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Protein

Magnesium-chelatase subunit ChlI-1, chloroplastic

Gene

CHLI1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. The magnesium-chelatase is a complex of three subunits, CHLI, CHLD and CHLH. The reaction takes place in two steps, with an ATP-dependent activation followed by an ATP-dependent chelation step. Possesses high affinity for ATP and may play a major role in chlorophyll biosynthesis. Does not bind abscisic acid (ABA), but is a positive regulator of ABA signaling.5 Publications

Catalytic activityi

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

Enzyme regulationi

Redox regulation; active in reducing conditions, inactive in oxidizing conditions. Thioredoxins f and m mediate the reversible reductive activation of oxidized CHLI1.1 Publication

Kineticsi

  1. KM=460 µM for ATP1 Publication
  1. Vmax=55 nmol/min/mg enzyme toward ATP1 Publication

Pathwayi: chlorophyll biosynthesis

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi119 – 126ATPSequence analysis8

GO - Molecular functioni

  • ATPase activity Source: TAIR
  • ATP binding Source: UniProtKB-KW
  • magnesium chelatase activity Source: TAIR

GO - Biological processi

  • chlorophyll biosynthetic process Source: TAIR
  • photosynthesis Source: UniProtKB-KW
  • response to cytokinin Source: TAIR

Keywordsi

Molecular functionLigase
Biological processChlorophyll biosynthesis, Photosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G18480-MONOMER
MetaCyc:MONOMER1F-75
UniPathwayiUPA00668

Names & Taxonomyi

Protein namesi
Recommended name:
Magnesium-chelatase subunit ChlI-1, chloroplastic (EC:6.6.1.1)
Short name:
Mg-chelatase subunit I-1
Alternative name(s):
Mg-protoporphyrin IX chelatase subunit ChlI-1
Protein CHLORINA 42
Gene namesi
Name:CHLI1
Synonyms:CH42, CS
Ordered Locus Names:At4g18480
ORF Names:F28J12.140
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

AraportiAT4G18480
TAIRilocus:2005500 AT4G18480

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Homozygous mutants are chlorotic lethal when grown on soil, but can grow on sucrose-containing medium.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi102C → S: Reduces ATPase activity 2-fold. 1 Publication1
Mutagenesisi193C → S: Reduces ATPase activity 2-fold. 1 Publication1
Mutagenesisi240D → N in aci5-3; white and inviable plants. Resistance to the herbicide acifluorfen when grown on sucrose-containing medium. 1 Publication1
Mutagenesisi354C → S: Reduces ATPase activity 5-fold. 1 Publication1
Mutagenesisi396C → S: Reduces ATPase activity 5-fold. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 60ChloroplastSequence analysisCombined sourcesAdd BLAST60
ChainiPRO_000000280161 – 424Magnesium-chelatase subunit ChlI-1, chloroplasticAdd BLAST364

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei61N-acetylvalineCombined sources1
Disulfide bondi102 ↔ 1931 Publication
Disulfide bondi354 ↔ 396Inhibitory under oxidizing conditions1 Publication
Modified residuei355PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP16127
PRIDEiP16127

2D gel databases

SWISS-2DPAGEiP16127

PTM databases

iPTMnetiP16127

Expressioni

Inductioni

Not regulated by light.1 Publication

Gene expression databases

ExpressionAtlasiP16127 baseline and differential
GenevisibleiP16127 AT

Interactioni

Subunit structurei

The magnesium chelatase complex is a heterotrimer consisting of subunits CHLI, CHLD, AND CHLH. Interacts with CHLH and CHLD.1 Publication

Protein-protein interaction databases

BioGridi12873, 1 interactor
IntActiP16127, 1 interactor
STRINGi3702.AT4G18480.1

Structurei

3D structure databases

ProteinModelPortaliP16127
SMRiP16127
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IESJ Eukaryota
COG1239 LUCA
HOGENOMiHOG000225091
InParanoidiP16127
KOiK03405
OMAiVMERRFA
OrthoDBiEOG09360D7Y
PhylomeDBiP16127

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16127-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLLGTSSS AIWASPSLSS PSSKPSSSPI CFRPGKLFGS KLNAGIQIRP
60 70 80 90 100
KKNRSRYHVS VMNVATEINS TEQVVGKFDS KKSARPVYPF AAIVGQDEMK
110 120 130 140 150
LCLLLNVIDP KIGGVMIMGD RGTGKSTTVR SLVDLLPEIN VVAGDPYNSD
160 170 180 190 200
PIDPEFMGVE VRERVEKGEQ VPVIATKINM VDLPLGATED RVCGTIDIEK
210 220 230 240 250
ALTEGVKAFE PGLLAKANRG ILYVDEVNLL DDHLVDVLLD SAASGWNTVE
260 270 280 290 300
REGISISHPA RFILIGSGNP EEGELRPQLL DRFGMHAQVG TVRDADLRVK
310 320 330 340 350
IVEERARFDS NPKDFRDTYK TEQDKLQDQI STARANLSSV QIDRELKVKI
360 370 380 390 400
SRVCSELNVD GLRGDIVTNR AAKALAALKG KDRVTPDDVA TVIPNCLRHR
410 420
LRKDPLESID SGVLVSEKFA EIFS
Length:424
Mass (Da):46,270
Last modified:April 1, 1990 - v1
Checksum:i30075DBBC31330DE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51799 Genomic DNA Translation: CAB38561.1
X91411 Genomic DNA Translation: CAA62754.1
AL021710 Genomic DNA Translation: CAA16728.1
AL161548 Genomic DNA Translation: CAB78850.1
CP002687 Genomic DNA Translation: AEE84051.1
AY093192 mRNA Translation: AAM13191.1
BT010129 mRNA Translation: AAQ22598.1
AK227146 mRNA Translation: BAE99191.1
PIRiS12785
RefSeqiNP_193583.1, NM_117962.3
UniGeneiAt.27665

Genome annotation databases

EnsemblPlantsiAT4G18480.1; AT4G18480.1; AT4G18480
GeneIDi827580
GrameneiAT4G18480.1; AT4G18480.1; AT4G18480
KEGGiath:AT4G18480

Similar proteinsi

Entry informationi

Entry nameiCHLI1_ARATH
AccessioniPrimary (citable) accession number: P16127
Secondary accession number(s): Q0WUK7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 25, 2018
This is version 149 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health