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Protein

Pyruvate, phosphate dikinase 1, chloroplastic

Gene

PPDK1

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Formation of phosphoenolpyruvate, which is the primary acceptor of CO2 in C4 and some Crassulacean acid metabolism plants.2 Publications

Catalytic activityi

ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate.3 Publications

Cofactori

Mg2+1 Publication1 Publication

Enzyme regulationi

Activated by light-induced dephosphorylation. Inhibited by dark-induced phosphorylation. Both reactions are catalyzed by PDRP1. Inactivated by cold due to the dissociation of the homotetramer. Independent of circadian regulation (PubMed:24710069).4 Publications

Kineticsi

  1. KM=158 µM for pyruvate1 Publication
  2. KM=178 µM for pyruvate1 Publication
  3. KM=95 µM for ATP1 Publication
  4. KM=194 µM for phosphoenolpyruvate1 Publication
  5. KM=408 µM for phosphate1 Publication

    Temperature dependencei

    Loss of activity below 10 degrees Celsius.1 Publication

    Pathwayi: C4 acid pathway

    This protein is involved in the pathway C4 acid pathway, which is part of Photosynthesis.
    View all proteins of this organism that are known to be involved in the pathway C4 acid pathway and in Photosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei529 – 5291Tele-phosphohistidine intermediate1 Publication
    Binding sitei635 – 6351Substrate1 Publication
    Binding sitei692 – 6921Substrate1 Publication
    Metal bindingi821 – 8211Magnesium1 Publication
    Binding sitei821 – 8211Substrate1 Publication
    Binding sitei842 – 8421Substrate; via carbonyl oxygen1 Publication
    Binding sitei843 – 8431Substrate; via amide nitrogen1 Publication
    Binding sitei844 – 8441Substrate1 Publication
    Metal bindingi845 – 8451Magnesium1 Publication
    Binding sitei845 – 8451Substrate; via amide nitrogen1 Publication
    Active sitei907 – 9071Proton donor1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Photosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.9.1. 6752.
    SABIO-RKP11155.
    UniPathwayiUPA00322.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate, phosphate dikinase 1, chloroplastic1 Publication (EC:2.7.9.14 Publications)
    Alternative name(s):
    Pyruvate, orthophosphate dikinase 1
    Gene namesi
    Name:PPDK11 Publication
    Synonyms:C4PPDKZM11 Publication, CYPPDKZM11 Publication, PPDK21 Publication
    OrganismiZea mays (Maize)
    Taxonomic identifieri4577 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
    Proteomesi
    • UP000007305 Componenti: Unplaced

    Organism-specific databases

    MaizeGDBi25385.

    Subcellular locationi

    • Plastidchloroplast 2 Publications
    • Cytoplasm 1 Publication

    • Note: Isoform C4PPDKZM1 is targeted to the chloroplast while isoform CYPPDKZM1 is found in the cytoplasm. Can be found associated with the thylakoid membrane.

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Cytoplasm, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi525 – 5251G → A or P: Greatly reduced activity. Strongly reduced or lack of phosphorylation by PDRP1 in vitro. 1 Publication
    Mutagenesisi527 – 5271T → D or E: Abolished activity. 2 Publications
    Mutagenesisi527 – 5271T → N: Greatly reduced activity. 2 Publications
    Mutagenesisi527 – 5271T → S or V: No effect on activity. 2 Publications
    Mutagenesisi527 – 5271T → Y: Greatly reduced activity. No tyrosine phosphorylation by PDRP1 in vitro. 2 Publications
    Mutagenesisi528 – 5281S → C: No effect on activity or phosphorylation by PDRP1 in vitro. 1 Publication
    Mutagenesisi528 – 5281S → Y or T: Greatly reduced activity. Strongly reduced or lack of phosphorylation by PDRP1 in vitro. 1 Publication
    Mutagenesisi529 – 5291H → N: Abolished activity. No phosphorylation on T-527 by PDRP1 in vitro. 1 Publication
    Mutagenesisi946 – 9461L → V: No decrease of the cold sensitivity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6262Chloroplast1 PublicationAdd
    BLAST
    Chaini63 – 947885Pyruvate, phosphate dikinase 1, chloroplasticPRO_0000431714Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei63 – 631N-acetylalanine; partial1 Publication
    Modified residuei309 – 3091Phosphothreonine1 Publication
    Modified residuei506 – 5061Phosphoserine1 Publication
    Modified residuei527 – 5271Phosphothreonine; by PDRP13 Publications
    Modified residuei528 – 5281Phosphoserine; by PDRP11 Publication

