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Protein

Light-independent protochlorophyllide reductase subunit B

Gene

bchB

Organism
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
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 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Iron-sulfur (4Fe-4S); shared with heterodimeric partner1 Publication
Active sitei274 – 2741Proton donorUniRule annotation1 Publication

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-13270.
RCAP272942:GJIY-677-MONOMER.
BRENDAi1.3.7.7. 5381.
UniPathwayiUPA00671.

Names & Taxonomyi

Protein namesi
Recommended name:
Light-independent protochlorophyllide reductase subunit BUniRule annotation (EC:1.3.7.7UniRule annotation1 Publication)
Short name:
DPOR subunit BUniRule annotation
Short name:
LI-POR subunit BUniRule annotation
Gene namesi
Name:bchBUniRule annotation
Synonyms:bchK
Ordered Locus Names:RCAP_rcc00664
OrganismiRhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Taxonomic identifieri272942 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000002361 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 361D → A: Retains 13% activity. 1 Publication
Mutagenesisi36 – 361D → C or S: Almost no enzymatic activity. 1 Publication
Mutagenesisi95 – 951C → A: Does not form heterotetramers. 1 Publication
Mutagenesisi274 – 2741D → A: Almost no enzymatic activity. 1 Publication
Mutagenesisi408 – 4081M → A: Retains 85% activity. 1 Publication
Mutagenesisi410 – 4101L → A: Almost no enzymatic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 525525Light-independent protochlorophyllide reductase subunit BPRO_0000219800Add
BLAST

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-59276N.
STRINGi272942.RCAP_rcc00664.

Structurei

Secondary structure

1
525
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Helixi12 – 209Combined sources
Beta strandi23 – 319Combined sources
Helixi36 – 394Combined sources
Helixi40 – 456Combined sources
Beta strandi54 – 574Combined sources
Helixi62 – 643Combined sources
Helixi68 – 8417Combined sources
Beta strandi87 – 937Combined sources
Helixi97 – 993Combined sources
Helixi104 – 1118Combined sources
Beta strandi117 – 1193Combined sources
Turni124 – 1263Combined sources
Helixi129 – 14416Combined sources
Beta strandi155 – 1617Combined sources
Helixi168 – 18013Combined sources
Turni181 – 1833Combined sources
Beta strandi185 – 1917Combined sources
Helixi196 – 2005Combined sources
Helixi201 – 2044Combined sources
Beta strandi205 – 2106Combined sources
Helixi213 – 22614Combined sources
Helixi239 – 25315Combined sources
Helixi266 – 2716Combined sources
Helixi273 – 2786Combined sources
Beta strandi282 – 2854Combined sources
Helixi289 – 30113Combined sources
Beta strandi306 – 3138Combined sources
Helixi315 – 3173Combined sources
Helixi318 – 32710Combined sources
Helixi338 – 34811Combined sources
Beta strandi351 – 3555Combined sources
Helixi357 – 36610Combined sources
Beta strandi370 – 3723Combined sources
Beta strandi374 – 3763Combined sources
Helixi379 – 3813Combined sources
Helixi391 – 40313Combined sources
Helixi409 – 4179Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AEKX-ray2.30B/D1-525[»]
3AEQX-ray2.90B/D1-525[»]
3AERX-ray2.80B/D1-525[»]
3AESX-ray2.50B/D1-525[»]
3AETX-ray2.91B/D1-525[»]
3AEUX-ray2.90B/D1-525[»]
ProteinModelPortaliP26163.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26163.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni409 – 4102Substrate binding1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105EVY. Bacteria.
COG2710. LUCA.
HOGENOMiHOG000032963.
KOiK04039.
OMAiIPCAVIS.
OrthoDBiPOG091H1082.

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.

P26163-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLTLWTYEG PPHVGAMRVA TAMKDLQLVL HGPQGDTYAD LLFTMIERRN
60 70 80 90 100
ARPPVSFSTF EASHMGTDTA ILLKDALAAA HARYKPQAMA VALTCTAELL
110 120 130 140 150
QDDPNGISRA LNLPVPVVPL ELPSYSRKEN YGADETFRAL VRALAVPMER
160 170 180 190 200
TPEVTCNLLG ATALGFRHRD DVAEVTKLLA TMGIKVNVCA PLGASPDDLR
210 220 230 240 250
KLGQAHFNVL MYPETGESAA RHLERACKQP FTKIVPIGVG ATRDFLAEVS
260 270 280 290 300
KITGLPVVTD ESTLRQPWWS ASVDSTYLTG KRVFIFGDGT HVIAAARIAA
310 320 330 340 350
KEVGFEVVGM GCYNREMARP LRTAAAEYGL EALITDDYLE VEKAIEAAAP
360 370 380 390 400
ELILGTQMER NIAKKLGLPC AVISAPVHVQ DFPARYAPQM GFEGANVLFD
410 420 430 440 450
TWVHPLVMGL EEHLLTMFRE DFEFHDAAGA SHHGGKAVAR EESPVAPADL
460 470 480 490 500
APAATSDTPA APSPVVVTQA SGEIRWMPEA ERELRKIPFF VRGKAKRNTE
510 520
LYAAHKGVCD ITVETLYEAK AHYAR
Length:525
Mass (Da):57,192
Last modified:May 1, 1992 - v1
Checksum:i4322A6D9F535C3F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11165 Genomic DNA. Translation: CAA77525.1.
CP001312 Genomic DNA. Translation: ADE84429.1.
PIRiC49851.
RefSeqiWP_013066408.1. NC_014034.1.

Genome annotation databases

EnsemblBacteriaiADE84429; ADE84429; RCAP_rcc00664.
KEGGircp:RCAP_rcc00664.
PATRICi35501396. VBIRhoCap134200_0675.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11165 Genomic DNA. Translation: CAA77525.1.
CP001312 Genomic DNA. Translation: ADE84429.1.
PIRiC49851.
RefSeqiWP_013066408.1. NC_014034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AEKX-ray2.30B/D1-525[»]
3AEQX-ray2.90B/D1-525[»]
3AERX-ray2.80B/D1-525[»]
3AESX-ray2.50B/D1-525[»]
3AETX-ray2.91B/D1-525[»]
3AEUX-ray2.90B/D1-525[»]
ProteinModelPortaliP26163.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59276N.
STRINGi272942.RCAP_rcc00664.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADE84429; ADE84429; RCAP_rcc00664.
KEGGircp:RCAP_rcc00664.
PATRICi35501396. VBIRhoCap134200_0675.

Phylogenomic databases

eggNOGiENOG4105EVY. Bacteria.
COG2710. LUCA.
HOGENOMiHOG000032963.
KOiK04039.
OMAiIPCAVIS.
OrthoDBiPOG091H1082.

Enzyme and pathway databases

UniPathwayiUPA00671.
BioCyciMetaCyc:MONOMER-13270.
RCAP272942:GJIY-677-MONOMER.
BRENDAi1.3.7.7. 5381.

Miscellaneous databases

EvolutionaryTraceiP26163.

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 nameiBCHB_RHOCB
AccessioniPrimary (citable) accession number: P26163
Secondary accession number(s): D5ANS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: September 7, 2016
This is version 96 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, Direct protein sequencing, 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.