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

A1WZE2 (A1WZE2_HALHL) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 50. Feed History...

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

Protein attributes

Sequence length883 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 SAAS021135

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 site1451 By similarity HAMAP-Rule MF_00595
Active site5511 By similarity HAMAP-Rule MF_00595

Sequences

Sequence LengthMass (Da)Tools
A1WZE2 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 92399F06BB33971E

FASTA883100,294
        10         20         30         40         50         60 
MEEHQDSDSA LREDIRDLGE LLGATLREQG GTELFETVER VRVLAKTARA GDDQAAQELE 

        70         80         90        100        110        120 
RTLSELPPEQ VTPVARAFSQ FLNLANIAEQ HHRVRRSREW ARTPEAQPLF GSLAETVPRL 

       130        140        150        160        170        180 
AADMEPEQLH EAICSMDINL VFTAHPTEVQ RRTMLQKYNR IAGLLDNRDR FGQTPTEVAE 

       190        200        210        220        230        240 
TRLALKREIT AAWHSDEIRR RRPTPQDEAR WGLAVVEQTL WDAVPRYLRS LDHTLREHTG 

       250        260        270        280        290        300 
RPLPLDCAPI TFGSWMGGDR DGNPNVTHRV TRDVAILSRW MAAYLYERDI QRLVSTLSLQ 

       310        320        330        340        350        360 
VCDDELRDEV GGEAWEPYRV VLKRLRARLR QTMRWAEAKL QGGRPPESDI LTEVEDLRQP 

       370        380        390        400        410        420 
LLRCYYSLQR VGAGVVAEGE LLDTIRRVSC FGLTLMPMDI RQHADRHTAA LDAITQAVGL 

       430        440        450        460        470        480 
GSYSEWDEET RQQWLFQELS HRRPLIPLDF KPEREVQEVL DTIHMLEEIG PDAVGAYIVS 

       490        500        510        520        530        540 
HASKPSDILA VELLQKECGL THPTRVVPLF ETRDTLARAA DTMEVLFKSD WYRQRIGGRQ 

       550        560        570        580        590        600 
EIMIGYSDST KDAGHLTATW TLYQAQEQLV ALSRRQRVDL TLFHGRGGSI GRGGGPTHAA 

       610        620        630        640        650        660 
ILAQPPGSVD GTLRVTEQGE VMQAKFGLPG IALRNLELYT TSVLEATVRP PEPPPKRWRE 

       670        680        690        700        710        720 
ILERLSDRAM TAYRQTVKER PEFMDYFQAA TPIDEISRLT IGSRPAKRAP DQMTVDSLRA 

       730        740        750        760        770        780 
IPWVFAWTQT RLMLPAWLGV GEALEEAIEE GLTEELQEMF ARWPFFEAFL DMVEMVVAKA 

       790        800        810        820        830        840 
EPGVNRLYEH ALVPDELHSV GDELRDRFAR TRDAVLTVTG HEEPLSDFPV VKRAVEVRNP 

       850        860        870        880 
YVDPLNLLQV ELLRRSRMCE DDSLRRGLQV VINGIAAGMR NTG 

« Hide

References

[1]"Complete sequence of Halorhodospira halophila SL1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 244 / SL1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000544 Genomic DNA. Translation: ABM63054.1.
RefSeqYP_001003856.1. NC_008789.1.

3D structure databases

ProteinModelPortalA1WZE2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349124.Hhal_2291.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM63054; ABM63054; Hhal_2291.
GeneID4709455.
KEGGhha:Hhal_2291.
PATRIC22098887. VBIHalHal112047_2268.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2352.
HOGENOMHOG000238648.
KOK01595.
OMAAIPWVFG.
OrthoDBEOG6TJ7T8.
ProtClustDBPRK00009.

Enzyme and pathway databases

BioCycHHAL349124:GI3I-2344-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. 1 hit.
[Graphical view]
PRINTSPR00150. PEPCARBXLASE.
SUPFAMSSF51621. SSF51621. 1 hit.
PROSITEPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA1WZE2_HALHL
AccessionPrimary (citable) accession number: A1WZE2
Entry history
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)