    Post-translational modificationi

    Phosphorylation of Thr-527 in the dark inactivates the enzyme, dephosphorylation upon light stimulation reactivates the enzyme (PubMed:2834385). More highly phosphorylated when grown under high rather than low light regimes (70 vs 900 µmol photons/m-2/s). the degree of phosphorylation is strictly regulated by light intensity and the light/dark transition has no influence (PubMed:24710069). Phosphorylated in both mesophyll and bundle sheath cells (PubMed:22833285). The phosphorylation at Ser-528 may be important for the phosphorylation at Thr-527 and may also be regulated by light intensity (PubMed:24710069).3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP11155.
    PRIDEiP11155.

    PTM databases

    iPTMnetiP11155.

    Expressioni

    Tissue specificityi

    Isoform C4PPDKZM1 mainly localized in mesophyll cells and only a low level is found in bundle sheath cells. Isoform CYPPDKZM1 expressed in roots, stems and etiolated leaves.3 Publications

    Inductioni

    Isoform C4ppdkZm1 is light-inducible.2 Publications

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi4577.GRMZM2G306345_P05.

    Structurei

    Secondary structure

    1
    947
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi76 – 816Combined sources
    Beta strandi84 – 874Combined sources
    Turni92 – 954Combined sources
    Helixi96 – 10712Combined sources
    Beta strandi115 – 1184Combined sources
    Helixi120 – 1289Combined sources
    Beta strandi129 – 1324Combined sources
    Helixi137 – 15216Combined sources
    Beta strandi159 – 1624Combined sources
    Beta strandi165 – 1684Combined sources
    Beta strandi182 – 1854Combined sources
    Helixi189 – 19911Combined sources
    Helixi201 – 21818Combined sources
    Helixi224 – 23815Combined sources
    Helixi243 – 2453Combined sources
    Helixi248 – 26619Combined sources
    Helixi274 – 28815Combined sources
    Helixi292 – 2998Combined sources
    Turni300 – 3023Combined sources
    Beta strandi311 – 3155Combined sources
    Beta strandi326 – 3338Combined sources
    Turni335 – 3373Combined sources
    Beta strandi343 – 3508Combined sources
    Helixi352 – 3576Combined sources
    Helixi366 – 3716Combined sources
    Helixi373 – 39018Combined sources
    Beta strandi394 – 4018Combined sources
    Beta strandi404 – 4129Combined sources
    Helixi417 – 42913Combined sources
    Helixi435 – 4384Combined sources
    Helixi439 – 4413Combined sources
    Helixi444 – 4496Combined sources
    Helixi458 – 4614Combined sources
    Turni462 – 4643Combined sources
    Beta strandi465 – 4684Combined sources
    Beta strandi470 – 4734Combined sources
    Beta strandi475 – 48410Combined sources
    Helixi485 – 4939Combined sources
    Beta strandi498 – 5036Combined sources
    Turni507 – 5093Combined sources
    Helixi510 – 5156Combined sources
    Beta strandi516 – 5238Combined sources
    Helixi529 – 5368Combined sources
    Beta strandi541 – 5433Combined sources
    Beta strandi548 – 5514Combined sources
    Turni552 – 5554Combined sources
    Beta strandi556 – 5594Combined sources
    Beta strandi562 – 5654Combined sources
    Beta strandi569 – 5735Combined sources
    Turni574 – 5774Combined sources
    Beta strandi578 – 5825Combined sources
    Helixi594 – 60512Combined sources
    Beta strandi608 – 6136Combined sources
    Helixi617 – 6259Combined sources
    Beta strandi630 – 6356Combined sources
    Helixi636 – 6405Combined sources
    Helixi644 – 65512Combined sources
    Helixi659 – 68325Combined sources
    Turni684 – 6863Combined sources
    Beta strandi687 – 6926Combined sources
    Helixi698 – 7014Combined sources
    Helixi707 – 71812Combined sources
    Helixi722 – 73211Combined sources
    Helixi737 – 7393Combined sources
    Helixi744 – 7496Combined sources
    Helixi751 – 76919Combined sources
    Turni770 – 7723Combined sources
    Beta strandi776 – 7816Combined sources
    Helixi787 – 80822Combined sources
    Beta strandi815 – 8206Combined sources
    Helixi823 – 8275Combined sources
    Helixi829 – 8324Combined sources
    Turni833 – 8353Combined sources
    Beta strandi837 – 8415Combined sources
    Helixi843 – 8519Combined sources
    Turni855 – 8573Combined sources
    Helixi858 – 8603Combined sources
    Helixi862 – 8676Combined sources
    Turni875 – 8773Combined sources
    Turni881 – 8833Combined sources
    Helixi884 – 89815Combined sources
    Beta strandi903 – 9086Combined sources
    Helixi909 – 9124Combined sources
    Helixi914 – 9229Combined sources
    Beta strandi926 – 9305Combined sources
    Helixi932 – 9343Combined sources
    Helixi935 – 94410Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VBGX-ray2.30A72-947[»]
    1VBHX-ray2.30A72-947[»]
    ProteinModelPortaliP11155.
    SMRiP11155. Positions 74-947.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11155.

