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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: -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: 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)DescriptionActionsGraphical viewLength
Nucleotide bindingi52 – 59ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processBacteriochlorophyll biosynthesis, Chlorophyll biosynthesis, Photosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciRCAP272942:G1GUE-681-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
Proteomesi
  • UP000002361 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002068591 – 350Magnesium-chelatase 38 kDa subunitAdd BLAST350

Proteomic databases

PRIDEiP26239

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
bchDP261755EBI-8453273,EBI-8453255

Protein-protein interaction databases

DIPiDIP-58976N
IntActiP26239, 1 interactor
MINTiP26239
STRINGi272942.RCAP_rcc00677

Structurei

Secondary structure

1350
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi23 – 25Combined sources3
Helixi30 – 41Combined sources12
Helixi43 – 45Combined sources3
Beta strandi48 – 51Combined sources4
Helixi54 – 56Combined sources3
Helixi60 – 68Combined sources9
Beta strandi72 – 75Combined sources4
Helixi85 – 87Combined sources3
Beta strandi99 – 102Combined sources4
Beta strandi106 – 109Combined sources4
Helixi115 – 119Combined sources5
Helixi124 – 130Combined sources7
Helixi132 – 134Combined sources3
Helixi139 – 143Combined sources5
Beta strandi146 – 150Combined sources5
Helixi153 – 155Combined sources3
Helixi158 – 170Combined sources13
Beta strandi171 – 175Combined sources5
Beta strandi182 – 185Combined sources4
Beta strandi188 – 194Combined sources7
Helixi203 – 206Combined sources4
Beta strandi210 – 214Combined sources5
Helixi221 – 236Combined sources16
Helixi238 – 262Combined sources25
Helixi263 – 265Combined sources3
Helixi270 – 282Combined sources13
Beta strandi283 – 285Combined sources3
Helixi288 – 304Combined sources17
Helixi312 – 323Combined sources12
Helixi324 – 326Combined sources3
Helixi342 – 348Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP26239

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105EET Bacteria
COG1239 LUCA
HOGENOMiHOG000225091
KOiK03405
OMAiHRGELTI
OrthoDBiPOG091H09MB

Family and domain databases

InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR011775 Mg_chelatase_ATPase-isu
IPR000523 Mg_chelatse_chII_dom
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF01078 Mg_chelatase, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
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

Genome annotation databases

EnsemblBacteriaiADE84442; ADE84442; RCAP_rcc00677
GeneIDi31489623
KEGGircp:RCAP_rcc00677

Similar proteinsi

Entry informationi

Entry nameiBCHI_RHOCB
AccessioniPrimary (citable) accession number: P26239
Secondary accession number(s): D5ANT8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: May 23, 2018
This is version 107 of the entry and version 1 of the sequence. See 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

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