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E4QAT8 (E4QAT8_CALH1) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 20. 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 length663 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) By similarity. SAAS SAAS003451

Catalytic activity

Dimethylallyl diphosphate + NAD(P)+ + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. SAAS SAAS003451

Isopentenyl diphosphate + NAD(P)+ + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. SAAS SAAS003451

Cofactor

Binds 1 3Fe-4S cluster per subunit By similarity. SAAS SAAS003451

Pathway

Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1. SAAS SAAS003451

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 6/6. SAAS SAAS003451

Sequences

Sequence LengthMass (Da)Tools
E4QAT8 [UniParc].

Last modified February 8, 2011. Version 1.
Checksum: FD8E06207CDF0027

FASTA66375,866
        10         20         30         40         50         60 
MIIKVAQSAG FCFGVQRAVE GVLAWAKANK GKSIKVYGML IHNSYVIDKL KDLGVEVIED 

        70         80         90        100        110        120 
IEQIGREDIV FIRSHGVSME EYAEIEKRAE KVYDFTCPYV KKIHEIVKEH SENGYDIIVV 

       130        140        150        160        170        180 
GDMNHPEVKG IVGHVSNNRK CFVVDSIEKV KEAINQIEGK AAVVCQTTFD SKKWSDIREF 

       190        200        210        220        230        240 
LETHTNYKVF DTICKATINR QKEAQELAKH VDMMLVVGDK KSSNTNKLYQ LLKEIKPTFF 

       250        260        270        280        290        300 
IDKVEDLDSI KLDSHIKSIG VTAGASTSPE QIEEVVKHLE EKFNEMSLKD FERFIGRNFL 

       310        320        330        340        350        360 
TVQRGEVVKG RIIKVEEDYV LVDIGYKAEG IIYKDEVIKN GNVNLKDLFK IGETIEAVVI 

       370        380        390        400        410        420 
KESDEEGNVV LSKYRADVLH GFEELLSKYE NKESVRVVVK SIKEKSIVCD FRGTNVYVPI 

       430        440        450        460        470        480 
SQWGEDLQTS DIGKIFEIEI TDVNKEKKIA FGSRKSLLKQ KEEERFIKQI ESLDFSREYE 

       490        500        510        520        530        540 
GIIAEIKQKG IVVNFENLRG FVPASEVGYL KKGADLKKLF EIGEKVKVKI LDIDKNKKQI 

       550        560        570        580        590        600 
YLSIKKTQDD EWIKKIKNLY LGMLVDCEVT KVLPFGLVVW ITEHDVDGFV HISNIPLGYN 

       610        620        630        640        650        660 
QRPHNVYKVG DSLRAKVIEI DEEKRRVALS LKDLHEEENI DTEHNEDFVI TLADFVKNIK 


LEQ 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of Caldicellulosiruptor hydrothermalis 108."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N. expand/collapse author list , Blumer-Schuette S.E., Kelly R.M., Woyke T.
Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 108.
[2]"Complete genome sequences for the anaerobic, extremely thermophilic plant biomass-degrading bacteria Caldicellulosiruptor hydrothermalis, Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis, Caldicellulosiruptor owensensis, and Caldicellulosiruptor lactoaceticus."
Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A., Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T., Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C., Walston-Davenport K., Han S., Adams M.W., Kelly R.M.
J. Bacteriol. 193:1483-1484(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 18901 / VKM B-2411 / 108.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002219 Genomic DNA. Translation: ADQ07116.1.
RefSeqYP_003992485.1. NC_014652.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADQ07116; ADQ07116; Calhy_1399.
GeneID9935950.
KEGGchd:Calhy_1399.
PATRIC42586445. VBICalHyd101559_1486.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000057927.
KOK02945.
K03527.
OMAKLIEDPW.

Enzyme and pathway databases

BioCycCHYD632292:GHA8-1442-MONOMER.
UniPathwayUPA00056; UER00097.
UPA00059; UER00105.

Family and domain databases

Gene3D2.40.50.140. 3 hits.
HAMAPMF_00191. IspH.
InterProIPR003451. LytB.
IPR012340. NA-bd_OB-fold.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR000110. Ribosomal_S1.
IPR022967. RNA-binding_domain_S1.
[Graphical view]
PfamPF02401. LYTB. 1 hit.
PF00575. S1. 3 hits.
[Graphical view]
PRINTSPR00681. RIBOSOMALS1.
SMARTSM00316. S1. 4 hits.
[Graphical view]
SUPFAMSSF50249. Nucleic_acid_OB. 4 hits.
TIGRFAMsTIGR00216. ispH_lytB. 1 hit.
PROSITEPS50126. S1. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE4QAT8_CALH1
AccessionPrimary (citable) accession number: E4QAT8
Entry history
Integrated into UniProtKB/TrEMBL: February 8, 2011
Last sequence update: February 8, 2011
Last modified: May 1, 2013
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)