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Protein

Pyruvate kinase

Gene

pkiA

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarity
  • K+By similarity

Pathwayi: glycolysis

This protein is involved in step 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (gpdA), Glyceraldehyde-3-phosphate dehydrogenase (ABL_09274)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. Pyruvate kinase (ABL_02840), Pyruvate kinase (pkiA)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei63SubstrateBy similarity1
Metal bindingi65PotassiumBy similarity1
Metal bindingi67PotassiumBy similarity1
Metal bindingi98PotassiumBy similarity1
Metal bindingi99Potassium; via carbonyl oxygenBy similarity1
Sitei254Transition state stabilizerBy similarity1
Metal bindingi256MagnesiumSequence analysis1
Binding sitei279Substrate; via amide nitrogenBy similarity1
Metal bindingi280MagnesiumBy similarity1
Binding sitei280Substrate; via amide nitrogenBy similarity1
Binding sitei312SubstrateBy similarity1
Binding sitei351ADPSequence analysis1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase (EC:2.7.1.40)
Short name:
PK
Gene namesi
Name:pkiA
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001121081 – 526Pyruvate kinaseAdd BLAST526

Proteomic databases

PaxDbiQ12669.
PRIDEiQ12669.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi5061.CADANGAP00006051.

Structurei

3D structure databases

ProteinModelPortaliQ12669.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGiKOG2323. Eukaryota.
COG0469. LUCA.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12669-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASSSLDHL SNRMKLEWHS KLNTEMVPSK NFRRTSIIGT IGPKTNSVEK
60 70 80 90 100
INSLRTAGLN VVRMNFSHGS YQYHQSVIDN AREAAKTQVG RPLAIALDTK
110 120 130 140 150
GPEIRTGNTP DDKDIPIKQG HELNITTDEQ YATASDDKNM YLDYKNITKV
160 170 180 190 200
ISPGKLIYVD DGILSFEVLE VVDDKTIRVR CLNNGNISSR KGVNLPGTDV
210 220 230 240 250
DLPALSEKDI ADLKFGVRNK VDMVFASFIR RGSDIRHIRE VLGEEGKEIQ
260 270 280 290 300
IIAKIENQQG VNNFDEILEE TDGVMVARGD LGIEIPAPKV FIAQKMMIAK
310 320 330 340 350
CNIKGKPVIC ATQMLESMTY NPRPTRAEVS DVANAVLDGA DCVMLSGETA
360 370 380 390 400
KGNYPNEAVK MMSETCLLAE VAIPHFNVFD ELRNLAPRPT DTVESIAMAA
410 420 430 440 450
VSASLELNAG AIVVLTTSGK TARYLSKYRP VCPIVMVTRN PAASRYSHLY
460 470 480 490 500
RGVWPFLFPE KKPDFNVKVW QEDVDRRLKW GINHALKLGI INKGDNIVCV
510 520
QGWRGGMGHT NTVRVVPAEE NLGLAE
Length:526
Mass (Da):58,134
Last modified:November 1, 1996 - v1
Checksum:i8B7ED999C46D780C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S38698 Genomic DNA. Translation: AAB22392.1.
PIRiS26869.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S38698 Genomic DNA. Translation: AAB22392.1.
PIRiS26869.

3D structure databases

ProteinModelPortaliQ12669.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00006051.

Proteomic databases

PaxDbiQ12669.
PRIDEiQ12669.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2323. Eukaryota.
COG0469. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKPYK_ASPNG
AccessioniPrimary (citable) accession number: Q12669
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 5, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.