Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P16127

Entry ID Method Resolution Chain Position Source
AF-P16127-F1 Predicted AlphaFoldDB

15 variants for P16127

Variant ID(s) Position Change Description Diseaes Association Provenance
ENSVATH02874508 16 P>H No 1000Genomes
ENSVATH14247299 20 S>F No 1000Genomes
ENSVATH02874507 29 P>S No 1000Genomes
ENSVATH06715951 35 G>E No 1000Genomes
ENSVATH06715950 39 G>R No 1000Genomes
ENSVATH06715949 52 K>N No 1000Genomes
tmp_4_10203124_T_A 53 N>Y No 1000Genomes
tmp_4_10203109_G_A 58 H>Y No 1000Genomes
tmp_4_10203102_G_A 60 S>L No 1000Genomes
ENSVATH02874502 83 S>N No 1000Genomes
tmp_4_10202697_C_G 159 V>L No 1000Genomes
tmp_4_10202210_G_A 321 T>I No 1000Genomes
ENSVATH06715941 325 K>Q No 1000Genomes
tmp_4_10202000_G_A 391 T>I No 1000Genomes
tmp_4_10201967_C_T 402 R>K No 1000Genomes

No associated diseases with P16127

3 regional properties for P16127

Type Name Position InterPro Accession
domain Magnesium chelatase ChlI-like, catalytic domain 200 - 270 IPR000523
domain AAA+ ATPase domain 111 - 293 IPR003593
domain ChlI/MoxR, AAA lid domain 350 - 408 IPR041628

Functions

Description
EC Number 6.6.1.1 Forming coordination complexes
Subcellular Localization
  • Plastid, chloroplast
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
chloroplast A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
chloroplast stroma The space enclosed by the double membrane of a chloroplast but excluding the thylakoid space. It contains DNA, ribosomes and some temporary products of photosynthesis.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
magnesium chelatase complex A heterotrimeric enzyme complex composed of three subunits, all of which are required for enzyme activity, which catalyzes the chelation of Mg by proto IX in an ATP-dependent manner.
plant-type cell wall A more or less rigid stucture lying outside the cell membrane of a cell and composed of cellulose and pectin and other organic and inorganic substances.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
magnesium chelatase activity Catalysis of the reaction: ATP + H2O + Mg2+ + protoporphyrin IX = ADP + 3 H+ + Mg-protoporphyrin IX + phosphate.

2 GO annotations of biological process

Name Definition
chlorophyll biosynthetic process The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors.
photosynthesis The synthesis by organisms of organic chemical compounds, especially carbohydrates, from carbon dioxide (CO2) using energy obtained from light rather than from the oxidation of chemical compounds.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q53RM0 CHLI Magnesium-chelatase subunit ChlI, chloroplastic Oryza sativa subsp japonica (Rice) PR
Q5XF33 CHLI2 Magnesium-chelatase subunit ChlI-2, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MASLLGTSSS AIWASPSLSS PSSKPSSSPI CFRPGKLFGS KLNAGIQIRP KKNRSRYHVS
70 80 90 100 110 120
VMNVATEINS TEQVVGKFDS KKSARPVYPF AAIVGQDEMK LCLLLNVIDP KIGGVMIMGD
130 140 150 160 170 180
RGTGKSTTVR SLVDLLPEIN VVAGDPYNSD PIDPEFMGVE VRERVEKGEQ VPVIATKINM
190 200 210 220 230 240
VDLPLGATED RVCGTIDIEK ALTEGVKAFE PGLLAKANRG ILYVDEVNLL DDHLVDVLLD
250 260 270 280 290 300
SAASGWNTVE REGISISHPA RFILIGSGNP EEGELRPQLL DRFGMHAQVG TVRDADLRVK
310 320 330 340 350 360
IVEERARFDS NPKDFRDTYK TEQDKLQDQI STARANLSSV QIDRELKVKI SRVCSELNVD
370 380 390 400 410 420
GLRGDIVTNR AAKALAALKG KDRVTPDDVA TVIPNCLRHR LRKDPLESID SGVLVSEKFA
EIFS