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Protein

Cellulose synthase catalytic subunit A [UDP-forming]

Gene

dcsA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Mg2+By similarity

Pathwayi: amoeba cellulose biosynthesis

This protein is involved in the pathway amoeba cellulose biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway amoeba cellulose biosynthesis and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei370Sequence analysis1
Binding sitei624SubstrateSequence analysis1
Binding sitei626SubstrateSequence analysis1
Active sitei717Sequence analysis1

GO - Molecular functioni

  • cellulose synthase (UDP-forming) activity Source: dictyBase

GO - Biological processi

  • cellulose biosynthetic process Source: dictyBase
  • sorocarp stalk development Source: dictyBase
  • spore wall assembly Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Keywords - Biological processi

Cellulose biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00838.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellulose synthase catalytic subunit A [UDP-forming] (EC:2.4.1.12)
Gene namesi
Name:dcsA
ORF Names:DDB_G0269124
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 1, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0269124. dcsA.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei246 – 266HelicalSequence analysisAdd BLAST21
Transmembranei280 – 300HelicalSequence analysisAdd BLAST21
Transmembranei306 – 323HelicalSequence analysisAdd BLAST18
Transmembranei790 – 810HelicalSequence analysisAdd BLAST21
Transmembranei813 – 833HelicalSequence analysisAdd BLAST21
Transmembranei963 – 983HelicalSequence analysisAdd BLAST21
Transmembranei993 – 1013HelicalSequence analysisAdd BLAST21
Transmembranei1035 – 1055HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • apical cortex Source: dictyBase
  • cytosol Source: dictyBase
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: dictyBase
  • mitochondrion Source: dictyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003278251 – 1059Cellulose synthase catalytic subunit A [UDP-forming]Add BLAST1059

Proteomic databases

PaxDbiQ9U720.

Expressioni

Developmental stagei

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

Interactioni

Protein-protein interaction databases

STRINGi44689.DDB0191159.

Structurei

3D structure databases

ProteinModelPortaliQ9U720.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni328 – 628Catalytic subdomain ABy similarityAdd BLAST301
Regioni701 – 761Catalytic subdomain BBy similarityAdd BLAST61

Domaini

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.

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IXTD. Eukaryota.
COG1215. LUCA.
InParanoidiQ9U720.
KOiK00694.
OMAiRSANNAC.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF13632. Glyco_trans_2_3. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9U720-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRNEGGDFP INTPNNINSS GGSYNNSMNN SSNNIGRDIG NNQSSRNLKP
60 70 80 90 100
KPSQSNLKWI ARDLKKKSVR KDSERKLKSS GVLKKKNTVM DFGEDDGGSG
110 120 130 140 150
DDGNITEGLP ISEGMDDLPS SSNSRGGSGN DEQKKQFPKE MNSPSSEYGT
160 170 180 190 200
TSGGQRFDTL VDPDISLAEM EEKMRQHKVY QEQQQQQQQQ QQQQKQKDKE
210 220 230 240 250
LSSQKKKPSS MQLSKKKHVA KEDSETLETI IGEEKKEVVF EVKPYFSHAI
260 270 280 290 300
LQATMAVFLI WNIFYFAYRA GWTMNRTDYI TFSYSILFII VEFISFLGSA
310 320 330 340 350
LHLNNFTNPC TFVLVVTLEQ ILAKRRKKHP TVMMYVCTYK EPPSIVSRTF
360 370 380 390 400
RTAISMDYPS ENLWIGLLDD SVNYRESRGW AHLQSVEKNF LYVLLQKAVY
410 420 430 440 450
SVHNIRPPVT SQHEDPHGIL NETSSKIESS TKEVIEAEVQ WFIEYFLLNS
460 470 480 490 500
WFGVGQEIPR DADDAERALI AKLRDDNFSP YRTFTKSESE KISNFTIDSL
510 520 530 540 550
QSLWHGSAFF RPLIRSILLK KDYVRNFVSE LNNQHRLRFL NTEALAMAQY
560 570 580 590 600
QVLMMGRQEL PWDEISSGNV RIDFDTCDGP IVSPKCTYLR RRKPPIPHNK
610 620 630 640 650
AGNINNALFN ESTKADYEFL GLLDADQQPH PDFLKRVLPY FYSDEGQDLA
660 670 680 690 700
FVQTPQFFSN IYPVDDPLGH RNMEFYGPVM EGRSANNACP FVGTNAIFRR
710 720 730 740 750
QPLYDIGGIM YNSVTEDMYT GMKLQVSGYK SWYHNEVLVV GTAPVDLKET
760 770 780 790 800
LEQRKRWAQG AVEIFSLTPW GYIRGKLGWR KMLYNLDSCI YPFLSPTAFF
810 820 830 840 850
YGASPLIMSI WTVPIVVKDP IIFILVGMIP VMVLPRVIQY MILRAKRPYE
860 870 880 890 900
AGKSGPSLWV EATDLWRAEQ TFFGFAGTYI SSWREGSASI VKLLKARKIS
910 920 930 940 950
RHKLAMWNWK RDFVKKPVVC EVFRQTKLVN ENDNAQESSG KHKAEQSFRT
960 970 980 990 1000
SNKESDTIKN SRLFLPNIIL FVVNILAMMS AVLRFNCFQN DMWLLVVVAG
1010 1020 1030 1040 1050
FSFSTLWHLW SFIPMALRQS EKQWPYASSY HAHNIVLFLV LGFLVLLFVD

VKVCIPRVG
Length:1,059
Mass (Da):121,412
Last modified:May 1, 2000 - v1
Checksum:i2CF8A701D7D99B81
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF163835 mRNA. Translation: AAF00200.1.
AAFI02000005 Genomic DNA. Translation: EAL71912.1.
RefSeqiXP_646256.1. XM_641164.1.

Genome annotation databases

EnsemblProtistsiEAL71912; EAL71912; DDB_G0269124.
GeneIDi8617212.
KEGGiddi:DDB_G0269124.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF163835 mRNA. Translation: AAF00200.1.
AAFI02000005 Genomic DNA. Translation: EAL71912.1.
RefSeqiXP_646256.1. XM_641164.1.

3D structure databases

ProteinModelPortaliQ9U720.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0191159.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Proteomic databases

PaxDbiQ9U720.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAL71912; EAL71912; DDB_G0269124.
GeneIDi8617212.
KEGGiddi:DDB_G0269124.

Organism-specific databases

dictyBaseiDDB_G0269124. dcsA.

Phylogenomic databases

eggNOGiENOG410IXTD. Eukaryota.
COG1215. LUCA.
InParanoidiQ9U720.
KOiK00694.
OMAiRSANNAC.

Enzyme and pathway databases

UniPathwayiUPA00838.

Miscellaneous databases

PROiQ9U720.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF13632. Glyco_trans_2_3. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDCSA_DICDI
AccessioniPrimary (citable) accession number: Q9U720
Secondary accession number(s): Q55D75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

Amoebae missing dcsA exhibit snowmen-shaped fruiting bodies.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.