    Family & Domainsi

    Domaini

    The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.

    Sequence similaritiesi

    Belongs to the PEP-utilizing enzyme family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0574. LUCA.

    Family and domain databases

    Gene3Di3.20.20.60. 1 hit.
    3.30.1490.20. 2 hits.
    3.30.470.20. 1 hit.
    3.50.30.10. 1 hit.
    InterProiIPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR008279. PEP-util_enz_mobile_dom.
    IPR018274. PEP_util_AS.
    IPR000121. PEP_util_C.
    IPR023151. PEP_util_CS.
    IPR002192. PPDK_PEP-bd.
    IPR010121. Pyruvate_phosphate_dikinase.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PANTHERiPTHR22931:SF9. PTHR22931:SF9. 1 hit.
    PfamiPF00391. PEP-utilizers. 1 hit.
    PF02896. PEP-utilizers_C. 1 hit.
    PF01326. PPDK_N. 3 hits.
    [Graphical view]
    PIRSFiPIRSF000853. PPDK. 1 hit.
    SUPFAMiSSF51621. SSF51621. 1 hit.
    SSF52009. SSF52009. 1 hit.
    TIGRFAMsiTIGR01828. pyru_phos_dikin. 1 hit.
    PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
    PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative promoter usage. AlignAdd to basket

    Isoform C4PPDKZM11 Publication (identifier: P11155-1) [UniParc]FASTAAdd to basket
    Also known as: C4PPDK1 Publication

