Q39735

PR
Gene name
Protein name
Pyruvate, phosphate dikinase, chloroplastic
Names
Cold-sensitive pyruvate, orthophosphate dikinase, Pyruvate, orthophosphate dikinase
Species
Flaveria bidentis (Coastal plain yellowtops) (Ethulia bidentis)
KEGG Pathway
EC number
2.7.9.1: Phosphotransferases with paired acceptors
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-120 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q39735

Entry ID Method Resolution Chain Position Source
AF-Q39735-F1 Predicted AlphaFoldDB

No variants for Q39735

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q39735

No associated diseases with Q39735

6 regional properties for Q39735

Type Name Position InterPro Accession
domain PEP-utilising enzyme, C-terminal 598 - 951 IPR000121
domain Pyruvate phosphate dikinase, AMP/ATP-binding 145 - 370 IPR002192-1
domain Pyruvate phosphate dikinase, AMP/ATP-binding 382 - 435 IPR002192-2
domain PEP-utilising enzyme, mobile domain 502 - 583 IPR008279
active_site PEP-utilising enzyme, active site 530 - 541 IPR018274
conserved_site PEP-utilising enzyme, conserved site 843 - 861 IPR023151

Functions

Description
EC Number 2.7.9.1 Phosphotransferases with paired acceptors
Subcellular Localization
  • Plastid, chloroplast
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MMSSLSVEGM LLKSARESCL PARVNQRRNG DLRRLNHHRQ SSFVRCLTPA RVSRPELRSS
70 80 90 100 110 120
GLTPPRAVLN PVSPPVTTAK KRVFTFGKGR SEGNRDMKSL LGGKGANLAE MSSIGLSVPP
130 140 150 160 170 180
GLTISTEACE EYQQNGKSLP PGLWDEISEG LDYVQKEMSA SLGDPSKPLP LSVRSGAAIS
190 200 210 220 230 240
MPGMMDTVLN LGLNDEVVAG LAGKSGARFA YDSYRRFLDM FGNVVMGIPH SLFDEKLEQM
250 260 270 280 290 300
KAEKGIHLDT DLTAADLKDL VEKYKNVYVE AKGEKFPTDP KKQLELAVNA VFDSWDSPRA
310 320 330 340 350 360
NKYRSINQIT GLKGTAVNIQ SMVFGNMGNT SGTGVLFTRN PSTGEKKLYG EFLINAQGED
370 380 390 400 410 420
VVAGIRTPED LGTMETCMPD AYKELVENCE ILEGHYKDMM DIEFTVQENR LWMLQCRTGK
430 440 450 460 470 480
RTGKGAVRIA VDMVNEWLID TRTAIKRVET QHLDQLLHPQ FEDPSAYKSH VVATGLPASP
490 500 510 520 530 540
GAAVGQVCFS AEDAETWHAQ GKSAILVRTE TSPEDVGGMH AAAGILTARG GMTSHAAVVA
550 560 570 580 590 600
RGWGKCCVSG CADIRVNDDM KIFTIGDRVI KEGDWLSLNG TTGEVILGKQ LLAPPAMSND
610 620 630 640 650 660
LEIFMSWADQ ARRLKVMANA DTPNDALTAR NNGAQGIGLC RTEHMFFASD ERIKAVRKMI
670 680 690 700 710 720
MAVTPEQRKV ALDLLLPYQR SDFEGIFRAM DGLPVTIRLL DPPLHEFLPE GDLEHIVNEL
730 740 750 760 770 780
AVDTGMSADE IYSKIENLSE VNPMLGFRGC RLGISYPELT EMQVRAIFQA AVSMTNQGVT
790 800 810 820 830 840
VIPEIMVPLV GTPQELRHQI SVIRGVAANV FAEMGVTLEY KVGTMIEIPR AALIAEEIGK
850 860 870 880 890 900
EADFFSFGTN DLTQMTFGYS RDDVGKFLQI YLAQGILQHD PFEVIDQKGV GQLIKMATEK
910 920 930 940 950
GRAANPNLKV GICGEHGGEP SSVAFFDGVG LDYVSCSPFR VPIARLAAAQ VIV