Reviewed, UniProtKB/Swiss-Prot Q0RCJ7 (PCKG_FRAAA)

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:	FRAAL6204

Organism

Frankia alni (strain ACN14a) [Complete proteome] [HAMAP]

Taxonomic identifier

326424 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	607 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 – 607	607	Phosphoenolpyruvate carboxykinase [GTP] HAMAP MF_00452		PRO_1000060289
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)
	Q0RCJ7-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 01D266786EDFF796	FASTA	607	66,582
	10 20 30 40 50 60 MTTAAQIPGL EAAPTKHARL VAWVREIAEL TQPERVEWCD GSEAEFDRLT SLLIEKGTLV 70 80 90 100 110 120 RLNDEKRPNS FYAASDPSDV ARVEDRTYIC SEKAEDAGPT NNWMDPAEMR VKLQGLFEGS 130 140 150 160 170 180 MRGRTMYVVP FCMGPLGSHI SALGVEITDS PYVVISMRTM TRMGAPALEQ LGEDGFFVPA 190 200 210 220 230 240 VHSLGAPLES GAADVPWPCN TTKYITHFPE TREIWSYGSG YGGNALLGKK CYALRIASVM 250 260 270 280 290 300 ARDEGWLAEH MLILKLTSPA GKVHYIAAAF PSACGKTNLA MLIPTLPGWK AETVGDDIAW 310 320 330 340 350 360 MRFGEDGRLY AVNPEAGFFG VAPGTGEQTN PNAIKTLWGN TVFTNVARTD DGDVWWEGLT 370 380 390 400 410 420 KQAPGHLTDW KGRDWTPEST EPAAHPNARF TVPAGQCPTI ASEWQDPKGV PISAILFGGR 430 440 450 460 470 480 RATAVPLVTE APDWRRGVFF GSIVASETTA AQAGAIGKLR RDPFAMLPFC GYNMADYFAH 490 500 510 520 530 540 WLEVGQKADQ AKLPRIYYVN WFRKSPEGKF LWPGFGENSR VLAWIVGRLE GHADGVETPL 550 560 570 580 590 600 GVLPTRDALP TDGLQIDEAD LDALLTVDID VWKQEAELIP EHYQTFGDRL PAALWAEHEA LVSRLDG

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	CT573213 Genomic DNA. Translation: CAJ64827.1.
RefSeq	YP_716342.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4233718.
GenomeReviews	Gene locus FRAAL6204 in contig CT573213_GR.
KEGG	fal:FRAAL6204.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	Q0RCJ7. SHPNARF.
Enzyme and pathway databases
BioCyc	FALN326424:FRAAL6204-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_FRAAA

Accession

Primary (citable) accession number: Q0RCJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 23 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)