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P26239 (BCHI_RHOCB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. 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:
Magnesium-chelatase 38 kDa subunit

EC=6.6.1.1
Alternative name(s):
Mg-protoporphyrin IX chelatase
Gene names
Name:bchI
Ordered Locus Names:RCAP_rcc00677
OrganismRhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) [Complete proteome] [HAMAP]
Taxonomic identifier272942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in bacteriochlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.

Catalytic activity

ATP + protoporphyrin IX + Mg2+ + H2O = ADP + phosphate + Mg-protoporphyrin IX + 2 H+.

Pathway

Porphyrin-containing compound metabolism; bacteriochlorophyll biosynthesis.

Sequence similarities

Belongs to the Mg-chelatase subunits D/I family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350Magnesium-chelatase 38 kDa subunit
PRO_0000206859

Regions

Nucleotide binding52 – 598ATP Potential

Secondary structure

........................................................... 350
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26239 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 5CBAA54A1F308568

FASTA35037,899
        10         20         30         40         50         60 
MTTAVARLQP SASGAKTRPV FPFSAIVGQE DMKLALLLTA VDPGIGGVLV FGDRGTGKST 

        70         80         90        100        110        120 
AVRALAALLP EIEAVEGCPV SSPNVEMIPD WATVLSTNVI RKPTPVVDLP LGVSEDRVVG 

       130        140        150        160        170        180 
ALDIERAISK GEKAFEPGLL ARANRGYLYI DECNLLEDHI VDLLLDVAQS GENVVERDGL 

       190        200        210        220        230        240 
SIRHPARFVL VGSGNPEEGD LRPQLLDRFG LSVEVLSPRD VETRVEVIRR RDTYDADPKA 

       250        260        270        280        290        300 
FLEEWRPKDM DIRNQILEAR ERLPKVEAPN TALYDCAALC IALGSDGLRG ELTLLRSARA 

       310        320        330        340        350 
LAALEGATAV GRDHLKRVAT MALSHRLRRD PLDEAGSTAR VARTVEETLP 

« Hide

References

« Hide 'large scale' references
[1]Burke D.H., Alberti M., Armstrong G.A., Hearst J.E.
Submitted (NOV-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
[2]"Nucleotide sequence, organization, and nature of the protein products of the carotenoid biosynthesis gene cluster of Rhodobacter capsulatus."
Armstrong G.A., Alberti M., Leach F., Hearst J.E.
Mol. Gen. Genet. 216:254-268(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
[3]"Complete genome sequence of the photosynthetic purple nonsulfur bacterium Rhodobacter capsulatus SB 1003."
Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., Haselkorn R.
J. Bacteriol. 192:3545-3546(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11165 Genomic DNA. Translation: CAA77538.1.
CP001312 Genomic DNA. Translation: ADE84442.1.
RefSeqYP_003576849.1. NC_014034.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G8PX-ray2.10A1-350[»]
2X31electron microscopy7.50G/H/I/J/K/L1-350[»]
ProteinModelPortalP26239.
SMRP26239. Positions 18-350.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-58976N.
IntActP26239. 1 interaction.
MINTMINT-7994720.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE84442; ADE84442; RCAP_rcc00677.
GeneID9003506.
KEGGrcp:RCAP_rcc00677.
PATRIC35501422. VBIRhoCap134200_0688.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000225091.
KOK03405.
OMAATEDRLC.

Enzyme and pathway databases

BioCycRCAP272942:GJIY-690-MONOMER.
UniPathwayUPA00669.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR011775. Mg_chelatase_ATPase-isu.
IPR000523. Mg_chelatse_chII.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF01078. Mg_chelatase. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR02030. BchI-ChlI. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP26239.

Entry information

Entry nameBCHI_RHOCB
AccessionPrimary (citable) accession number: P26239
Secondary accession number(s): D5ANT8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 84 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