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MAASVSRAIC VQKPGSKCTR DREATSFARR SVAAPRPPHA KAAGVIRSDS
    60 70 80 90 100
    GAGRGQHCSP LRAVVDAAPI QTTKKRVFHF GKGKSEGNKT MKELLGGKGA
    110 120 130 140 150
    NLAEMASIGL SVPPGFTVST EACQQYQDAG CALPAGLWAE IVDGLQWVEE
    160 170 180 190 200
    YMGATLGDPQ RPLLLSVRSG AAVSMPGMMD TVLNLGLNDE VAAGLAAKSG
    210 220 230 240 250
    ERFAYDSFRR FLDMFGNVVM DIPRSLFEEK LEHMKESKGL KNDTDLTASD
    260 270 280 290 300
    LKELVGQYKE VYLSAKGEPF PSDPKKQLEL AVLAVFNSWE SPRAKKYRSI
    310 320 330 340 350
    NQITGLRGTA VNVQCMVFGN MGNTSGTGVL FTRNPNTGEK KLYGEFLVNA
    360 370 380 390 400
    QGEDVVAGIR TPEDLDAMKN LMPQAYDELV ENCNILESHY KEMQDIEFTV
    410 420 430 440 450
    QENRLWMLQC RTGKRTGKSA VKIAVDMVNE GLVEPRSAIK MVEPGHLDQL
    460 470 480 490 500
    LHPQFENPSA YKDQVIATGL PASPGAAVGQ VVFTAEDAEA WHSQGKAAIL
    510 520 530 540 550
    VRAETSPEDV GGMHAAVGIL TERGGMTSHA AVVARWWGKC CVSGCSGIRV
    560 570 580 590 600
    NDAEKLVTIG SHVLREGEWL SLNGSTGEVI LGKQPLSPPA LSGDLGTFMA
    610 620 630 640 650
    WVDDVRKLKV LANADTPDDA LTARNNGAQG IGLCRTEHMF FASDERIKAV
    660 670 680 690 700
    RQMIMAPTLE LRQQALDRLL TYQRSDFEGI FRAMDGLPVT IRLLDHPSYE
    710 720 730 740 750
    FLPEGNIEDI VSELCAETGA NQEDALARIE KLSEVNPMLG FRGCRLGISY
    760 770 780 790 800
    PELTEMQARA IFEAAIAMTN QGVQVFPEIM VPLVGTPQEL GHQVTLIRQV
    810 820 830 840 850
    AEKVFANVGK TIGYKVGTMI EIPRAALVAD EIAEQAEFFS FGTNDLTQMT
    860 870 880 890 900
    FGYSRDDVGK FIPVHLAQGI LQHDPFEVLD QRGVGELVKF ATERGRKARP
    910 920 930 940
    NLKVGICGEH GGEPSSVAFF AKAGLDFVSC SPFRVPIARL AAAQVLV
    Length:947
    Mass (Da):102,674
    Last modified:July 1, 2008 - v2
    Checksum:i6D11F51D150ACFD1
    GO
    Isoform CYPPDKZM12 Publications (identifier: P11155-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-75: MAASVSRAIC...DAAPIQTTKK → MAPVQCARSQ

    Note: Produced by alternative promoter usage (PubMed:1668653). Cytoplasmic (PubMed:1668653). Initiator Met-1 is removed (PubMed:24710069).2 Publications
    Show »
    Length:882
    Mass (Da):95,968
    Checksum:i2836A730291B5524
    GO

    Sequence cautioni

    The sequence AAA33495 differs from that shown. Reason: Frameshift at positions 43 and 56. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → T in AAA33498 (PubMed:2170354).Curated
    Sequence conflicti2 – 21A → T in AAB23730 (PubMed:1668653).Curated
    Sequence conflicti218 – 2181Missing in ACR78549 (PubMed:19329568).Curated
    Sequence conflicti404 – 4041R → G in ACR78549 (PubMed:19329568).Curated
    Sequence conflicti536 – 5361W → G in AAA33498 (PubMed:2170354).Curated
    Sequence conflicti536 – 5361W → G in ACR78549 (PubMed:19329568).Curated
    Sequence conflicti561 – 5611S → G in AAA33498 (PubMed:2170354).Curated
    Sequence conflicti561 – 5611S → G in ACR78549 (PubMed:19329568).Curated
    Sequence conflicti671 – 6711T → P in AAA33498 (PubMed:2170354).Curated
    Sequence conflicti671 – 6711T → P in ACR78549 (PubMed:19329568).Curated
    Sequence conflicti696 – 6994HPSY → PPLH in AAA33498 (PubMed:2170354).Curated
    Sequence conflicti696 – 6994HPSY → PPLH in ACR78549 (PubMed:19329568).Curated
    Sequence conflicti760 – 7601A → V in ACR78549 (PubMed:19329568).Curated
    Sequence conflicti865 – 8651H → Y in AAA33498 (PubMed:2170354).Curated
    Sequence conflicti865 – 8651H → Y in ACR78549 (PubMed:19329568).Curated
    Sequence conflicti869 – 8735GILQH → EFGTS in AAD45281 (Ref. 8) Curated
    Sequence conflicti878 – 8781V → I in ACR78549 (PubMed:19329568).Curated
    Sequence conflicti890 – 8901F → L in AAA33498 (PubMed:2170354).Curated
    Sequence conflicti890 – 8901F → L in ACR78549 (PubMed:19329568).Curated
    Sequence conflicti927 – 9271F → Y in AAA33498 (PubMed:2170354).Curated
    Sequence conflicti927 – 9271F → Y in AAD45281 (Ref. 8) Curated
    Sequence conflicti927 – 9271F → Y in ACR78549 (PubMed:19329568).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7575MAASV…QTTKK → MAPVQCARSQ in isoform CYPPDKZM1. VSP_057373Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J03901 mRNA. Translation: AAA33495.1. Frameshift.
    M58656, M58655 Genomic DNA. Translation: AAA33498.1.
    S46966 Genomic DNA. Translation: AAB23731.1.
    S46965, S46964 Genomic DNA. Translation: AAB23730.1.
    X14927 Genomic DNA. Translation: CAA33054.1.
    FJ935764 Genomic DNA. Translation: ACR78549.1.
    AF152599 mRNA. Translation: AAD45281.1.
    PIRiA29225. KIZMPO.
    PQ0190.
    UniGeneiZm.19489.

