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Protein

Light-independent protochlorophyllide reductase subunit B

Gene

chlB

Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
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 sitei290Proton 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:Pro_0545
OrganismiProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
Taxonomic identifieri167539 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000001420 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000484111 – 530Light-independent protochlorophyllide reductase subunit BAdd BLAST530

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

STRINGi167539.Pro0545.

Structurei

Secondary structure

1530
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi12 – 22Combined sources11
Beta strandi23 – 31Combined sources9
Helixi36 – 39Combined sources4
Helixi40 – 44Combined sources5
Beta strandi54 – 57Combined sources4
Helixi62 – 66Combined sources5
Helixi69 – 84Combined sources16
Beta strandi87 – 93Combined sources7
Helixi95 – 100Combined sources6
Helixi104 – 108Combined sources5
Turni109 – 112Combined sources4
Beta strandi117 – 119Combined sources3
Turni124 – 126Combined sources3
Helixi129 – 145Combined sources17
Helixi159 – 163Combined sources5
Beta strandi168 – 172Combined sources5
Beta strandi178 – 180Combined sources3
Helixi181 – 194Combined sources14
Beta strandi198 – 204Combined sources7
Helixi209 – 212Combined sources4
Helixi213 – 217Combined sources5
Beta strandi218 – 224Combined sources7
Helixi226 – 240Combined sources15
Helixi252 – 266Combined sources15
Helixi277 – 279Combined sources3
Helixi282 – 287Combined sources6
Helixi289 – 294Combined sources6
Beta strandi298 – 301Combined sources4
Helixi305 – 317Combined sources13
Beta strandi322 – 329Combined sources8
Helixi331 – 333Combined sources3
Helixi334 – 343Combined sources10
Helixi354 – 364Combined sources11
Beta strandi367 – 371Combined sources5
Helixi373 – 382Combined sources10
Beta strandi386 – 388Combined sources3
Beta strandi390 – 392Combined sources3
Helixi395 – 397Combined sources3
Helixi407 – 419Combined sources13
Helixi425 – 433Combined sources9
Beta strandi438 – 440Combined sources3
Helixi446 – 448Combined sources3
Helixi483 – 490Combined sources8
Helixi494 – 496Combined sources3
Helixi497 – 510Combined sources14
Helixi518 – 527Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YNMX-ray2.10D1-530[»]
ProteinModelPortaliQ7VD38.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni425 – 426Substrate bindingUniRule annotation2

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105EVY. Bacteria.
COG2710. LUCA.
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.

Q7VD38-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELTLWTYEG PPHIGAMRIA TSMKGLHYVL HAPQGDTYAD LLFTMIERRG
60 70 80 90 100
SRPPVTYTTF QARDLGGDTA ELVKGHIFEA VERFKPEALL VGESCTAELI
110 120 130 140 150
QDQPGSLAKG MGLNIPIVSL ELPAYSKKEN WGASETFYQL IRGLLKEISE
160 170 180 190 200
DSSNNAKQSW QEEGRRPRVN LLGPSLLGFR CRDDVLEIQK ILGENGIDIN
210 220 230 240 250
VIAPLGASPS DLMRLPKADA NVCLYPEIAE STCLWLERNF KTPFTKVVPI
260 270 280 290 300
GVKATQDFLE ELYELLGMEV SNSISNSDQS KLPWYSKSVD SNYLTGKRVF
310 320 330 340 350
IFGDGTHVLA AARIANEELG FEVVGIGTYS REMARKVRAA ATELGLEALI
360 370 380 390 400
TNDYLEVEES IKECAPELVL GTQMERHSAK RLGIPCAVIS TPMHVQDVPA
410 420 430 440 450
RYSPQMGWEG ANVIFDDWVH PLMMGLEEHL IGMFRHDFEF TDGHQSHLGH
460 470 480 490 500
LGGHASETKT SSKGINQSPN NHSPAGESIH WTSEGESELA KIPFFVRGKV
510 520 530
RRNTEKYARQ AGCREIDGET LLDAKAHFGA
Length:530
Mass (Da):58,729
Last modified:October 1, 2003 - v1
Checksum:i7D5A10C8B8D0FF2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAP99590.1.
RefSeqiNP_874938.1. NC_005042.1.
WP_011124699.1. NC_005042.1.

Genome annotation databases

EnsemblBacteriaiAAP99590; AAP99590; Pro_0545.
GeneIDi1461927.
KEGGipma:Pro_0545.
PATRICi23027723. VBIProMar8617_0560.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAP99590.1.
RefSeqiNP_874938.1. NC_005042.1.
WP_011124699.1. NC_005042.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YNMX-ray2.10D1-530[»]
ProteinModelPortaliQ7VD38.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi167539.Pro0545.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP99590; AAP99590; Pro_0545.
GeneIDi1461927.
KEGGipma:Pro_0545.
PATRICi23027723. VBIProMar8617_0560.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00670.

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_PROMA
AccessioniPrimary (citable) accession number: Q7VD38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2003
Last modified: November 2, 2016
This is version 75 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.