Reviewed, UniProtKB/Swiss-Prot Q2J645 (PCKG_FRASC)

Names and origin

Protein names

Recommended name:
    Phosphoenolpyruvate carboxykinase [GTP]
      Short name=PEP carboxykinase
      Short name=PEPCK
    EC=4.1.1.32
Alternative name(s):
    Phosphoenolpyruvate carboxylase

Gene names

Name:	pckG
Ordered Locus Names:	Francci3_3897

Organism

Frankia sp. (strain CcI3) [Complete proteome] [HAMAP]

Taxonomic identifier

106370 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Frankiaceae › Frankia

Protein attributes

Sequence length	609 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	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. HAMAP MF_00452
Cofactor	Binds 1 manganese ion per subunit By similarity.
Pathway	Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_00452
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.

Ontologies

Keywords
Biological process	Gluconeogenesis
Cellular component	Cytoplasm
Ligand	GTP-binding Manganese Metal-binding Nucleotide-binding
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoenolpyruvate carboxykinase (GTP) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 609	609	Phosphoenolpyruvate carboxykinase [GTP] HAMAP MF_00452		PRO_1000060290
Regions
	Nucleotide binding	273 – 278	6	GTP By similarity
	Nucleotide binding	515 – 518	4	GTP By similarity
	Region	387 – 389	3	Substrate binding By similarity
Sites
	Active site	274	1	By similarity
	Metal binding	230	1	Manganese By similarity
	Metal binding	250	1	Manganese By similarity
	Metal binding	297	1	Manganese By similarity
	Binding site	82	1	Substrate By similarity
	Binding site	223	1	Substrate; via amide nitrogen By similarity
	Binding site	230	1	Substrate By similarity
	Binding site	272	1	Substrate By similarity
	Binding site	389	1	GTP By similarity
	Binding site	420	1	GTP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2J645-1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: 3790D69E45471916	FASTA	609	66,912
	10 20 30 40 50 60 MTTAAQVSGL DVAPTRHARL VAWVREIAEL TQPDRVEWCD GSEAEFDRLT SLLIEQGTLV 70 80 90 100 110 120 RLNDEKRPNS FYAASDPGDV ARVEDRTYIC SEQAEDAGPT NNWLDPAEMR ATLRGLFAGC 130 140 150 160 170 180 MRGRTMYVVP FCMGPLGSRI SALGVEITDS PYVVISMRTM TRMGTPALEQ LGTDGFFVPA 190 200 210 220 230 240 VHSLGAPLEP GQADVPWPCN TTKYITHFPE TREIWSYGSG YGGNALLGKK CYALRIASVM 250 260 270 280 290 300 ARDEGWLAEH MLILKLTSPA GKVHYIAAAF PSACGKTNLA MLIPTLPGWQ AETVGDDIAW 310 320 330 340 350 360 MRFGEDGRLY AVNPEAGFFG VAPGTGEQTN PNAVRTLWGN AIYTNVARTD NGDVWWEGLT 370 380 390 400 410 420 KQPPAHLIDW KGRDWTPESS EPAAHPNARF TVPAGQCPTI APEWEDPRGV PISAILFGGR 430 440 450 460 470 480 RATAVPLVTE APDWRRGVFF GSIVASETTA AQAGAIGKLR RDPFAMLPFC GYNMADYFAH 490 500 510 520 530 540 WLEVGQKADQ TKLPRVYYVN WFRKSPEGRF LWPGFGDNSR VLAWIVGRLE GTAAGVETPL 550 560 570 580 590 600 GVLPTKDALP VDGIDIAEED LETLLTVDVE VWKQEAQLIP EHYQTFGERL PAALWTEHEA LVERLNSAD

References

[1]

"Genome characteristics of facultatively symbiotic Frankia sp. strains reflect host range and host plant biogeography." Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P., Goltsman E., Huang Y. , Kopp O.R., Labarre L., Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R. Genome Res. 17:7-15(2007) [PubMed: 17151343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000249 Genomic DNA. Translation: ABD13247.1.
RefSeq	YP_482976.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3906665.
GenomeReviews	Gene locus Francci3_3897 in contig CP000249_GR.
KEGG	fra:Francci3_3897.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2J645.
OMA	Q2J645. SHPNARF.
Enzyme and pathway databases
BioCyc	FSP106370:FRANCCI3_3897-MON.
Family and domain databases
HAMAP	MF_00452. [Tree]
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. 1 hit. 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.
ProDom	PD004738. PEPCK_N. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00505. PEPCK_GTP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PCKG_FRASC

Accession

Primary (citable) accession number: Q2J645

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	March 7, 2006
Last modified:	June 16, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)