    Keywords - Coding sequence diversityi

    Alternative promoter usage

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J03901 mRNA. Translation: AAA33495.1. Frameshift.
    M58656, M58655 Genomic DNA. Translation: AAA33498.1.
    S46966 Genomic DNA. Translation: AAB23731.1.
    S46965, S46964 Genomic DNA. Translation: AAB23730.1.
    X14927 Genomic DNA. Translation: CAA33054.1.
    FJ935764 Genomic DNA. Translation: ACR78549.1.
    AF152599 mRNA. Translation: AAD45281.1.
    PIRiA29225. KIZMPO.
    PQ0190.
    UniGeneiZm.19489.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VBGX-ray2.30A72-947[»]
    1VBHX-ray2.30A72-947[»]
    ProteinModelPortaliP11155.
    SMRiP11155. Positions 74-947.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi4577.GRMZM2G306345_P05.

    PTM databases

    iPTMnetiP11155.

    Proteomic databases

    PaxDbiP11155.
    PRIDEiP11155.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Organism-specific databases

    MaizeGDBi25385.

    Phylogenomic databases

    eggNOGiCOG0574. LUCA.

    Enzyme and pathway databases

    UniPathwayiUPA00322.
    BRENDAi2.7.9.1. 6752.
    SABIO-RKP11155.

    Miscellaneous databases

    EvolutionaryTraceiP11155.

    Family and domain databases

    Gene3Di3.20.20.60. 1 hit.
    3.30.1490.20. 2 hits.
    3.30.470.20. 1 hit.
    3.50.30.10. 1 hit.
    InterProiIPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR008279. PEP-util_enz_mobile_dom.
    IPR018274. PEP_util_AS.
    IPR000121. PEP_util_C.
    IPR023151. PEP_util_CS.
    IPR002192. PPDK_PEP-bd.
    IPR010121. Pyruvate_phosphate_dikinase.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PANTHERiPTHR22931:SF9. PTHR22931:SF9. 1 hit.
    PfamiPF00391. PEP-utilizers. 1 hit.
    PF02896. PEP-utilizers_C. 1 hit.
    PF01326. PPDK_N. 3 hits.
    [Graphical view]
    PIRSFiPIRSF000853. PPDK. 1 hit.
    SUPFAMiSSF51621. SSF51621. 1 hit.
    SSF52009. SSF52009. 1 hit.
    TIGRFAMsiTIGR01828. pyru_phos_dikin. 1 hit.
    PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
    PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPPDK1_MAIZE
    AccessioniPrimary (citable) accession number: P11155
    Secondary accession number(s): C5IHE0
    , Q41846, Q41847, Q42367, Q7DMU6, Q9XGW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 2008
    Last modified: February 17, 2016
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain.
    PubMed:1668653 shows the existence of a second gene coding only for the short cytoplasmic isoform of PPDK.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.