ID A0A1F5LKJ0_9EURO Unreviewed; 2344 AA.
AC A0A1F5LKJ0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=PENARI_c007G11622 {ECO:0000313|EMBL:OGE53520.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE53520.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE53520.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE53520.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGE53520.1}.
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DR EMBL; LXJU01000007; OGE53520.1; -; Genomic_DNA.
DR STRING; 1835702.A0A1F5LKJ0; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000177622; 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 CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 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; IPR001296; Glyco_trans_1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013534; Starch_synth_cat_dom.
DR PANTHER; PTHR47182:SF1; ALPHA-1,3-GLUCAN SYNTHASE; 1.
DR PANTHER; PTHR47182; CELL WALL ALPHA-1,3-GLUCAN SYNTHASE AGS1-RELATED; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 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:UP000177622};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..2344
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009519660"
FT TRANSMEM 1068..1093
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1984..2004
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2016..2035
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2042..2064
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2076..2097
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2109..2130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2150..2176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2199..2219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2243..2263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2270..2293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2313..2336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..518
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1664..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1801..1844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1915..1954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1664..1698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1801..1824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1918..1945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2344 AA; 263728 MW; F01B7D63A8ED1487 CRC64;
MYWKRTITAA ALFAVPGISW PYDESLTDYN INENQTASDP LDYWGEWPDH TYFPSPDNWR
FPVYTLFLDR FVNGDPTNDN INETLFEHDI SSNQMRHGGD VAGLLDTLDY LQGMGIKGIY
LAGLVLMNQP WGSDGYSALD TTLLDQHFGT VETWRNAITE IHSRGMYVIF DNTVATMGDL
IGFEGYMNTT TPFSMREHKA YWKSDRHYVD FSYGNSYNES CDYPRFWNET GYPVDQYVRD
ELGGCYDSDF DQYGDIEAFG VYPDWQRELA KFASVQDRLR EWVPSVRERL VRHSCMIIAS
FDIDGFRYDK ATQATIDALG DISGAYRDCA RRVGKNNFFL PGEVTSGNTL GSIFHGRGRQ
PDMQPETLEE AFKMTNSSDP AYFIRDQNQQ AIDAAAFHYS VYRSLTRFLG MDGNLAAGYD
VPVNWTEAWY QMVLTNDMIN ANTGKFDPRH MYGATNQDVF RWPAVEYGVE RQLLALFITT
LHMPGIPLLL WGEEQAFYVL DASAVNYIYG RQAMSPATAW RTHGCFQLNS TQYFQWPIKS
GRLGCTDETV TYDHRDPSHP VRNIIKHMYQ MRQDFAALND GWWVQLLSNQ THKIYLPGSN
GVPTETGMWS VLRSPYYQMQ DLGEMGNQTV WLVYQNSNRT VDYEFDCSDQ NAALVAPFDV
NTTVKNLFYP HDEITLQESP IKLGLYGTSE YNGCIDVMTM KPYEFRAYIP KEKFLSPRPM
ITKFLPGHDV PLLSAVSPGE SESMEVSLFF NAEMNCTMVT DSISLESKTE TGNIPSLDLD
SVTCETLEAE SITWTGQIPY IWAWRATLTG VYNGIHRLTV NNATTTDGRT TNAVDHFLVR
IGQQDNPMIF GSANYSRSLL HERKNGTIFI RQHAAGADKY RYSTNWGSTF SKWLPYEGGN
HTIEELPWSG TKKQRWEGKH VRVEYWSRLT GSSDYVQEGD GPGWNPTIRR RFPHLFFNGP
FNEYGYDAGL DNVVRQDEDG IWKFRFMAEW PAQGQLNVWG INPDGQPDQS YIYGDSDGDS
VLDRLPPSSL SVTSINITDH PPSPHLAWRI HLDDSNLQFK LVPAGSKYAQ MALFFLLWIV
PVVTASTCAY VFMKTFYRIK FNQVGVSEKK TLISMDFVSR FKIPPMESGK SSNPLVRLAN
KSNFLQSSSA FGKRTYHRRK VLIATMEYDI DDWAIKIKIG GLGVMAQLMG KQLGHQDLIW
VIPCVGGVDY PVDKPAESMF VMILGNSYEI KIQYHQLRNI TYVLLDAPVF RQQSATEPYP
ARMDDLDSAI YYSAWNQCIA QTMERFPVEL YHINDYHGSV APLYLLPETI PICLSLHNAE
FQGLWPMRTQ KEKTEVCSVF NLDLDVATRY VQFGEVFNLL HAGASYLRLH QQGFGAVGVS
KKYGKRSYAR YPIFWGLRKV GNLPNPDPSD TGEWNRELPK ESDINVDNDY EARRAELKRQ
AQEWAGLEQK PNADLLVFVG RWSMQKGIDL IADVLPSVLE ARPNVQLICV GPLIDLYGKF
AALKLARMMK LYPSRVCSKP QFTVLPPFIF SGAEFALIPS RDEPFGLVAV EFGRKGALGI
GARVGGLGQM PGWWYTVEST TTSHLLKQFK LAIDSALNSK SEVRAMMRAR SAKQRFPVAQ
WVEDLEILQS TSIRVHDKEH AKAQNLSTAA GAYNAIYGMM TPQAASTRSG ASTPPMQPSS
RPGTMGSLQR SSIIYSRDPS PGADSRPRSG LSRQVPFGIR PISSSTEPRG RRDLGKGSIV
EGDDSTGKAS PEAEEDSDEE LMATCYGDDD YPVLPDGVDA ARAQNPQSPG IAFTKEALSA
RHLARSSNTP SSSTAPSTAE TDDTLIPPSR PWAGPGSRLS SSSALSVDSV VGEKKDFKLQ
KVDPFFTDSN GEYYKEFEKR LEELNGANSD NQLCIEQYLE KSEKKWFNKF RDARLGRNQG
SPTGSMHLGK GDSPTGSITN DDATSHDSVV PERKDGPLDE FMLGDNYVPP TGLKKWMQMR
LGEWPVYSLF LGLGQIIAAN SYQITLLTGE VGQTAAKLYG IASVYLITSI LWWFFFRFCK
SVLVLTVPWF LYGTAFMIIG MAHFEPDAYV RGWIQNVGSG IYAAASSSGS IFFALNFGDE
SGAPVKQWVF RACLIQGTQQ AYVIALWYWG STLTKASSAG NTNSQSSITN TWVMTAICTP
IMIFLWSIGL LIYFGLPNYY RQTPGKVPSF YKSVFRRKIV LWNWVVVVLQ NFFLSAPYGR
NWNCLFLPWA GSYTSGALVS RSLWLWLGVL DALQGLGFGM ILLQTLTRMH ICFTLLVSQV
IGSIATMCAR SFAPNNIGPG PISPDITAGV GALANAWFWI ALLLQLLICG GFLLFFRREQ
LSKP
//
