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Protein

Phosphoenolpyruvate carboxykinase [GTP]

Gene

PEPCK

Organism
Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
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 sitei102 – 1021SubstrateBy similarity
Metal bindingi262 – 2621ManganeseBy similarity
Metal bindingi282 – 2821Manganese; via tele nitrogenBy similarity
Binding sitei304 – 3041SubstrateBy similarity
Active sitei306 – 3061By similarity
Metal bindingi329 – 3291ManganeseBy similarity
Binding sitei424 – 4241GTPBy similarity
Binding sitei455 – 4551GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi305 – 3106GTPBy similarity
Nucleotide bindingi548 – 5514GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18260.
SABIO-RKQ05893.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate carboxykinase [GTP] (EC:4.1.1.32)
Short name:
PEPCK
Gene namesi
Name:PEPCK
OrganismiAscaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifieri6253 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 643643Phosphoenolpyruvate carboxykinase [GTP]PRO_0000103632Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliQ05893.
SMRiQ05893. Positions 27-641.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni253 – 2553Substrate bindingBy similarity
Regioni422 – 4243Substrate 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.

Q05893-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRCRSLSHFK DDDFAVVSEV VTHKQNHIPV IKGDFVSLPK HVQRFVAEKA
60 70 80 90 100
ELMKPSAIFI CDGSQNEADE LIARCVERGV LVPLKAYKNN YLCRTDPRDV
110 120 130 140 150
ARVESKTWMI TPEKYDSVCH TPEGVKPMMG QWMSPDEFGK ELDDRFPGCM
160 170 180 190 200
AGRTMYVIPY SMGPVGGPLS KIGIELTDSD YVVLCMRIMT RMGEPVLKAL
210 220 230 240 250
AKNNGEFVRC VHSVGQPKPV ATKVINHWPC NPEKTIIAHR PAEREIWSFG
260 270 280 290 300
SGYGGNSLLG KKCFALRIAM NIGYDEGWMA EHMLIMGVTS PKGEERFVAA
310 320 330 340 350
AFPSACGKTN LAMLEPTIPG WKVRVIGDDI AWMKFGADGR LYAINPEYGF
360 370 380 390 400
FGVAPGTSHK TNPMAMASFQ ENTIFTNVAE TADGEYFWEG LEHEVKNPKV
410 420 430 440 450
DMINWLGEPW HIGDESKAAH PNSRFTAPAG QCPIIHPDWE KPEGVPIDAI
460 470 480 490 500
IFGGRRPEGV PLVFESRSWV HGIFVGACVK SEATAAAEHT GKQVMHDPMA
510 520 530 540 550
MRPFMGYNFG RYMRHWMKLG QPPHKVPKIF HVNWFRQSAD HKFLWPGYGD
560 570 580 590 600
NIRVIDWILR RCSGDATIAE ETPIGFIPKK GTINLEGLPN VNWDELMSIP
610 620 630 640
KSYWLEDMVE TKTFFENQVG SDLPPEIAKE LEAQTERIKA LKE
Length:643
Mass (Da):72,230
Last modified:February 1, 1994 - v1
Checksum:iA9C369959AA79E27
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01787 mRNA. Translation: AAA29378.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01787 mRNA. Translation: AAA29378.1.

3D structure databases

ProteinModelPortaliQ05893.
SMRiQ05893. Positions 27-641.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18260.
SABIO-RKQ05893.

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. "Ascaris suum: cloning of a cDNA encoding phosphoenolpyruvate carboxykinase."
    Geary T.G., Winterrowd C.A., Alexander-Bowman S.J., Favreau M.A., Nulf S.C., Klein R.D.
    Exp. Parasitol. 77:155-161(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Nerve cord and Pharynx.

Entry informationi

Entry nameiPCKG_ASCSU
AccessioniPrimary (citable) accession number: Q05893
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 22, 2015
This is version 71 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.