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Protein

Magnesium-chelatase 38 kDa subunit

Gene

bchI

Organism
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathway: bacteriochlorophyll biosynthesis

This protein is involved in the pathway bacteriochlorophyll biosynthesis, which is part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the pathway bacteriochlorophyll biosynthesis and in Porphyrin-containing compound metabolism.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi52 – 598ATPSequence Analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Bacteriochlorophyll biosynthesis, Chlorophyll biosynthesis, Photosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciRCAP272942:GJIY-690-MONOMER.
BRENDAi6.6.1.1. 5381.
UniPathwayiUPA00669.

Names & Taxonomyi

Protein namesi
Recommended name:
Magnesium-chelatase 38 kDa subunit (EC:6.6.1.1)
Alternative name(s):
Mg-protoporphyrin IX chelatase
Gene namesi
Name:bchI
Ordered Locus Names:RCAP_rcc00677
OrganismiRhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Taxonomic identifieri272942 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
ProteomesiUP000002361 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Magnesium-chelatase 38 kDa subunitPRO_0000206859Add
BLAST

Interactioni

Protein-protein interaction databases

DIPiDIP-58976N.
IntActiP26239. 1 interaction.
MINTiMINT-7994720.
STRINGi272942.RCAP_rcc00677.

Structurei

Secondary structure

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 253Combined sources
Helixi30 – 4112Combined sources
Helixi43 – 453Combined sources
Beta strandi48 – 514Combined sources
Helixi54 – 563Combined sources
Helixi60 – 689Combined sources
Beta strandi72 – 754Combined sources
Helixi85 – 873Combined sources
Beta strandi99 – 1024Combined sources
Beta strandi106 – 1094Combined sources
Helixi115 – 1195Combined sources
Helixi124 – 1307Combined sources
Helixi132 – 1343Combined sources
Helixi139 – 1435Combined sources
Beta strandi146 – 1505Combined sources
Helixi153 – 1553Combined sources
Helixi158 – 17013Combined sources
Beta strandi171 – 1755Combined sources
Beta strandi182 – 1854Combined sources
Beta strandi188 – 1947Combined sources
Helixi203 – 2064Combined sources
Beta strandi210 – 2145Combined sources
Helixi221 – 23616Combined sources
Helixi238 – 26225Combined sources
Helixi263 – 2653Combined sources
Helixi270 – 28213Combined sources
Beta strandi283 – 2853Combined sources
Helixi288 – 30417Combined sources
Helixi312 – 32312Combined sources
Helixi324 – 3263Combined sources
Helixi342 – 3487Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G8PX-ray2.10A1-350[»]
2X31electron microscopy7.50G/H/I/J/K/L1-350[»]
ProteinModelPortaliP26239.
SMRiP26239. Positions 18-350.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26239.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000225091.
KOiK03405.
OMAiAVIGQEE.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR011775. Mg_chelatase_ATPase-isu.
IPR000523. Mg_chelatse_chII.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01078. Mg_chelatase. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR02030. BchI-ChlI. 1 hit.

Sequencei

Sequence statusi: Complete.

P26239-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTAVARLQP SASGAKTRPV FPFSAIVGQE DMKLALLLTA VDPGIGGVLV
60 70 80 90 100
FGDRGTGKST AVRALAALLP EIEAVEGCPV SSPNVEMIPD WATVLSTNVI
110 120 130 140 150
RKPTPVVDLP LGVSEDRVVG ALDIERAISK GEKAFEPGLL ARANRGYLYI
160 170 180 190 200
DECNLLEDHI VDLLLDVAQS GENVVERDGL SIRHPARFVL VGSGNPEEGD
210 220 230 240 250
LRPQLLDRFG LSVEVLSPRD VETRVEVIRR RDTYDADPKA FLEEWRPKDM
260 270 280 290 300
DIRNQILEAR ERLPKVEAPN TALYDCAALC IALGSDGLRG ELTLLRSARA
310 320 330 340 350
LAALEGATAV GRDHLKRVAT MALSHRLRRD PLDEAGSTAR VARTVEETLP
Length:350
Mass (Da):37,899
Last modified:May 1, 1992 - v1
Checksum:i5CBAA54A1F308568
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11165 Genomic DNA. Translation: CAA77538.1.
CP001312 Genomic DNA. Translation: ADE84442.1.
RefSeqiWP_013066421.1. NC_014034.1.
YP_003576849.1. NC_014034.1.

Genome annotation databases

EnsemblBacteriaiADE84442; ADE84442; RCAP_rcc00677.
KEGGircp:RCAP_rcc00677.
PATRICi35501422. VBIRhoCap134200_0688.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11165 Genomic DNA. Translation: CAA77538.1.
CP001312 Genomic DNA. Translation: ADE84442.1.
RefSeqiWP_013066421.1. NC_014034.1.
YP_003576849.1. NC_014034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G8PX-ray2.10A1-350[»]
2X31electron microscopy7.50G/H/I/J/K/L1-350[»]
ProteinModelPortaliP26239.
SMRiP26239. Positions 18-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58976N.
IntActiP26239. 1 interaction.
MINTiMINT-7994720.
STRINGi272942.RCAP_rcc00677.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADE84442; ADE84442; RCAP_rcc00677.
KEGGircp:RCAP_rcc00677.
PATRICi35501422. VBIRhoCap134200_0688.

Phylogenomic databases

HOGENOMiHOG000225091.
KOiK03405.
OMAiAVIGQEE.

Enzyme and pathway databases

UniPathwayiUPA00669.
BioCyciRCAP272942:GJIY-690-MONOMER.
BRENDAi6.6.1.1. 5381.

Miscellaneous databases

EvolutionaryTraceiP26239.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR011775. Mg_chelatase_ATPase-isu.
IPR000523. Mg_chelatse_chII.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01078. Mg_chelatase. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR02030. BchI-ChlI. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiBCHI_RHOCB
AccessioniPrimary (citable) accession number: P26239
Secondary accession number(s): D5ANT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 24, 2015
This is version 93 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

External Data

Dasty 3

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 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.