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P07378

- PGKC_TRYBB

UniProt

P07378 - PGKC_TRYBB

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Protein

Phosphoglycerate kinase, glycosomal

Gene
N/A
Organism
Trypanosoma brucei brucei
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391Substrate1 Publication
Binding sitei135 – 1351Substrate1 Publication
Binding sitei172 – 1721Substrate1 Publication
Binding sitei223 – 2231ATP
Binding sitei338 – 3381ATP
Binding sitei345 – 3451ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi375 – 3784ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphoglycerate kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKP07378.
UniPathwayiUPA00109; UER00185.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate kinase, glycosomal (EC:2.7.2.3)
Short name:
Phosphoglycerate kinase C
OrganismiTrypanosoma brucei brucei
Taxonomic identifieri5702 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Subcellular locationi

GO - Cellular componenti

  1. glycosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Glycosome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Phosphoglycerate kinase, glycosomalPRO_0000145866Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
440
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113Combined sources
Beta strandi18 – 236Combined sources
Beta strandi33 – 353Combined sources
Helixi38 – 5215Combined sources
Beta strandi56 – 605Combined sources
Helixi71 – 733Combined sources
Helixi74 – 796Combined sources
Helixi88 – 903Combined sources
Helixi93 – 10311Combined sources
Beta strandi108 – 1114Combined sources
Helixi117 – 1215Combined sources
Beta strandi128 – 1314Combined sources
Helixi134 – 1363Combined sources
Helixi138 – 1414Combined sources
Helixi145 – 15612Combined sources
Beta strandi160 – 1656Combined sources
Helixi167 – 1693Combined sources
Turni175 – 1784Combined sources
Helixi179 – 1846Combined sources
Helixi191 – 20414Combined sources
Beta strandi209 – 2157Combined sources
Helixi221 – 2233Combined sources
Helixi224 – 2307Combined sources
Helixi231 – 2333Combined sources
Beta strandi235 – 2395Combined sources
Helixi243 – 2519Combined sources
Helixi262 – 2643Combined sources
Helixi265 – 27713Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi286 – 29510Combined sources
Beta strandi304 – 3063Combined sources
Beta strandi313 – 3175Combined sources
Helixi319 – 32911Combined sources
Beta strandi333 – 3397Combined sources
Helixi347 – 3493Combined sources
Helixi351 – 36717Combined sources
Beta strandi370 – 3734Combined sources
Helixi376 – 3849Combined sources
Turni388 – 3903Combined sources
Beta strandi391 – 3944Combined sources
Helixi398 – 4058Combined sources
Helixi411 – 4144Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
13PKX-ray2.50A/B/C/D5-417[»]
16PKX-ray1.60A5-417[»]
ProteinModelPortaliP07378.
SMRiP07378. Positions 5-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07378.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 263Substrate binding
Regioni62 – 654Substrate binding

Sequence similaritiesi

Belongs to the phosphoglycerate kinase family.Curated

Family and domain databases

Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase.
InterProiIPR027250. Pgk_euglenozoa.
IPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERiPTHR11406. PTHR11406. 1 hit.
PfamiPF00162. PGK. 1 hit.
[Graphical view]
PIRSFiPIRSF000724. Pgk. 1 hit.
PIRSF500126. Pgk_euglenozoa. 1 hit.
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF53748. SSF53748. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07378-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTLNEKKSIN ECDLKGKKVL IRVDFNVPVK NGKITNDYRI RSALPTLKKV
60 70 80 90 100
LTEGGSCVLM SHLGRPKGIP MAQAGKIRST GGVPGFQQKA TLKPVAKALS
110 120 130 140 150
ELLLRPVTFA PDCLNAADVV SKMSPGDVVL LENVRFYKEE GSKKAKDREA
160 170 180 190 200
MAKILASYGD VYISDAFGTA HRDSATMTGI PKILGNGAAG YLMEKEISYF
210 220 230 240 250
AKVLGNPPRP LVAIVGGAKV SDKIQLLDNM LQRIDYLLIG GAMAYTFLKA
260 270 280 290 300
QGYSIGKSKC EESKLEFARS LLKKAEDRKV QVILPIDHVC HTEFKAVDSP
310 320 330 340 350
LITEDQNIPE GHMALDIGPK TIEKYVQTIG KCKSAIWNGP MGVFEMVPYS
360 370 380 390 400
KGTFAIAKAM GRGTHEHGLM SIIGGGDSAS AAELSGEAKR MSHVSTGGGA
410 420 430 440
SLELLEGKTL PGVTVLDEKS AVVSYASAGT GTLSNRWSSL
Length:440
Mass (Da):47,119
Last modified:April 1, 1988 - v1
Checksum:iEF95775C216ABDC3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751G → D in allele 4.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03370 Genomic DNA. Translation: CAA27069.1.
X05889 Genomic DNA. Translation: CAA29318.1.
X05890 Genomic DNA. Translation: CAA29321.1.
PIRiB25119. KIUTGG.
S02235. TVUTGB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03370 Genomic DNA. Translation: CAA27069.1 .
X05889 Genomic DNA. Translation: CAA29318.1 .
X05890 Genomic DNA. Translation: CAA29321.1 .
PIRi B25119. KIUTGG.
S02235. TVUTGB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
13PK X-ray 2.50 A/B/C/D 5-417 [» ]
16PK X-ray 1.60 A 5-417 [» ]
ProteinModelPortali P07378.
SMRi P07378. Positions 5-419.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL1741167.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00185 .
SABIO-RK P07378.

Miscellaneous databases

EvolutionaryTracei P07378.

Family and domain databases

Gene3Di 3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPi MF_00145. Phosphoglyc_kinase.
InterProi IPR027250. Pgk_euglenozoa.
IPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view ]
PANTHERi PTHR11406. PTHR11406. 1 hit.
Pfami PF00162. PGK. 1 hit.
[Graphical view ]
PIRSFi PIRSF000724. Pgk. 1 hit.
PIRSF500126. Pgk_euglenozoa. 1 hit.
PRINTSi PR00477. PHGLYCKINASE.
SUPFAMi SSF53748. SSF53748. 1 hit.
PROSITEi PS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Evidence for gene conversion between the phosphoglycerate kinase genes of Trypanosoma brucei."
    le Blancq S.M., Swinkels B.W., Gibson W.C., Borst P.
    J. Mol. Biol. 200:439-447(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES 2 AND 4).
  2. "Topogenesis of microbody enzymes: a sequence comparison of the genes for the glycosomal (microbody) and cytosolic phosphoglycerate kinases of Trypanosoma brucei."
    Osinga K.A., Swinkels B.W., Gibson W.C., Borst P., Veeneman G.H., van Boom J.H., Michels P.A.M., Opperdoes F.R.
    EMBO J. 4:3811-3817(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation."
    Bernstein B.E., Michels P.A.M., Hol W.G.J.
    Nature 385:275-278(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  4. "A bisubstrate analog induces unexpected conformational changes in phosphoglycerate kinase from Trypanosoma brucei."
    Bernstein B.E., Williams D.M., Bressi J.C., Kuhn P., Gelb M.H., Blackburn G.M., Hol W.G.J.
    J. Mol. Biol. 279:1137-1148(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 5-419 IN COMPLEX WITH ADP AND SUBSTRATE.

Entry informationi

Entry nameiPGKC_TRYBB
AccessioniPrimary (citable) accession number: P07378
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 26, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

In T.brucei, three genes code for phosphoglycerate kinase isozymes, which are transported to different cell compartments.

Keywords - Technical termi

3D-structure

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

External Data

Dasty 3