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Protein

Phosphoenolpyruvate carboxykinase [GTP]

Gene

PEPCK

Organism
Haemonchus contortus (Barber pole worm)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

In parasitic nematodes PEPCK carboxylates phosphoenolpyruvate to oxaloacetate thus introducing the products of glycolysis to mitochondrial metabolism.
Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.By similarity

Catalytic activityi

GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.

Cofactori

Mn2+By similarityNote: Binds 1 Mn2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei81 – 811SubstrateBy similarity
Binding sitei232 – 2321Substrate; via amide nitrogenBy similarity
Metal bindingi239 – 2391ManganeseBy similarity
Binding sitei239 – 2391SubstrateBy similarity
Metal bindingi259 – 2591Manganese; via tele nitrogenBy similarity
Binding sitei281 – 2811SubstrateBy similarity
Active sitei283 – 2831By similarity
Metal bindingi306 – 3061ManganeseBy similarity
Binding sitei401 – 4011GTPBy similarity
Binding sitei432 – 4321GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi282 – 2876GTPBy similarity
Nucleotide bindingi525 – 5284GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

GTP-binding, Manganese, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate carboxykinase [GTP] (EC:4.1.1.32)
Short name:
PEPCK
Gene namesi
Name:PEPCK
OrganismiHaemonchus contortus (Barber pole worm)
Taxonomic identifieri6289 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaStrongylidaTrichostrongyloideaHaemonchidaeHaemonchinaeHaemonchus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 619619Phosphoenolpyruvate carboxykinase [GTP]PRO_0000103633Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP29190.
SMRiP29190. Positions 7-617.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni399 – 4013Substrate bindingBy similarity

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPiMF_00452. PEPCK_GTP.
InterProiIPR018091. PEP_carboxykin_GTP_CS.
IPR013035. PEP_carboxykinase_C.
IPR008209. PEP_carboxykinase_GTP.
IPR008210. PEP_carboxykinase_N.
[Graphical view]
PANTHERiPTHR11561. PTHR11561. 1 hit.
PfamiPF00821. PEPCK. 1 hit.
[Graphical view]
PIRSFiPIRSF001348. PEP_carboxykinase_GTP. 1 hit.
SUPFAMiSSF68923. SSF68923. 1 hit.
PROSITEiPS00505. PEPCK_GTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29190-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRLGHVPIH KGDFHLLPPK VQRFVAEKAE LMRPRGIYIC DGSQHEADEI
60 70 80 90 100
IDKLIERGML SPLKAYENNY ICRTDPKDVA RVESKTWMVT PDKYQTVCHT
110 120 130 140 150
PDGIEPIMGH WMSPDSLATE LDSRFPGCMA GRIMYVIPFS MGPVGGPLSK
160 170 180 190 200
IGVQLTDSNY VVLSMRIMTR VGHEVWDALG DNDFVRCIHS VGLPRPVKQR
210 220 230 240 250
VINHWPCNPE RVLIAHRPAE REIWSFGSGY GGNSLLGKKM LALRIASNIA
260 270 280 290 300
KDEGWMAEHM LIMGVTRPDG KEHFIAAAFP SACGKTNLAM LEPALPGWKV
310 320 330 340 350
RCVGDDIAWM KFGEDGRLYA INPEYGFFGV APGTSKKTNP MAVATFQKNS
360 370 380 390 400
IFTNVGETAN GEYFWEGLED EIKDKNVDMI NWLGEKWRIG DPGLCAHPNS
410 420 430 440 450
RFAAPASQCP IIHPEWESPK GVPIDAIIFG GRRPAGVPLV FETRSWLHGI
460 470 480 490 500
FTGACLKSEA TAAAEHKGKT VMHDPMAMRP FMGYNFGHYL QHWIDLNKDG
510 520 530 540 550
RKVPKIYHVN WFRRDANNKF LWPGYGQNIR VIDWIVRRLD GEPDIGVDTP
560 570 580 590 600
IGIVPKKGAI NASGLPDIQW DELMSVPKEY WTNDAKEIRK FLEEQVGPDL
610
PKEIRAEMDA QEERINKQA
Length:619
Mass (Da):69,656
Last modified:December 1, 1992 - v1
Checksum:i40A801A1EB647CFD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76494 mRNA. Translation: AAA29180.1.
PIRiA45625.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76494 mRNA. Translation: AAA29180.1.
PIRiA45625.

3D structure databases

ProteinModelPortaliP29190.
SMRiP29190. Positions 7-617.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPiMF_00452. PEPCK_GTP.
InterProiIPR018091. PEP_carboxykin_GTP_CS.
IPR013035. PEP_carboxykinase_C.
IPR008209. PEP_carboxykinase_GTP.
IPR008210. PEP_carboxykinase_N.
[Graphical view]
PANTHERiPTHR11561. PTHR11561. 1 hit.
PfamiPF00821. PEPCK. 1 hit.
[Graphical view]
PIRSFiPIRSF001348. PEP_carboxykinase_GTP. 1 hit.
SUPFAMiSSF68923. SSF68923. 1 hit.
PROSITEiPS00505. PEPCK_GTP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning of a cDNA encoding phosphoenolpyruvate carboxykinase from Haemonchus contortus."
    Klein R.D., Winterrowd C.A., Hatzenbuhler N.T., Shea M.H., Favreau M.A., Nulf S.C., Geary T.G.
    Mol. Biochem. Parasitol. 50:285-294(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPCKG_HAECO
AccessioniPrimary (citable) accession number: P29190
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 26, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.