Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q65FV7 (PCKA_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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 [ATP]

Short name=PCK
Short name=PEP carboxykinase
Short name=PEPCK
EC=4.1.1.49
Gene names
Name:pckA
Ordered Locus Names:BLi03197, BL00839
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA By similarity. HAMAP-Rule MF_00453

Catalytic activity

ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO2. HAMAP-Rule MF_00453

Cofactor

Binds 1 manganese ion per subunit By similarity. HAMAP-Rule MF_00453

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP-Rule MF_00453

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00453.

Sequence similarities

Belongs to the phosphoenolpyruvate carboxykinase [ATP] family.

Ontologies

Keywords
   Biological processGluconeogenesis
   Cellular componentCytoplasm
   LigandATP-binding
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoenolpyruvate carboxykinase (ATP) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 527527Phosphoenolpyruvate carboxykinase [ATP] HAMAP-Rule MF_00453
PRO_0000236919

Regions

Nucleotide binding233 – 2419ATP By similarity

Sites

Metal binding1981Manganese By similarity
Metal binding2171Manganese; via tele nitrogen By similarity
Metal binding2541Manganese By similarity
Binding site561Substrate By similarity
Binding site1921Substrate By similarity
Binding site1981ATP By similarity
Binding site1981Substrate By similarity
Binding site2171ATP By similarity
Binding site2821ATP By similarity
Binding site3191ATP By similarity
Binding site3191Substrate By similarity
Binding site4441ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65FV7 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: BE2002BCB9FF58C0

FASTA52758,167
        10         20         30         40         50         60 
MNSVDLTTDL QTLLTGENVQ MNLSVPHLVE KILERKEGVL TSSGAVRATT GTYTGRSPKD 

        70         80         90        100        110        120 
KFIVEEASTK DKIDWGAVNQ PISEAAFDRL YAKVLGYLKE RDELYVFEGF AGADEKYRLP 

       130        140        150        160        170        180 
ITVVNEFAWH NLFARQLFIR PEEHDKKPEE QPFTILSAPH FKADPLVDGT RSETFIIVSF 

       190        200        210        220        230        240 
EKRTILIGGT EYAGEMKKSI FSIMNFLLPE QNILPMHCSA NIGEEGGTAL FFGLSGTGKT 

       250        260        270        280        290        300 
TLSADPKRKL IGDDEHGWSS TGVFNIEGGC YAKCINLSEE KEPQIYNAIR FGSVLENVVV 

       310        320        330        340        350        360 
DSKTGEPDYS DSFYTENTRA AYPIDAIDNI VKPSIAAHPQ TIVFLTADAF GVLPPISKLT 

       370        380        390        400        410        420 
KEQAMYHFLS GYTSKLAGTE RGITTPEATF STCFGSPFLP LPAHVYAEML GRKIDEHGVG 

       430        440        450        460        470        480 
VFLVNTGWTG GGYGTGERMS LAYTRAMVQA AIEGELDKAE MRTDRIFGLH SPVHVPGVPD 

       490        500        510        520 
QVLDPAKTWT DENEYEEKAI HLAKAFKQNF KKFSNTENIE KAGGPLV 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU42057.1.
CP000002 Genomic DNA. Translation: AAU24695.1.
RefSeqYP_006714528.1. NC_006322.1.
YP_080333.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65FV7.
SMRQ65FV7. Positions 16-523.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL00839.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU24695; AAU24695; BL00839.
AAU42057; AAU42057; BLi03197.
GeneID3027890.
3099051.
KEGGbld:BLi03197.
bli:BL00839.
PATRIC18952140. VBIBacLic203714_3270.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1866.
HOGENOMHOG000271471.
KOK01610.
OMAGADPEHY.
OrthoDBEOG6DG2RK.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-3168-MONOMER.
UniPathwayUPA00138.

Family and domain databases

Gene3D3.40.449.10. 1 hit.
3.90.228.20. 2 hits.
HAMAPMF_00453. PEPCK_ATP.
InterProIPR001272. PEP_carboxykinase_ATP.
IPR013035. PEP_carboxykinase_C.
IPR008210. PEP_carboxykinase_N.
[Graphical view]
PfamPF01293. PEPCK_ATP. 1 hit.
[Graphical view]
PIRSFPIRSF006294. PEP_crbxkin. 1 hit.
SUPFAMSSF68923. SSF68923. 1 hit.
TIGRFAMsTIGR00224. pckA. 1 hit.
ProtoNetSearch...

Entry information

Entry namePCKA_BACLD
AccessionPrimary (citable) accession number: Q65FV7
Secondary accession number(s): Q62RB5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways