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F0RJT2 (F0RJT2_DEIPM) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length842 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle By similarity. HAMAP-Rule MF_00595 SAAS SAAS022805

Catalytic activity

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-. HAMAP-Rule MF_00595 SAAS SAAS021135

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00595 SAAS SAAS021135

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00595

Sequence similarities

Belongs to the PEPCase type 1 family. HAMAP-Rule MF_00595

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1311 By similarity HAMAP-Rule MF_00595
Active site5081 By similarity HAMAP-Rule MF_00595

Sequences

Sequence LengthMass (Da)Tools
F0RJT2 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: C54F310A9DFA3CF3

FASTA84293,075
        10         20         30         40         50         60 
MALNRDVSTL GRLLGQVLRE QEGEAFFELV EKTRALVREV RAGGDSAELS GLLRGLSREE 

        70         80         90        100        110        120 
ASNLARAFSW YFQLVNLAEE YERVRVLRER QGTRPQSLLQ AVEELHRQGL SAAEAHELLA 

       130        140        150        160        170        180 
TLQLELTFTA HPTEMRRRTV RQHLVDVVEQ LPRLDEEEAQ ERVLAHIEAL WGTPELRRIK 

       190        200        210        220        230        240 
PTVADEVKAG LTYISSIARA LPVLERDLDR AFAAVYGERG AAGISTQLPL RFSSWMGGDR 

       250        260        270        280        290        300 
DGNPFVTPQA TRAALELHRQ RARDLLAAAL RQAYADVSQE DLQAGEGQPT YRDELLALFQ 

       310        320        330        340        350        360 
AVQRGEAADL SPRLGRVYRQ LLEQGQRRTA EELLLPALTL ARVFGQHLVS LDIREHSSQT 

       370        380        390        400        410        420 
GRAVAELLQA SGVTQDYLAL DEDARLALLS AELRSRRPLW PAGEPLTETL ETAIGPIREV 

       430        440        450        460        470        480 
QAAAREVGPA AFGHYVVSMS ESVSDVLEPL LLAREVGFRI LPVPLFETLD DLEGAPDIVA 

       490        500        510        520        530        540 
RLLALPEYRA HLGSDVQEIM LGYSDSNKDA GFLAANWALH EAQRRISAVC REAGVRWRFF 

       550        560        570        580        590        600 
HGRGTSIGRG GGPASRAILG QPAGTIDAGL RITEQGEALA DKYSHPVLAR RNLEQALYGM 

       610        620        630        640        650        660 
IVAAARPPQD PPAEWMDALD RAARAAAAAY RAFVQDPAFL PFFEQVTPIH EISRLNIASR 

       670        680        690        700        710        720 
PVRRPGNPTL SNLRAIPWVM SWTQTRANLP GWYGLNIGLR EIGTEQARQM YAEWPFFRAV 

       730        740        750        760        770        780 
LDNAQMSLAK TDPAIFREYA ALLAGADTPE AVEGGRALAG IIEEAYRDTV ALVGEVVGGE 

       790        800        810        820        830        840 
LLAREPRLAQ SILLRNPYVD PIHRIQIELL RRARAEEGGL DRYEHALMLT LQGISAGVRN 


TG

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References

[1]"The complete sequence of chromosome of Deinococcus proteolyticus DSM 20540."
US DOE Joint Genome Institute (JGI-PGF)
Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F. expand/collapse author list , Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P., Eisen J.A.
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002536 Genomic DNA. Translation: ADY25558.1.
RefSeqYP_004255175.1. NC_015161.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADY25558; ADY25558; Deipr_0388.
GeneID10255855.
KEGGdpt:Deipr_0388.
PATRIC46928532. VBIDeiPro159979_0382.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01595.

Enzyme and pathway databases

BioCycDPRO693977:GCFA-405-MONOMER.

Family and domain databases

HAMAPMF_00595. PEPcase_type1.
InterProIPR021135. PEP_COase.
IPR018129. PEP_COase_AS.
IPR022805. PEP_COase_bac/pln-type.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamPF00311. PEPcase. 2 hits.
[Graphical view]
PRINTSPR00150. PEPCARBXLASE.
SUPFAMSSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
PROSITEPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF0RJT2_DEIPM
AccessionPrimary (citable) accession number: F0RJT2
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: May 29, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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