Q05893 (PCKG_ASCSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoenolpyruvate carboxykinase [GTP]
Short name=PEPCK
EC=4.1.1.32

Alternative name(s):
Phosphoenolpyruvate carboxylase

Gene names

Name:

PEPCK

Organism

Ascaris suum (Pig roundworm) (Ascaris lumbricoides)

Taxonomic identifier

6253 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Ascaridida › Ascaridoidea › Ascarididae › Ascaris

Protein attributes

Sequence length	643 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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 activity	GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.
Cofactor	Binds 1 manganese ion per subunit By similarity.
Subunit structure	Monomer.
Sequence similarities	Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.

Ontologies

Keywords
Ligand	GTP-binding Manganese Metal-binding Nucleotide-binding
Molecular function	Decarboxylase Lyase
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from electronic annotation. Source: InterPro
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoenolpyruvate carboxykinase (GTP) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 643	643	Phosphoenolpyruvate carboxykinase [GTP]		PRO_0000103632
Regions
	Nucleotide binding	305 – 310	6	GTP By similarity
	Nucleotide binding	548 – 551	4	GTP By similarity
	Region	422 – 424	3	Substrate binding By similarity
Sites
	Active site	306	1	By similarity
	Metal binding	262	1	Manganese By similarity
	Metal binding	282	1	Manganese By similarity
	Metal binding	329	1	Manganese By similarity
	Binding site	102	1	Substrate By similarity
	Binding site	255	1	Substrate; via amide nitrogen By similarity
	Binding site	262	1	Substrate By similarity
	Binding site	304	1	Substrate By similarity
	Binding site	424	1	GTP By similarity
	Binding site	455	1	GTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q05893 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: A9C369959AA79E27	FASTA	643	72,230
	10 20 30 40 50 60 MRCRSLSHFK DDDFAVVSEV VTHKQNHIPV IKGDFVSLPK HVQRFVAEKA ELMKPSAIFI 70 80 90 100 110 120 CDGSQNEADE LIARCVERGV LVPLKAYKNN YLCRTDPRDV ARVESKTWMI TPEKYDSVCH 130 140 150 160 170 180 TPEGVKPMMG QWMSPDEFGK ELDDRFPGCM AGRTMYVIPY SMGPVGGPLS KIGIELTDSD 190 200 210 220 230 240 YVVLCMRIMT RMGEPVLKAL AKNNGEFVRC VHSVGQPKPV ATKVINHWPC NPEKTIIAHR 250 260 270 280 290 300 PAEREIWSFG SGYGGNSLLG KKCFALRIAM NIGYDEGWMA EHMLIMGVTS PKGEERFVAA 310 320 330 340 350 360 AFPSACGKTN LAMLEPTIPG WKVRVIGDDI AWMKFGADGR LYAINPEYGF FGVAPGTSHK 370 380 390 400 410 420 TNPMAMASFQ ENTIFTNVAE TADGEYFWEG LEHEVKNPKV DMINWLGEPW HIGDESKAAH 430 440 450 460 470 480 PNSRFTAPAG QCPIIHPDWE KPEGVPIDAI IFGGRRPEGV PLVFESRSWV HGIFVGACVK 490 500 510 520 530 540 SEATAAAEHT GKQVMHDPMA MRPFMGYNFG RYMRHWMKLG QPPHKVPKIF HVNWFRQSAD 550 560 570 580 590 600 HKFLWPGYGD NIRVIDWILR RCSGDATIAE ETPIGFIPKK GTINLEGLPN VNWDELMSIP 610 620 630 640 KSYWLEDMVE TKTFFENQVG SDLPPEIAKE LEAQTERIKA LKE

References

[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: 8375484] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Nerve cord and Pharynx.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L01787 mRNA. Translation: AAA29378.1.
3D structure databases
ProteinModelPortal	Q05893.
SMR	Q05893. Positions 27-641.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR018091. PEP_carboxykin_GTP_CS. IPR013035. PEP_carboxykinase_C. IPR008209. PEP_carboxykinase_GTP. IPR008210. PEP_carboxykinase_N. [Graphical view]
Gene3D	G3DSA:3.90.228.20. PEP_carboxykinase_C. 2 hits. G3DSA:3.40.449.10. PEP_carboxykinase_N. 1 hit.
PANTHER	PTHR11561. PEP_carboxykin. 1 hit.
Pfam	PF00821. PEPCK. 1 hit. [Graphical view]
PIRSF	PIRSF001348. PEP_carboxykinase_GTP. 1 hit.
SUPFAM	SSF68923. PEP_carboxykinase_N. 1 hit.
PROSITE	PS00505. PEPCK_GTP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PCKG_ASCSU

Accession

Primary (citable) accession number: Q05893

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 31, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)