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Q7VD38 (CHLB_PROMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Light-independent protochlorophyllide reductase subunit B

Short name=DPOR subunit B
Short name=LI-POR subunit B
EC=1.3.7.7
Gene names
Name:chlB
Ordered Locus Names:Pro_0545
OrganismProchlorococcus marinus (strain SARG / CCMP1375 / SS120) [Reference proteome] [HAMAP]
Taxonomic identifier167539 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00353

Catalytic activity

Protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O = chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate. HAMAP-Rule MF_00353

Cofactor

Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits By similarity.

Pathway

Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent). HAMAP-Rule MF_00353

Subunit structure

Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN subunits By similarity.

Sequence similarities

Belongs to the ChlB/BchB/BchZ family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 530530Light-independent protochlorophyllide reductase subunit B HAMAP-Rule MF_00353
PRO_1000048411

Regions

Region425 – 4262Substrate binding By similarity

Sites

Active site2901Proton donor By similarity
Metal binding361Iron-sulfur (4Fe-4S); shared with heterodimeric partner By similarity

Secondary structure

....................................................................................... 530
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7VD38 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 7D5A10C8B8D0FF2E

FASTA53058,729
        10         20         30         40         50         60 
MELTLWTYEG PPHIGAMRIA TSMKGLHYVL HAPQGDTYAD LLFTMIERRG SRPPVTYTTF 

        70         80         90        100        110        120 
QARDLGGDTA ELVKGHIFEA VERFKPEALL VGESCTAELI QDQPGSLAKG MGLNIPIVSL 

       130        140        150        160        170        180 
ELPAYSKKEN WGASETFYQL IRGLLKEISE DSSNNAKQSW QEEGRRPRVN LLGPSLLGFR 

       190        200        210        220        230        240 
CRDDVLEIQK ILGENGIDIN VIAPLGASPS DLMRLPKADA NVCLYPEIAE STCLWLERNF 

       250        260        270        280        290        300 
KTPFTKVVPI GVKATQDFLE ELYELLGMEV SNSISNSDQS KLPWYSKSVD SNYLTGKRVF 

       310        320        330        340        350        360 
IFGDGTHVLA AARIANEELG FEVVGIGTYS REMARKVRAA ATELGLEALI TNDYLEVEES 

       370        380        390        400        410        420 
IKECAPELVL GTQMERHSAK RLGIPCAVIS TPMHVQDVPA RYSPQMGWEG ANVIFDDWVH 

       430        440        450        460        470        480 
PLMMGLEEHL IGMFRHDFEF TDGHQSHLGH LGGHASETKT SSKGINQSPN NHSPAGESIH 

       490        500        510        520        530 
WTSEGESELA KIPFFVRGKV RRNTEKYARQ AGCREIDGET LLDAKAHFGA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017126 Genomic DNA. Translation: AAP99590.1.
RefSeqNP_874938.1. NC_005042.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YNMX-ray2.10D1-530[»]
ProteinModelPortalQ7VD38.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167539.Pro0545.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP99590; AAP99590; Pro_0545.
GeneID1461927.
KEGGpma:Pro_0545.
PATRIC23027723. VBIProMar8617_0560.

Phylogenomic databases

eggNOGCOG2710.
KOK04039.
OMATQMERHS.
OrthoDBEOG6WX4K1.
ProtClustDBPRK02910.

Enzyme and pathway databases

BioCycPMAR167539:GJN2-563-MONOMER.
UniPathwayUPA00670.

Family and domain databases

HAMAPMF_00353. ChlB_BchB.
InterProIPR000510. Nase/OxRdtase_comp1.
IPR013580. P-CP/CP_red_C.
IPR005969. Protochl_reductB.
IPR016209. Protochlorophyllide_Rdtase.
[Graphical view]
PfamPF00148. Oxidored_nitro. 1 hit.
PF08369. PCP_red. 1 hit.
[Graphical view]
PIRSFPIRSF000163. PCP_ChlB. 1 hit.
TIGRFAMsTIGR01278. DPOR_BchB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCHLB_PROMA
AccessionPrimary (citable) accession number: Q7VD38
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways