ID A1CLJ7_ASPCL Unreviewed; 2398 AA.
AC A1CLJ7;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=ACLA_042430 {ECO:0000313|EMBL:EAW10021.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW10021.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW10021.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19749, Rhea:RHEA-
CC COMP:11150, Rhea:RHEA-COMP:11151, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28100, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC EC=2.4.1.183; Evidence={ECO:0000256|ARBA:ARBA00000687};
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC {ECO:0000256|ARBA:ARBA00006122}.
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DR EMBL; DS027056; EAW10021.1; -; Genomic_DNA.
DR RefSeq; XP_001271447.1; XM_001271446.1.
DR STRING; 344612.A1CLJ7; -.
DR EnsemblFungi; EAW10021; EAW10021; ACLA_042430.
DR GeneID; 4702724; -.
DR KEGG; act:ACLA_042430; -.
DR VEuPathDB; FungiDB:ACLA_042430; -.
DR eggNOG; ENOG502QQX3; Eukaryota.
DR HOGENOM; CLU_000488_0_0_1; -.
DR OMA; KYCQFGN; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0047657; F:alpha-1,3-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11323; AmyAc_AGS; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013534; Starch_synth_cat_dom.
DR PANTHER; PTHR47182; CELL WALL ALPHA-1,3-GLUCAN SYNTHASE AGS1-RELATED; 1.
DR PANTHER; PTHR47182:SF2; CELL WALL ALPHA-1,3-GLUCAN SYNTHASE MOK13; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF13692; Glyco_trans_1_4; 1.
DR Pfam; PF08323; Glyco_transf_5; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..2398
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002633561"
FT TRANSMEM 1069..1094
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1973..1990
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2010..2027
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2034..2057
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2069..2089
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2101..2121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2141..2168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2188..2211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2223..2244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2325..2347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2370..2390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..560
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1656..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1766..1801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1719..1733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1777..1797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2398 AA; 269824 MW; C0858023F0956782 CRC64;
