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Reviewed, UniProtKB/Swiss-Prot Q9U720 (DCSA_DICDI)

Last modified June 16, 2009. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cellulose synthase catalytic subunit A [UDP-forming]
    EC=2.4.1.12
Gene names
Name: dcsA
ORF Names: DDB_G0269124
OrganismDictyostelium discoideum (Slime mold) [Complete proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length1059 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose, which is produced as an extracellular component for mechanical and chemical protection at the onset of the stalk formation, when the cells exhibit multicellular behavior during culmination. Ref.1

Catalytic activity

UDP-glucose + (1,4-beta-D-glucosyl)(n) = UDP + (1,4-beta-D-glucosyl)(n+1).

Cofactor

Magnesium By similarity.

Pathway

Glycan metabolism; amoeba cellulose biosynthesis.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Developmental stage

Progressively accumulates during culmination, especially at the onset of the stalk formation. Present in fruiting body (at protein level). Ref.1

Domain

There are two conserved domains in the globular part of the protein: the N-terminal domain (domain A) contains the conserved DXD motif and is possibly involved in catalysis and substrate binding. The C-terminal domain (domain B) contains the QXXRW motif and is present only in processive glycosyl transferases. It could be involved in the processivity function of the enzyme, possibly required for holding the growing glycan chain in the active site.

Miscellaneous

Amoebae missing dcsA exhibit snowmen-shaped fruiting bodies.

Sequence similarities

Belongs to the glycosyltransferase 2 family.

Ontologies

Keywords
   Biological processCellulose biosynthesis
   Cellular componentMembrane
   DomainTransmembrane
   Molecular functionDevelopmental protein
Glycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcellulose biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncellulose synthase (UDP-forming) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10591059Cellulose synthase catalytic subunit A [UDP-forming]
PRO_0000327825

Regions

Transmembrane246 – 26621 Potential
Transmembrane280 – 30021 Potential
Transmembrane306 – 32318 Potential
Transmembrane790 – 81021 Potential
Transmembrane813 – 83321 Potential
Transmembrane963 – 98321 Potential
Transmembrane993 – 101321 Potential
Transmembrane1035 – 105521 Potential
Region328 – 628301Catalytic subdomain A By similarity
Region701 – 76161Catalytic subdomain B By similarity

Sites

Active site3701 Potential
Active site7171 Potential
Binding site6241Substrate Potential
Binding site6261Substrate Potential

Sequences

Sequence LengthMass (Da)Tools
Q9U720-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 2CF8A701D7D99B81

FASTA1,059121,412
        10         20         30         40         50         60 
MDRNEGGDFP INTPNNINSS GGSYNNSMNN SSNNIGRDIG NNQSSRNLKP KPSQSNLKWI 

        70         80         90        100        110        120 
ARDLKKKSVR KDSERKLKSS GVLKKKNTVM DFGEDDGGSG DDGNITEGLP ISEGMDDLPS 

       130        140        150        160        170        180 
SSNSRGGSGN DEQKKQFPKE MNSPSSEYGT TSGGQRFDTL VDPDISLAEM EEKMRQHKVY 

       190        200        210        220        230        240 
QEQQQQQQQQ QQQQKQKDKE LSSQKKKPSS MQLSKKKHVA KEDSETLETI IGEEKKEVVF 

       250        260        270        280        290        300 
EVKPYFSHAI LQATMAVFLI WNIFYFAYRA GWTMNRTDYI TFSYSILFII VEFISFLGSA 

       310        320        330        340        350        360 
LHLNNFTNPC TFVLVVTLEQ ILAKRRKKHP TVMMYVCTYK EPPSIVSRTF RTAISMDYPS 

       370        380        390        400        410        420 
ENLWIGLLDD SVNYRESRGW AHLQSVEKNF LYVLLQKAVY SVHNIRPPVT SQHEDPHGIL 

       430        440        450        460        470        480 
NETSSKIESS TKEVIEAEVQ WFIEYFLLNS WFGVGQEIPR DADDAERALI AKLRDDNFSP 

       490        500        510        520        530        540 
YRTFTKSESE KISNFTIDSL QSLWHGSAFF RPLIRSILLK KDYVRNFVSE LNNQHRLRFL 

       550        560        570        580        590        600 
NTEALAMAQY QVLMMGRQEL PWDEISSGNV RIDFDTCDGP IVSPKCTYLR RRKPPIPHNK 

       610        620        630        640        650        660 
AGNINNALFN ESTKADYEFL GLLDADQQPH PDFLKRVLPY FYSDEGQDLA FVQTPQFFSN 

       670        680        690        700        710        720 
IYPVDDPLGH RNMEFYGPVM EGRSANNACP FVGTNAIFRR QPLYDIGGIM YNSVTEDMYT 

       730        740        750        760        770        780 
GMKLQVSGYK SWYHNEVLVV GTAPVDLKET LEQRKRWAQG AVEIFSLTPW GYIRGKLGWR 

       790        800        810        820        830        840 
KMLYNLDSCI YPFLSPTAFF YGASPLIMSI WTVPIVVKDP IIFILVGMIP VMVLPRVIQY 

       850        860        870        880        890        900 
MILRAKRPYE AGKSGPSLWV EATDLWRAEQ TFFGFAGTYI SSWREGSASI VKLLKARKIS 

       910        920        930        940        950        960 
RHKLAMWNWK RDFVKKPVVC EVFRQTKLVN ENDNAQESSG KHKAEQSFRT SNKESDTIKN 

       970        980        990       1000       1010       1020 
SRLFLPNIIL FVVNILAMMS AVLRFNCFQN DMWLLVVVAG FSFSTLWHLW SFIPMALRQS 

      1030       1040       1050 
EKQWPYASSY HAHNIVLFLV LGFLVLLFVD VKVCIPRVG 

« Hide

References

« Hide 'large scale' references
[1]"The cellulose synthase gene of Dictyostelium."
Blanton R.L., Fuller D., Iranfar N., Grimson M.J., Loomis W.F.
Proc. Natl. Acad. Sci. U.S.A. 97:2391-2396(2000) [PubMed: 10681463] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
Strain: AX4.
[2]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed: 15875012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF163835 mRNA. Translation: AAF00200.1.
AAFI02000005 Genomic DNA. Translation: EAL71912.1.
RefSeqXP_646256.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

Genome annotation databases

GeneID3397696.
KEGGddi:DDB_0191159.

Organism-specific databases

dictyBaseDDB_G0269124. dcsA.

Enzyme and pathway databases

BRENDA2.4.1.12. 424.

Family and domain databases

InterProIPR005150. Cellulose_synth.
IPR001173. Glyco_trans_2.
[Graphical view]
PfamPF03552. Cellulose_synt. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDCSA_DICDI
AccessionPrimary (citable) accession number: Q9U720
Secondary accession number(s): Q55D75
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents