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H2H669 (H2H669_CORDD) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length917 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. SAAS SAAS022805 HAMAP-Rule MF_00595

Catalytic activity

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

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 site1471 By similarity HAMAP-Rule MF_00595
Active site5761 By similarity HAMAP-Rule MF_00595

Sequences

Sequence LengthMass (Da)Tools
H2H669 [UniParc].

Last modified March 21, 2012. Version 1.
Checksum: C01FB9F9BE95BD04

FASTA917102,829
        10         20         30         40         50         60 
MGTLCIHHFC RKAELVTAAI SDRVREDIRL LGRVLGRVIV QQEGEEVYEL VEATRRMAFD 

        70         80         90        100        110        120 
VFHGDADPED LMVIFRDLDI TKTNLVARAF SYFALLANLA EDLDDESVEA DVSLRKTFAK 

       130        140        150        160        170        180 
LKQEGVSAAD AASVIRSAEV APVLTAHPTE TRRRTVFDTQ TRIKQLLKDA HHGGDMQVIE 

       190        200        210        220        230        240 
QEMYLRMTLL WQTALIRIAR PTLEDEIDVG LRYYKKSLLE QVPALNRSIR HSMRETFGLQ 

       250        260        270        280        290        300 
LPDIAVMRPG SWIGGDHDGN PYVNARTLTY ATRQAAKTVA RYYVEQLGEL ERELSLSDRY 

       310        320        330        340        350        360 
SSCSKELLAL AEASGNNWES RVDEPYRRAV YGMRARMKSN VDALERPEKT AGKKSSKRTP 

       370        380        390        400        410        420 
YATPEEFLRD LDVIDRSLRA HNDDVIADDR LARIRSAVTT FGFHLYTLDI RQNSESFEAV 

       430        440        450        460        470        480 
IEEVFAAARR VPGGKRYSEL AETEKVELLI QELQTPRPLL FPGALEVEDA FSADTTKELG 

       490        500        510        520        530        540 
IFLAAAQAVR DFGSRSIAHC IISMTATVSD ILEPMVLLKE VGLRDVDVVP LFETIDDLRC 

       550        560        570        580        590        600 
GAAILRELWS HPFYREHLRA RGDIQEVMLG YSDSNKDGGY LQANWALYDA ELGLVELCRE 

       610        620        630        640        650        660 
HNIELRLAHG RGGAVGRGGG PTYDAILAQP KGAVSGSVRI TEQGEVISAK YGAPETARRH 

       670        680        690        700        710        720 
LEAFVSGALE ASLLDTEPIA DPDRAYAIMR DLAGFSGQRY QELVGDPGFI EYFTQSTPLH 

       730        740        750        760        770        780 
EIGELNLGSR PAARKQTTAI SDLRAIPWVL SWSQSRTNIP GWFGVGSAVS RFVSAVPEKD 

       790        800        810        820        830        840 
RESRWQELRD LYATWPFFRS VMSNMAQVMA KAEISLARLY ADLVDDPEVA DRIYALIAEE 

       850        860        870        880        890        900 
FELTRRAYLA ITGNEALVSE NQRQARSLKR RYPYLLPLNA IQLELLRRYR GGDDQFLVSK 

       910 
TIQVTMNGLA TALRNAG 

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References

[1]"Pangenomic Study of Corynebacterium diphtheriae That Provides Insights into the Genomic Diversity of Pathogenic Isolates from Cases of Classical Diphtheria, Endocarditis, and Pneumonia."
Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., Santos C.S., Santos L.S., Hirata R.Jr. expand/collapse author list , Mattos-Guaraldi A.L., Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.
J. Bacteriol. 194:3199-3215(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDCE 8392 EMBL AEX72017.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003211 Genomic DNA. Translation: AEX72017.1.
RefSeqYP_005133565.1. NC_016785.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEX72017; AEX72017; CDCE8392_1024.
GeneID11705606.
KEGGcdd:CDCE8392_1024.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01595.

Enzyme and pathway databases

BioCycCDIP698965:GHJP-1049-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 nameH2H669_CORDD
AccessionPrimary (citable) accession number: H2H669
Entry history
Integrated into UniProtKB/TrEMBL: March 21, 2012
Last sequence update: March 21, 2012
Last modified: April 16, 2014
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)