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Protein

Light-independent protochlorophyllide reductase subunit B

Gene

chlB

Organism
Anabaena variabilis (strain ATCC 29413 / PCC 7937)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Iron-sulfur (4Fe-4S); shared with heterodimeric partnerUniRule annotation
Active sitei294 – 2941Proton donorUniRule annotation

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

BioCyciAVAR240292:GCY3-3512-MONOMER.
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:Ava_3466
OrganismiAnabaena variabilis (strain ATCC 29413 / PCC 7937)
Taxonomic identifieri240292 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena
Proteomesi
  • UP000002533 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508Light-independent protochlorophyllide reductase subunit BPRO_1000048399Add
BLAST

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

STRINGi240292.Ava_3466.

Structurei

3D structure databases

ProteinModelPortaliQ3M7G3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni429 – 4302Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105EVY. Bacteria.
COG2710. LUCA.
HOGENOMiHOG000032963.
KOiK04039.
OMAiIPCAVIS.
OrthoDBiEOG6WX4K1.

Family and domain databases

HAMAPiMF_00353. ChlB_BchB.
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.

Q3M7G3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLAYWMYAG PAHIGTLRVA TSFKNVHAIM HAPLGDDYFN VMRSMLSRER
60 70 80 90 100
DFTPVTTSVV DRHVLARGSQ EKVVENITRK DAEEHPDLIV LTPTCTSSIL
110 120 130 140 150
QEDLENFVER AQLDAKGDVL LADVNHYRVN ELQAGDRTLH QIVQYYIEKA
160 170 180 190 200
RKKGELPEGK TAKPSVNIIG ISTLGFHNNH DCTELKRLMA DLGIEVNAVI
210 220 230 240 250
PEGASVHELK NLPRAWFNLV PYRELGLMTA SYLEKEFGTP CIDIVPMGVV
260 270 280 290 300
ETARCIRKIQ EVINAQGADV NYEEYINEQT LYVSQAAWFS RSIDCQNLTG
310 320 330 340 350
KKAVVFGDNT HAAALTKILS REMGIHVVWA GTYCKYDADW FREQVSEYCD
360 370 380 390 400
EVLITEDHGE IGDAIARVEP SAIFGTQMER HVGKRLDIPC GVIAAPIHVQ
410 420 430 440 450
NFPIGYKPFL GYEGTNQITD LIYNSFTLGM EDHLLEIFGG HDTKEVITKG
460 470 480 490 500
ISAESDLSWT KDGLAELNKI PGFVRGKVKR NTEKFARDRG FKDISAEVLY

AAKEAVGA
Length:508
Mass (Da):56,807
Last modified:October 25, 2005 - v1
Checksum:iED4DB6A0A6F069E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000117 Genomic DNA. Translation: ABA23073.1.

Genome annotation databases

EnsemblBacteriaiABA23073; ABA23073; Ava_3466.
KEGGiava:Ava_3466.
PATRICi35428035. VBIAnaVar43351_4550.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000117 Genomic DNA. Translation: ABA23073.1.

3D structure databases

ProteinModelPortaliQ3M7G3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi240292.Ava_3466.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA23073; ABA23073; Ava_3466.
KEGGiava:Ava_3466.
PATRICi35428035. VBIAnaVar43351_4550.

Phylogenomic databases

eggNOGiENOG4105EVY. Bacteria.
COG2710. LUCA.
HOGENOMiHOG000032963.
KOiK04039.
OMAiIPCAVIS.
OrthoDBiEOG6WX4K1.

Enzyme and pathway databases

UniPathwayiUPA00670.
BioCyciAVAR240292:GCY3-3512-MONOMER.

Family and domain databases

HAMAPiMF_00353. ChlB_BchB.
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...

Publicationsi

  1. "Complete sequence of Anabaena variabilis ATCC 29413."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29413 / PCC 7937.

Entry informationi

Entry nameiCHLB_ANAVT
AccessioniPrimary (citable) accession number: Q3M7G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2005
Last modified: November 11, 2015
This is version 68 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

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.