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

3 structures for P11155

Entry ID Method Resolution Chain Position Source
1VBG X-ray 230 A A 72-947 PDB
1VBH X-ray 230 A A 72-947 PDB
AF-P11155-F1 Predicted AlphaFoldDB

No variants for P11155

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P11155

No associated diseases with P11155

7 regional properties for P11155

Type Name Position InterPro Accession
domain PEP-utilising enzyme, C-terminal 591 - 945 IPR000121
domain Pyruvate phosphate dikinase, AMP/ATP-binding 93 - 128 IPR002192-1
domain Pyruvate phosphate dikinase, AMP/ATP-binding 139 - 365 IPR002192-2
domain Pyruvate phosphate dikinase, AMP/ATP-binding 374 - 430 IPR002192-3
domain PEP-utilising enzyme, mobile domain 497 - 577 IPR008279
active_site PEP-utilising enzyme, active site 524 - 535 IPR018274
conserved_site PEP-utilising enzyme, conserved site 837 - 855 IPR023151

Functions

Description
EC Number 2.7.9.1 Phosphotransferases with paired acceptors
Subcellular Localization
  • Plastid, chloroplast
  • Cytoplasm
  • Isoform C4PPDKZM1 is targeted to the chloroplast while isoform CYPPDKZM1 is found in the cytoplasm
  • Can be found associated with the thylakoid membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 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.

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
Q42368 PPDK2 Pyruvate, phosphate dikinase 2 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
MAASVSRAIC VQKPGSKCTR DREATSFARR SVAAPRPPHA KAAGVIRSDS GAGRGQHCSP
70 80 90 100 110 120
LRAVVDAAPI QTTKKRVFHF GKGKSEGNKT MKELLGGKGA NLAEMASIGL SVPPGFTVST
130 140 150 160 170 180
EACQQYQDAG CALPAGLWAE IVDGLQWVEE YMGATLGDPQ RPLLLSVRSG AAVSMPGMMD
190 200 210 220 230 240
TVLNLGLNDE VAAGLAAKSG ERFAYDSFRR FLDMFGNVVM DIPRSLFEEK LEHMKESKGL
250 260 270 280 290 300
KNDTDLTASD LKELVGQYKE VYLSAKGEPF PSDPKKQLEL AVLAVFNSWE SPRAKKYRSI
310 320 330 340 350 360
NQITGLRGTA VNVQCMVFGN MGNTSGTGVL FTRNPNTGEK KLYGEFLVNA QGEDVVAGIR
370 380 390 400 410 420
TPEDLDAMKN LMPQAYDELV ENCNILESHY KEMQDIEFTV QENRLWMLQC RTGKRTGKSA
430 440 450 460 470 480
VKIAVDMVNE GLVEPRSAIK MVEPGHLDQL LHPQFENPSA YKDQVIATGL PASPGAAVGQ
490 500 510 520 530 540
VVFTAEDAEA WHSQGKAAIL VRAETSPEDV GGMHAAVGIL TERGGMTSHA AVVARWWGKC
550 560 570 580 590 600
CVSGCSGIRV NDAEKLVTIG SHVLREGEWL SLNGSTGEVI LGKQPLSPPA LSGDLGTFMA
610 620 630 640 650 660
WVDDVRKLKV LANADTPDDA LTARNNGAQG IGLCRTEHMF FASDERIKAV RQMIMAPTLE
670 680 690 700 710 720
LRQQALDRLL TYQRSDFEGI FRAMDGLPVT IRLLDHPSYE FLPEGNIEDI VSELCAETGA
730 740 750 760 770 780
NQEDALARIE KLSEVNPMLG FRGCRLGISY PELTEMQARA IFEAAIAMTN QGVQVFPEIM
790 800 810 820 830 840
VPLVGTPQEL GHQVTLIRQV AEKVFANVGK TIGYKVGTMI EIPRAALVAD EIAEQAEFFS
850 860 870 880 890 900
FGTNDLTQMT FGYSRDDVGK FIPVHLAQGI LQHDPFEVLD QRGVGELVKF ATERGRKARP
910 920 930 940
NLKVGICGEH GGEPSSVAFF AKAGLDFVSC SPFRVPIARL AAAQVLV