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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)DescriptionActionsGraphical viewLength
Metal bindingi36Iron-sulfur (4Fe-4S); shared with heterodimeric partner1 Publication1
Active sitei274Proton donorUniRule annotation1 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-13270.
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)DescriptionActionsGraphical viewLength
Mutagenesisi36D → A: Retains 13% activity. 1 Publication1
Mutagenesisi36D → C or S: Almost no enzymatic activity. 1 Publication1
Mutagenesisi95C → A: Does not form heterotetramers. 1 Publication1
Mutagenesisi274D → A: Almost no enzymatic activity. 1 Publication1
Mutagenesisi408M → A: Retains 85% activity. 1 Publication1
Mutagenesisi410L → A: Almost no enzymatic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002198001 – 525Light-independent protochlorophyllide reductase subunit BAdd BLAST525

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

1525
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Helixi12 – 20Combined sources9
Beta strandi23 – 31Combined sources9
Helixi36 – 39Combined sources4
Helixi40 – 45Combined sources6
Beta strandi54 – 57Combined sources4
Helixi62 – 64Combined sources3
Helixi68 – 84Combined sources17
Beta strandi87 – 93Combined sources7
Helixi97 – 99Combined sources3
Helixi104 – 111Combined sources8
Beta strandi117 – 119Combined sources3
Turni124 – 126Combined sources3
Helixi129 – 144Combined sources16
Beta strandi155 – 161Combined sources7
Helixi168 – 180Combined sources13
Turni181 – 183Combined sources3
Beta strandi185 – 191Combined sources7
Helixi196 – 200Combined sources5
Helixi201 – 204Combined sources4
Beta strandi205 – 210Combined sources6
Helixi213 – 226Combined sources14
Helixi239 – 253Combined sources15
Helixi266 – 271Combined sources6
Helixi273 – 278Combined sources6
Beta strandi282 – 285Combined sources4
Helixi289 – 301Combined sources13
Beta strandi306 – 313Combined sources8
Helixi315 – 317Combined sources3
Helixi318 – 327Combined sources10
Helixi338 – 348Combined sources11
Beta strandi351 – 355Combined sources5
Helixi357 – 366Combined sources10
Beta strandi370 – 372Combined sources3
Beta strandi374 – 376Combined sources3
Helixi379 – 381Combined sources3
Helixi391 – 403Combined sources13
Helixi409 – 417Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP26163.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26163.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni409 – 410Substrate binding1 Publication2

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
PDB 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.
SMRiP26163.
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.
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: November 2, 2016
This is version 97 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.