1029.
[4]Fujita Y.
Unpublished observations (JUL-2001)
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11165 Genomic DNA. Translation: CAA77526.1.
CP001312 Genomic DNA. Translation: ADE84430.1.
PIRB49851.
RefSeqYP_003576837.1. NC_014034.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP26164.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-59277N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE84430; ADE84430; RCAP_rcc00665.
GeneID9003494.
KEGGrcp:RCAP_rcc00665.
PATRIC35501398. VBIRhoCap134200_0676.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000265994.
KOK04038.
OMAMIFAEPR.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13269.
RCAP272942:GJIY-678-MONOMER.
UniPathwayUPA00671.

Family and domain databases

HAMAPMF_00352. ChlN_BchN.
InterProIPR000510. Nase/OxRdtase_comp1.
IPR005970. Protochl_reductN.
[Graphical view]
PfamPF00148. Oxidored_nitro. 1 hit.
[Graphical view]
PIRSFPIRSF000162. P_chlorophyll_rd. 1 hit.
TIGRFAMsTIGR01279. DPOR_bchN. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP26164.

Entry information

Entry nameBCHN_RHOCB
AccessionPrimary (citable) accession number: P26164
Secondary accession number(s): D5ANS6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families