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A0QP32 (PCKG_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:MSMEG_0255, MSMEI_0248
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium ›

Protein attributes

Sequence length608 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. HAMAP-Rule MF_00452

Catalytic activity

GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2. HAMAP-Rule MF_00452

Cofactor

Binds 1 manganese ion per subunit By similarity.

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP-Rule MF_00452

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the phosphoenolpyruvate carboxykinase [GTP] family.

Ontologies

Keywords
   Biological processGluconeogenesis
   Cellular componentCytoplasm
   LigandGTP-binding
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionDecarboxylase
Lyase
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgluconeogenesis

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: HAMAP

manganese ion binding

Inferred from electronic annotation. Source: HAMAP

phosphoenolpyruvate carboxykinase (GTP) activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 608608Phosphoenolpyruvate carboxykinase [GTP] HAMAP-Rule MF_00452
PRO_1000060292

Regions

Nucleotide binding272 – 2776GTP By similarity
Nucleotide binding514 – 5174GTP By similarity
Region386 – 3883Substrate binding By similarity

Sites

Active site2731 By similarity
Metal binding2291Manganese By similarity
Metal binding2491Manganese By similarity
Metal binding2961Manganese By similarity
Binding site811Substrate By similarity
Binding site2221Substrate; via amide nitrogen By similarity
Binding site2291Substrate By similarity
Binding site2711Substrate By similarity
Binding site3881GTP By similarity
Binding site4191GTP By similarity

Amino acid modifications

Cross-link485Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) HAMAP-Rule MF_00452

Sequences

Sequence LengthMass (Da)Tools
A0QP32 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 42835F8DBA46DE0E

FASTA60867,297
        10         20         30         40         50         60 
MTSATIPGLD TAPTKHQGLL AWVQEVAELT QPDRVVFADG SDEEYERLCA HLVEAGTFQK 

        70         80         90        100        110        120 
LNPEKQPNSY LALSDPSDVA RVESRTFICT EREIDAGPTN NWMDPAEMRG IMTDLYRGSM 

       130        140        150        160        170        180 
RGRTLYVVPF CMGPLDAEDP KLGVEITDSE YVVVSMRTMT RMGRAALDKL GDDGFFVKAL 

       190        200        210        220        230        240 
HSIGAPLEPG QKDVPWPCND TKYITHFPET REIWSFGSGY GGNALLGKKC YSLRIASAMA 

       250        260        270        280        290        300 
HDEGWLAEHM LILKLISPEN KAYFIAAAFP SACGKTNLAM LQPTIEGWRA ETVGDDIAWM 

       310        320        330        340        350        360 
RFGKDGRLYA TNPEFGFFGV APGTNWSSNP NAMKTIAAGN TVFTNVAKTD DGDVWWEGLE 

       370        380        390        400        410        420 
GDPQHLIDWK GNDWTPESGE KAAHPNSRYC TPISQCPTLA PEWDDPQGVP ISAILFGGRR 

       430        440        450        460        470        480 
KTTVPLITEA RDWQHGVFIG ATLGSEQTAA AEGKVGTVRR DPMAMLPFLG YNVGDYFAHW 

       490        500        510        520        530        540 
INVGKNADES KLPKVFFVNW FRRGDDGRFL WPGFGENSRV LKWAVERIEH KADGKSTPIG 

       550        560        570        580        590        600 
IVPTAADLDL EGLDVDPADV DEALAVKPEE WRAELPLIEE WFEFVGEKLP TGLKDEFDAL 


KHRLSEEG

« Hide

References

« Hide 'large scale' references
[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[2]"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[3]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[4]"Expansion of the mycobacterial 'PUPylome'."
Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V., Barry C.E. III, Bark S., Dorrestein P.C.
Mol. Biosyst. 6:376-385(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PUPYLATION AT LYS-485, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000480 Genomic DNA. Translation: ABK74449.1.
CP001663 Genomic DNA. Translation: AFP36729.1.
RefSeqYP_006565024.1. NC_018289.1.
YP_884670.1. NC_008596.1.

3D structure databases

ProteinModelPortalA0QP32.
SMRA0QP32. Positions 12-605.
ModBaseSearch...

Protein-protein interaction databases

STRING246196.MSMEG_0255.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK74449; ABK74449; MSMEG_0255.
GeneID13426770.
4531575.
KEGGmsg:MSMEI_0248.
msm:MSMEG_0255.
PATRIC18072977. VBIMycSme59918_0251.

Phylogenomic databases

eggNOGCOG1274.
HOGENOMHOG000191700.
KOK01596.
OMAWMRFGED.
ProtClustDBPRK04210.

Enzyme and pathway databases

BioCycMSME246196:GJ4Y-255-MONOMER.
UniPathwayUPA00138.

Family and domain databases

Gene3D3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPMF_00452. PEPCK_GTP.
InterProIPR018091. PEP_carboxykin_GTP_CS.
IPR013035. PEP_carboxykinase_C.
IPR008209. PEP_carboxykinase_GTP.
IPR008210. PEP_carboxykinase_N.
[Graphical view]
PANTHERPTHR11561. PTHR11561. 1 hit.
PfamPF00821. PEPCK. 1 hit.
[Graphical view]
PIRSFPIRSF001348. PEP_carboxykinase_GTP. 1 hit.
SUPFAMSSF68923. PEP_carboxykinase_N. 1 hit.
PROSITEPS00505. PEPCK_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePCKG_MYCS2
AccessionPrimary (citable) accession number: A0QP32
Secondary accession number(s): I7G2R6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 9, 2007
Last modified: May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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