DCSA_DICDI
ID DCSA_DICDI Reviewed; 1059 AA.
AC Q9U720; Q55D75;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cellulose synthase catalytic subunit A [UDP-forming];
DE Short=DcsA {ECO:0000303|PubMed:10681463};
DE EC=2.4.1.12 {ECO:0000269|PubMed:10681463};
GN Name=dcsA; ORFNames=DDB_G0269124;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=AX4;
RX PubMed=10681463; DOI=10.1073/pnas.040565697;
RA Blanton R.L., Fuller D., Iranfar N., Grimson M.J., Loomis W.F.;
RT "The cellulose synthase gene of Dictyostelium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2391-2396(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalytic subunit of cellulose synthase. It incorporates
CC glucose from uridine 5'-diphosphate glucose (UDP-alpha-D-glucose) to
CC cellulose (a (1->4)-beta-D-glucan), which is produced as an
CC extracellular component for mechanical and chemical protection at the
CC onset of the stalk formation, when the cells exhibit multicellular
CC behavior during culmination. {ECO:0000269|PubMed:10681463}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-
CC COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12;
CC Evidence={ECO:0000269|PubMed:10681463};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19930;
CC Evidence={ECO:0000269|PubMed:10681463};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Glycan metabolism; amoeba cellulose biosynthesis.
CC {ECO:0000305|PubMed:10681463}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Progressively accumulates during culmination,
CC especially at the onset of the stalk formation. Present in fruiting
CC body (at protein level). {ECO:0000269|PubMed:10681463}.
CC -!- DOMAIN: There are two conserved domains in the globular part of the
CC protein: the N-terminal domain (domain A) contains the conserved DXD
CC motif and is possibly involved in catalysis and substrate binding. The
CC C-terminal domain (domain B) contains the QXXRW motif and is present
CC only in processive glycosyl transferases. It could be involved in the
CC processivity function of the enzyme, possibly required for holding the
CC growing glycan chain in the active site.
CC -!- MISCELLANEOUS: Amoebae missing dcsA exhibit snowmen-shaped fruiting
CC bodies.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AF163835; AAF00200.1; -; mRNA.
DR EMBL; AAFI02000005; EAL71912.1; -; Genomic_DNA.
DR RefSeq; XP_646256.1; XM_641164.1.
DR AlphaFoldDB; Q9U720; -.
DR STRING; 44689.DDB0191159; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q9U720; -.
DR EnsemblProtists; EAL71912; EAL71912; DDB_G0269124.
DR GeneID; 8617212; -.
DR KEGG; ddi:DDB_G0269124; -.
DR dictyBase; DDB_G0269124; dcsA.
DR eggNOG; ENOG502QQSH; Eukaryota.
DR HOGENOM; CLU_289588_0_0_1; -.
DR InParanoid; Q9U720; -.
DR OMA; MDYPSEN; -.
DR UniPathway; UPA00838; -.
DR PRO; PR:Q9U720; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0045179; C:apical cortex; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:dictyBase.
DR GO; GO:0005739; C:mitochondrion; IDA:dictyBase.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IDA:dictyBase.
DR GO; GO:0030244; P:cellulose biosynthetic process; IDA:dictyBase.
DR GO; GO:0031150; P:sorocarp stalk development; IMP:dictyBase.
DR GO; GO:0042244; P:spore wall assembly; IMP:dictyBase.
DR Gene3D; 3.90.550.10; -; 2.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF13632; Glyco_trans_2_3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cellulose biosynthesis; Developmental protein; Glycosyltransferase;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1059
FT /note="Cellulose synthase catalytic subunit A [UDP-
FT forming]"
FT /id="PRO_0000327825"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..810
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 963..983
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 993..1013
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1035..1055
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..628
FT /note="Catalytic subdomain A"
FT /evidence="ECO:0000250"
FT REGION 701..761
FT /note="Catalytic subdomain B"
FT /evidence="ECO:0000250"
FT REGION 933..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 370
FT /evidence="ECO:0000255"
FT ACT_SITE 717
FT /evidence="ECO:0000255"
FT BINDING 624
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 626
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1059 AA; 121412 MW; 2CF8A701D7D99B81 CRC64;
MDRNEGGDFP INTPNNINSS GGSYNNSMNN SSNNIGRDIG NNQSSRNLKP KPSQSNLKWI
ARDLKKKSVR KDSERKLKSS GVLKKKNTVM DFGEDDGGSG DDGNITEGLP ISEGMDDLPS
SSNSRGGSGN DEQKKQFPKE MNSPSSEYGT TSGGQRFDTL VDPDISLAEM EEKMRQHKVY
QEQQQQQQQQ QQQQKQKDKE LSSQKKKPSS MQLSKKKHVA KEDSETLETI IGEEKKEVVF
EVKPYFSHAI LQATMAVFLI WNIFYFAYRA GWTMNRTDYI TFSYSILFII VEFISFLGSA
LHLNNFTNPC TFVLVVTLEQ ILAKRRKKHP TVMMYVCTYK EPPSIVSRTF RTAISMDYPS
ENLWIGLLDD SVNYRESRGW AHLQSVEKNF LYVLLQKAVY SVHNIRPPVT SQHEDPHGIL
NETSSKIESS TKEVIEAEVQ WFIEYFLLNS WFGVGQEIPR DADDAERALI AKLRDDNFSP
YRTFTKSESE KISNFTIDSL QSLWHGSAFF RPLIRSILLK KDYVRNFVSE LNNQHRLRFL
NTEALAMAQY QVLMMGRQEL PWDEISSGNV RIDFDTCDGP IVSPKCTYLR RRKPPIPHNK
AGNINNALFN ESTKADYEFL GLLDADQQPH PDFLKRVLPY FYSDEGQDLA FVQTPQFFSN
IYPVDDPLGH RNMEFYGPVM EGRSANNACP FVGTNAIFRR QPLYDIGGIM YNSVTEDMYT
GMKLQVSGYK SWYHNEVLVV GTAPVDLKET LEQRKRWAQG AVEIFSLTPW GYIRGKLGWR
KMLYNLDSCI YPFLSPTAFF YGASPLIMSI WTVPIVVKDP IIFILVGMIP VMVLPRVIQY
MILRAKRPYE AGKSGPSLWV EATDLWRAEQ TFFGFAGTYI SSWREGSASI VKLLKARKIS
RHKLAMWNWK RDFVKKPVVC EVFRQTKLVN ENDNAQESSG KHKAEQSFRT SNKESDTIKN
SRLFLPNIIL FVVNILAMMS AVLRFNCFQN DMWLLVVVAG FSFSTLWHLW SFIPMALRQS
EKQWPYASSY HAHNIVLFLV LGFLVLLFVD VKVCIPRVG
