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P26239

- BCHI_RHOCB

UniProt

P26239 - BCHI_RHOCB

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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: 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+.

Pathwayi

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium chelatase activity Source: UniProtKB-EC

GO - Biological processi

  1. bacteriochlorophyll biosynthetic process Source: UniProtKB-UniPathway
  2. photosynthesis Source: UniProtKB-KW
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.
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: 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.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiAVVGCPY.

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:
EMBL
GenBank
DDBJ
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.
GeneIDi9003506.
KEGGircp:RCAP_rcc00677.
PATRICi35501422. VBIRhoCap134200_0688.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11165 Genomic DNA. Translation: CAA77538.1 .
CP001312 Genomic DNA. Translation: ADE84442.1 .
RefSeqi WP_013066421.1. NC_014034.1.
YP_003576849.1. NC_014034.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G8P X-ray 2.10 A 1-350 [» ]
2X31 electron microscopy 7.50 G/H/I/J/K/L 1-350 [» ]
ProteinModelPortali P26239.
SMRi P26239. Positions 18-350.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-58976N.
IntActi P26239. 1 interaction.
MINTi MINT-7994720.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADE84442 ; ADE84442 ; RCAP_rcc00677 .
GeneIDi 9003506.
KEGGi rcp:RCAP_rcc00677.
PATRICi 35501422. VBIRhoCap134200_0688.

Phylogenomic databases

HOGENOMi HOG000225091.
KOi K03405.
OMAi AVVGCPY.

Enzyme and pathway databases

UniPathwayi UPA00669 .
BioCyci RCAP272942:GJIY-690-MONOMER.

Miscellaneous databases

EvolutionaryTracei P26239.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR003593. AAA+_ATPase.
IPR011775. Mg_chelatase_ATPase-isu.
IPR000523. Mg_chelatse_chII.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF01078. Mg_chelatase. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR02030. BchI-ChlI. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 88 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