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

A0LTY9 (A0LTY9_ACIC1) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 53. 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·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length692 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate By similarity. RuleBase RU004996

Catalytic activity

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate. RuleBase RU004996

Cofactor

Binds 1 magnesium ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+ By similarity. RuleBase RU004996

Binds 1 thiamine pyrophosphate per subunit By similarity. RuleBase RU004996

Subunit structure

Homodimer By similarity. RuleBase RU004996

Sequence similarities

Belongs to the transketolase family. RuleBase RU004996

Sequences

Sequence LengthMass (Da)Tools
A0LTY9 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: C503BEE17193683C

FASTA69275,276
        10         20         30         40         50         60 
MTEHDTVEWT ELDARAVDII RALAMDAVEA AGSGHPGTAM GLAPAAYLLF QRLLRHDPTD 

        70         80         90        100        110        120 
PRWLGRDRFV LSCGHSSLTL YIQLYLSGYG LTLDDLRSYR QWGSLTPGHP EYGHTPGVET 

       130        140        150        160        170        180 
TTGPLGQGFG NAVGMAMAAR RERGLFDPDA APGSSVFDHT IWVFASDGDI EEGVQAEAAA 

       190        200        210        220        230        240 
IAGHQQLGNL VVLYDDNRIS IEGDTRVAHS EDVGKRYEAY GWHVQHVADV NDVQALYRAL 

       250        260        270        280        290        300 
VTARDTTDRP SLVIVRSIIA WPAPNLQNTG KAHGSALGAE EVAATKRVLG LDPEKTFYVP 

       310        320        330        340        350        360 
DDVLSHARQV VDRGRLAHKE WQERFEAWRA AHPQRAAELD RMLARRLPEG WDADIPHFAP 

       370        380        390        400        410        420 
DKPMSTRKAS GVVINALAKK LPELWGGSAD LAESNNTTIE GERDFLPAAH GGDPYGRVLH 

       430        440        450        460        470        480 
FGIREHAMGA ILNGITLHGP TRVFGGTFLV FSDYMRPPVR LAAMMKLPVI YVWTHDSIGL 

       490        500        510        520        530        540 
GEDGPTHQPV EHLAALRAIP GLDVVRPADA NETAVAWRTI MQQTDRPAAL CLTRQNVPVI 

       550        560        570        580        590        600 
DRTQYASADG TAKGAYVLAE AGSGAPQVIL IATGSEVHLA LAARERLEAD GVPTRVVSMP 

       610        620        630        640        650        660 
CREWFEAQPE SYRRTVLPDD VRARVSIEAA VALGWRDYVG DFGECVSLEH FGASASYQVL 

       670        680        690 
FEQFGFTPER VVAAAHASMA RVRAAGLPVL GS 

« Hide

References

[1]"Complete sequence of Acidothermus cellulolyticus 11B."
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., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43068 / 11B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000481 Genomic DNA. Translation: ABK52899.1.
RefSeqYP_872885.1. NC_008578.1.

3D structure databases

ProteinModelPortalA0LTY9.
SMRA0LTY9. Positions 11-676.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351607.Acel_1127.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK52899; ABK52899; Acel_1127.
GeneID4485183.
KEGGace:Acel_1127.
PATRIC20672712. VBIAciCel132453_1193.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0021.
HOGENOMHOG000225954.
KOK00615.
OMASAPCLEW.
OrthoDBEOG6N3CRG.

Enzyme and pathway databases

BioCycACEL351607:GIXW-1152-MONOMER.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005478. Transketolase_bac-like.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsTIGR00232. tktlase_bact. 1 hit.
PROSITEPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA0LTY9_ACIC1
AccessionPrimary (citable) accession number: A0LTY9
Entry history
Integrated into UniProtKB/TrEMBL: December 12, 2006
Last sequence update: December 12, 2006
Last modified: June 11, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)