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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)DescriptionActionsGraphical viewLength
    Active sitei529Tele-phosphohistidine intermediate1 Publication1
    Binding sitei635Substrate1 Publication1
    Binding sitei692Substrate1 Publication1
    Metal bindingi821Magnesium1 Publication1
    Binding sitei821Substrate1 Publication1
    Binding sitei842Substrate; via carbonyl oxygen1 Publication1
    Binding sitei843Substrate; via amide nitrogen1 Publication1
    Binding sitei844Substrate1 Publication1
    Metal bindingi845Magnesium1 Publication1
    Binding sitei845Substrate; via amide nitrogen1 Publication1
    Active sitei907Proton donor1 Publication1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi525G → A or P: Greatly reduced activity. Strongly reduced or lack of phosphorylation by PDRP1 in vitro. 1 Publication1
    Mutagenesisi527T → D or E: Abolished activity. 2 Publications1
    Mutagenesisi527T → N: Greatly reduced activity. 2 Publications1
    Mutagenesisi527T → S or V: No effect on activity. 2 Publications1
    Mutagenesisi527T → Y: Greatly reduced activity. No tyrosine phosphorylation by PDRP1 in vitro. 2 Publications1
    Mutagenesisi528S → C: No effect on activity or phosphorylation by PDRP1 in vitro. 1 Publication1
    Mutagenesisi528S → Y or T: Greatly reduced activity. Strongly reduced or lack of phosphorylation by PDRP1 in vitro. 1 Publication1
    Mutagenesisi529H → N: Abolished activity. No phosphorylation on T-527 by PDRP1 in vitro. 1 Publication1
    Mutagenesisi946L → V: No decrease of the cold sensitivity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 62Chloroplast1 PublicationAdd BLAST62
    ChainiPRO_000043171463 – 947Pyruvate, phosphate dikinase 1, chloroplasticAdd BLAST885

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei63N-acetylalanine; partial1 Publication1
    Modified residuei309Phosphothreonine1 Publication1
    Modified residuei506Phosphoserine1 Publication1
    Modified residuei527Phosphothreonine; by PDRP13 Publications1
    Modified residuei528Phosphoserine; by PDRP11 Publication1

