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 Q42368

Entry ID Method Resolution Chain Position Source
AF-Q42368-F1 Predicted AlphaFoldDB

12 variants for Q42368

Variant ID(s) Position Change Description Diseaes Association Provenance
PZE08105710899 17 G>S No EnsemblPlants
PZE08105711345 132 A>S No EnsemblPlants
PZE08105711976 176 L>V No EnsemblPlants
PZE08105712007 186 D>G No EnsemblPlants
PZE08105712013 188 K>R No EnsemblPlants
PZE08105712036 196 N>D No EnsemblPlants
PZE08105712592 313 K>Q No EnsemblPlants
PZE08105712606 317 E>D No EnsemblPlants
PZE08105713662 497 G>D No EnsemblPlants
PZE08105714267 585 A>T No EnsemblPlants
PZE08105714809 703 A>G No EnsemblPlants
PZE08105714808 703 A>T No EnsemblPlants

No associated diseases with Q42368

7 regional properties for Q42368

Type Name Position InterPro Accession
domain PEP-utilising enzyme, C-terminal 527 - 881 IPR000121
domain Pyruvate phosphate dikinase, AMP/ATP-binding 29 - 66 IPR002192-1
domain Pyruvate phosphate dikinase, AMP/ATP-binding 76 - 301 IPR002192-2
domain Pyruvate phosphate dikinase, AMP/ATP-binding 312 - 366 IPR002192-3
domain PEP-utilising enzyme, mobile domain 432 - 513 IPR008279
active_site PEP-utilising enzyme, active site 460 - 471 IPR018274
conserved_site PEP-utilising enzyme, conserved site 773 - 791 IPR023151

Functions

Description
EC Number 2.7.9.1 Phosphotransferases with paired acceptors
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
kinase activity Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
metal ion binding Binding to a metal ion.
pyruvate, phosphate dikinase activity Catalysis of the reaction: ATP + phosphate + pyruvate = AMP + diphosphate + 2 H(+) + phosphoenolpyruvate.

3 GO annotations of biological process

Name Definition
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
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.
pyruvate metabolic process The chemical reactions and pathways involving pyruvate, 2-oxopropanoate.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P11155 PPDK1 Pyruvate, phosphate dikinase 1, chloroplastic Zea mays (Maize) PR
Q6AVA8 PPDK1 Pyruvate, phosphate dikinase 1, chloroplastic Oryza sativa subsp japonica (Rice) PR
O23404 PPDK Pyruvate, phosphate dikinase 1, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAPAPCGRSS QRVFHFGKGK SEGNKNMKEL LGGKGANLAE MASIGLSVPP GFTVSTEACQ
70 80 90 100 110 120
QYQEAGRALP PGLWAEVLDG LRWVEEYMGA ALGDPRRPLL LSVRSGAAVS MPGMMDTVLN
130 140 150 160 170 180
LGLNDQVAAG LAAKSGDRFA YDSFRRFLDM FGNVVMDIPH ALFEEKLEAM KKAKGLKNDT
190 200 210 220 230 240
DLTATDLKEL VSQYKNVYVE AKGEPFPSDP KRQLELAVLA VFDSWESPRA KKYRSINQIT
250 260 270 280 290 300
GLRGTAVNVQ CMVFGNMGNT SGTGVLFTRN PNTGEKKLYG EFLVNAQGED VVAGIRTPED
310 320 330 340 350 360
LDAMKDVMPQ AYKELVENCR ILESHYKEMQ DIEFTVQESR LWMLQCRTGK RTGKSAVKIA
370 380 390 400 410 420
VDMVNEGLVE RRAAIKMVEP GHLDQLLHPQ FENPSAYKDQ VIATGLPASP GAAVGQVVFT
430 440 450 460 470 480
AEDAETWHSQ GKSVILVRAE TSPEDVGGMH AAAGILTERG GMTSHAAVVA RGWGKCCVSG
490 500 510 520 530 540
CSGIRVNDAE KVVKIGGNVL REGEWLSLNG STGEVILGKQ PLSPPALSGD LGTFMSWVDD
550 560 570 580 590 600
VRKLKVLANA DTPEDALAAR NNGAEGIGLC RTEHMFFASD ERIKAVRQMI MAPTVELRQQ
610 620 630 640 650 660
ALDRLLPYQR SDFEGIFRAM DGLSVTIRLL DPPLHEFLPE GNVEEIVREL CSETGANQED
670 680 690 700 710 720
ALARIEKLSE VNPMLGFRGC RLGISYPELT EMQARAIFEA AIAMTNQGVQ VFPEIMVPLV
730 740 750 760 770 780
GTPQELGHQV ALIRQVANKV FTSMGKTIGY KIGTMIEIPR AALVADEIAE QAEFFSFGTN
790 800 810 820 830 840
DLTQMTFGYS RDDVGKFIPI YLAQGILQHD PFEVLDQRGV GELVKLATER GRKARPNLKV
850 860 870 880
GICGEHGGEP SSVAFFAKTG LDYVSCSPFR VPIARLAAAQ VLV