MQRLATLLLS LLLSVHQVLC WPYTESLVDY NLNENKSAES PIDYWGEWPD HKYHPSPKNW
RFPVYTIFLD RIANGDPTND DINGTAFEHV VNSNQMRHGG DLVGLIDSLD YIRGMGFKGI
YFAGTGLMNL PWAYDGYSPV DTTLLDMHHG TLQDWRRTIS EIHDRDMYVI LDNTLATLSN
LIGFQGHLND SADFRPDEYH VEWISDRRYA DFHFSNEYNE SCAYPKFWYE TGFPLGSGGV
EKLHGCYNSD FDQYGELEAF GNFPDWQRQL TKFASVQDRL REWHKPVRDI ITKHYCIQIA
SLDIDGFRYD KAAQATLEPL GEISAAFREC ATKLGKDNFF ISGEITSGDT FGSLYLGRGR
QPNQRLNSTI DALKLNNNSA PQYFLREDGH QALDSAAFHY TIYRSMTRFL GMDGNLVAGF
DLNTDFIQAW NEMLVNNDFL NHFTNEVDPR HMYGVSNQDN FRWPAIKNGT AKYLLGLFIV
TLELPGIPLI LWGEEQDMYV FDATATNYLF GRQPMTYQTA WWTHGCFNLN TTKFYDFPNE
RGLYGCHDIT VTYDQRNPAH PLRNIMKRMF EIREQYPVAN DGIYLQTLSQ LTKDIYLPGS
STTPTVTGLW SVLRSYFPGI QKEADSKDNS TFWLVYHNDN RTVSYGGDCK KKDTALLAPY
KAGTKLTNLF YPYDELTLQE GPGPIGGPGS ESYGCTSNLT LQAWEYRAYV RTEEFVEPGP
TVTEFAPGHD ARLLSSEDTG ETVDIRLGYS KEMSCDGVTR AISLNSTSQK GITPTLDTSS
VNCTKITPRT SGNGYAGEIP TVWTWSAKLK NVHHGVHEII VKNVTTTSGL STNAVDRFLL
RMGSLTNPLM TPLANYSSSL VHKSQDGSIY IQHDAAGADQ FRYSTTFGRT WSDWTAYEGG
NTTIDVAPWS GTDAQHWKGT HVRVQYFSRL TGSSDYIQEG DEGWEDDVPR RFPQLWWNGP
YNQYGYDAGL ESSMRYDSKE RVWKYDFVYE WPSVGQISVW GVGPDGIPDP TEVYGDVANS
SVVQKLPPSY LSSNVINITT LPPFPHLGWT ISLNDANLRY VMTPVGSGWA QLVLFVLLWV
VPILMGLFGA FIFMRKFYRV KLNRDGAAAK EVKLPMIWRK IRGHFANKDE AEIDLPDKGI
IANATIAGAP EQRRTVLIAT MEYNIEDWNV KVKIGGLGVM AQLMAQNLKH QNLIWAVPCV
GDIEYPEDTP AEPMVVTILD KPYLVNVQYH VVDNITYVIL DAPVFRQQTK AEPYPPRMDD
LDSAIYYSAW NQCIAETIKR FPSIDLYHIN DFHGCLAPLY LLPTRTIPVC LSLHNAEFQG
LWPLRTQQEK KEVCSVFNLP VETATKYCQF GNVFNLLHTG ASYLRFHQHS FGAVGVSKKY
GKRSWARYPI FWSLDKIGSL PNPDPSDTGA VGHGTDATVP IPSPQERIND KLKAQKWAGL
KEDADANLLV FVGRWSKQKG VDLIADVIPA ILSSRPEVQL ICVGPIIDLY GKLAAVKLEK
IMAMFPGRVF SKPEFTILPP YVFSGADFAL IPSRDEPFGL IAVEFGRKGA LGIGSRIGGL
GQMPGWWYTV ESDATRHLLH QLRTAIKSAL DSDLETREEM RTNSAQQRFP VLEWIQKLET
LQRTAIKIHH EKNKDTASGP MPDSQIYWET QNMRDSTVSL PGLPPSLRDG TDSPPARLSL
NAQSRLRELQ ADDQNSGRLG RKLSLGRRAG PGQGRSRLMK KSLRSSQVAE GQTDDETTDA
DLDEDDLDAR LVNYISSEEA MRAVGHDLGS PDIRDSYRSE NLGTPSQSMS TSPYYVSRAP
SPAPRAPSEL FQHPFQLALH SGASTPSIHS RNVSVLSLPS VKGDHNQQVF ELNKVDPTFT
DSMGHFTRRF EEILEGLDKK NSMTDCCIET FLMKSERKFF NMYNDAQLKK HRAKNAVYPS
GAADYVEDET SYNRLSDPGA GTDISDSDEI DRWLSRLGYM RPMAIQRFMR RRVGNWPVYA
LFLGLGQIIA TNSAQITLLV GQVGESATKL YVIAAIYCVA SIVWWLMYSR LPAVIVLSVP
WFIYGFAFII IGVSPYGASV ASRGWAQNVA AAVYAVASSS GSLFFALNFG DQGSVPVKDW
MFRAGLIQGI SQLYTVALWY WSSRVTTVEI GGVSSLTLGT WRLTAVVMPI AAVCFVIGVL
LALGLPNYYR QAPSRILFFY TSLFRRRIVL WFFFMVIVQN WFLAAAFGRN WSFLWSSNHA
KTWQIVVLII CFFLVLWVII LSAFRILSKE HSWILPVFGL SLGAPRWAQT WWGTSNIGYY
LPWAGSLTSG AVVSRSLWLW LGVLDEVQQV GLGMILLQTL TRVHVCFVLL AAQAVGSIAT
ICARGFAPNR LGPDGVSPNV GTSVDKVGNA WFWISLFFQL LASFGFLLFY RKEQLNRP
//