    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

    1947
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi76 – 81Combined sources6
    Beta strandi84 – 87Combined sources4
    Turni92 – 95Combined sources4
    Helixi96 – 107Combined sources12
    Beta strandi115 – 118Combined sources4
    Helixi120 – 128Combined sources9
    Beta strandi129 – 132Combined sources4
    Helixi137 – 152Combined sources16
    Beta strandi159 – 162Combined sources4
    Beta strandi165 – 168Combined sources4
    Beta strandi182 – 185Combined sources4
    Helixi189 – 199Combined sources11
    Helixi201 – 218Combined sources18
    Helixi224 – 238Combined sources15
    Helixi243 – 245Combined sources3
    Helixi248 – 266Combined sources19
    Helixi274 – 288Combined sources15
    Helixi292 – 299Combined sources8
    Turni300 – 302Combined sources3
    Beta strandi311 – 315Combined sources5
    Beta strandi326 – 333Combined sources8
    Turni335 – 337Combined sources3
    Beta strandi343 – 350Combined sources8
    Helixi352 – 357Combined sources6
    Helixi366 – 371Combined sources6
    Helixi373 – 390Combined sources18
    Beta strandi394 – 401Combined sources8
    Beta strandi404 – 412Combined sources9
    Helixi417 – 429Combined sources13
    Helixi435 – 438Combined sources4
    Helixi439 – 441Combined sources3
    Helixi444 – 449Combined sources6
    Helixi458 – 461Combined sources4
    Turni462 – 464Combined sources3
    Beta strandi465 – 468Combined sources4
    Beta strandi470 – 473Combined sources4
    Beta strandi475 – 484Combined sources10
    Helixi485 – 493Combined sources9
    Beta strandi498 – 503Combined sources6
    Turni507 – 509Combined sources3
    Helixi510 – 515Combined sources6
    Beta strandi516 – 523Combined sources8
    Helixi529 – 536Combined sources8
    Beta strandi541 – 543Combined sources3
    Beta strandi548 – 551Combined sources4
    Turni552 – 555Combined sources4
    Beta strandi556 – 559Combined sources4
    Beta strandi562 – 565Combined sources4
    Beta strandi569 – 573Combined sources5
    Turni574 – 577Combined sources4
    Beta strandi578 – 582Combined sources5
    Helixi594 – 605Combined sources12
    Beta strandi608 – 613Combined sources6
    Helixi617 – 625Combined sources9
    Beta strandi630 – 635Combined sources6
    Helixi636 – 640Combined sources5
    Helixi644 – 655Combined sources12
    Helixi659 – 683Combined sources25
    Turni684 – 686Combined sources3
    Beta strandi687 – 692Combined sources6
    Helixi698 – 701Combined sources4
    Helixi707 – 718Combined sources12
    Helixi722 – 732Combined sources11
    Helixi737 – 739Combined sources3
    Helixi744 – 749Combined sources6
    Helixi751 – 769Combined sources19
    Turni770 – 772Combined sources3
    Beta strandi776 – 781Combined sources6
    Helixi787 – 808Combined sources22
    Beta strandi815 – 820Combined sources6
    Helixi823 – 827Combined sources5
    Helixi829 – 832Combined sources4
    Turni833 – 835Combined sources3
    Beta strandi837 – 841Combined sources5
    Helixi843 – 851Combined sources9
    Turni855 – 857Combined sources3
    Helixi858 – 860Combined sources3
    Helixi862 – 867Combined sources6
    Turni875 – 877Combined sources3
    Turni881 – 883Combined sources3
    Helixi884 – 898Combined sources15
    Beta strandi903 – 908Combined sources6
    Helixi909 – 912Combined sources4
    Helixi914 – 922Combined sources9
    Beta strandi926 – 930Combined sources5
    Helixi932 – 934Combined sources3
    Helixi935 – 944Combined sources10

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1VBGX-ray2.30A72-947[»]
    1VBHX-ray2.30A72-947[»]
    ProteinModelPortaliP11155.
    SMRiP11155.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti2A → T in AAA33498 (PubMed:2170354).Curated1
    Sequence conflicti2A → T in AAB23730 (PubMed:1668653).Curated1
    Sequence conflicti218Missing in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti404R → G in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti536W → G in AAA33498 (PubMed:2170354).Curated1
    Sequence conflicti536W → G in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti561S → G in AAA33498 (PubMed:2170354).Curated1
    Sequence conflicti561S → G in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti671T → P in AAA33498 (PubMed:2170354).Curated1
    Sequence conflicti671T → P in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti696 – 699HPSY → PPLH in AAA33498 (PubMed:2170354).Curated4
    Sequence conflicti696 – 699HPSY → PPLH in ACR78549 (PubMed:19329568).Curated4
    Sequence conflicti760A → V in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti865H → Y in AAA33498 (PubMed:2170354).Curated1
    Sequence conflicti865H → Y in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti869 – 873GILQH → EFGTS in AAD45281 (Ref. 8) Curated5
    Sequence conflicti878V → I in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti890F → L in AAA33498 (PubMed:2170354).Curated1
    Sequence conflicti890F → L in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti927F → Y in AAA33498 (PubMed:2170354).Curated1
    Sequence conflicti927F → Y in AAD45281 (Ref. 8) Curated1
    Sequence conflicti927F → Y in ACR78549 (PubMed:19329568).Curated1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0573731 – 75MAASV…QTTKK → MAPVQCARSQ in isoform CYPPDKZM1. Add BLAST75

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1VBGX-ray2.30A72-947[»]
    1VBHX-ray2.30A72-947[»]
    ProteinModelPortaliP11155.
    SMRiP11155.
    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: November 2, 2016
    This is version 134 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.