ID B6Q1R3_TALMQ Unreviewed; 2395 AA.
AC B6Q1R3;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=PMAA_037050 {ECO:0000313|EMBL:EEA28916.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA28916.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995899; EEA28916.1; -; Genomic_DNA.
DR RefSeq; XP_002145431.1; XM_002145395.1.
DR STRING; 441960.B6Q1R3; -.
DR VEuPathDB; FungiDB:PMAA_037050; -.
DR HOGENOM; CLU_000488_0_0_1; -.
DR OrthoDB; 141134at2759; -.
DR PhylomeDB; B6Q1R3; -.
DR Proteomes; UP000001294; 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; cd06174; MFS; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
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; 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; 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:UP000001294};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..2395
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002847765"
FT TRANSMEM 1080..1102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1969..1991
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2003..2020
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2027..2050
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2135..2161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2182..2199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2219..2241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2248..2268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2293..2313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2320..2339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2367..2387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..525
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1724..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1920..1940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2395 AA; 269908 MW; EDEEDEDD2FA9D4FB CRC64;
MKLSSLILND FLLLFSNIQL TVALAYTPDQ VGFNLNENKT ATNPLDYWGQ WQDHEYHPSP
SNWRMPFYTV FLDRFANGDP SNDDANGTQW EHDILSNQLR NGGDVRGLMD SFDYLQGMGI
KGLYIAGMPH INEPWAADGY SPLDLTLLDR HLGSIDDWRS MIEEAHRRGM YVVMENTMAT
MGDLIGFEGH LNNSALFNSH GYNYVWKTSR RYHDFQPGNE WLDDCEWEYP RFWDDSGQGV
IETNLTRGCQ NSEFDQYGEV SSFGDYPEWE RQITKFAFVQ DRLREWRPDV RRKLELFSCI
TIAMLDVDGF RIDKALQVTL DAQGDWSNSI RQCARRFNKH NFFIPGEIVS GNAFGALYIG
RGQQTNQTMD NMTEIITMAN SSIPGLHLRS SDKVALDAAA FHYTVYRALT RFLGMDGVYE
AAGDPPTNFV ELWDTLVQTN DMTNTNTGEF DPRHLYGLSN QDVFRWPSIT NGVERQLLGL
YIVSLLFPGI PALVWGEEQA FYILDNTNSN YVFGRSPMTS SLAWQLHGCY KVGSVKYSDF
PTDSALRGCM DDSVSLDHRD PTHPVRGLLK TMHEIRQNYP VLNDGFYLQQ LSNMTHDIHL
PGSNGTRTET GLWSILRSRF APTQDFTGQA QGNQSVWLVY HNDDMAVNYQ FNCSDEQQAL
VSPFDSGTTV KNLLPPFEEY TLQPSVHKLG LDGSTGFNGC LSNLTLPAYS FKAFVPKSAF
VAPSPYITKF EPGHDARLLS IDTTGERVPI SFSFSEEMDC DSITAGLSVT STALNGEAAR
FDNSSISCNL LPERQQTIYQ GTFEGVFNYS IELENVFHGI HEIVLNNVTN RDQNRTTNSV
DHFMIRIGSQ ENPMVWPNQA NYSRSLLYAD DANDGSLWVS HKASGADQWR YSLDFGSSYT
PWMPYTGANV SIAPKSWSGT KLQAWQGEHI IAQYWNRVAG SSNHYQHGDL DWDNKPPRRF
PHLWIQGDFN QFGYDSGYPS QMHLHNSSGR WEYNLMTEWP TQLSLNAWGV NEDGHPDITQ
VYGDIDGDMI LDRIPPITLM NNVINVTEPP SWPFLSWKLS LDDGNLKIDL SPHGSQKTQI
AIFVLLGICP VVTAVLAVWI YFKVFYQVKR IVFGVTQRNF RSHAQQLTDD SATDVSSSID
DNGSNFVNML RRNINRSPSP RPSAHNQALN ADAGDSRRTV LIATMEYDIE DWAIKIKIGG
LGVMAQLMGA NLGHQNLIWV VPCVGGVDYP VDEVAEPMKI KVLDQSFLVH VQYHHLRNIT
YVLLDAPIFR AQSKSEPYPA RMDDLDSAIY YSAWNSCIAE TLQRFPVDLY HINDYHGAVA
QLHLLPRTIP CCLSLHNAEF QGLWPMRTSQ ECEEISQIFN LDPVVVKKYV QFGDVFNLLH
AAATYLQIHQ NGFGAVGVSR KYGKRSWARY PIFWGLREIG SLPNPDPSDT AEYNQDSQAT
DAEVDPAFEA MRSDMKSEAQ KWAGLEQNPN AELFVFVGRW SMQKGIDLIA DVFPSIMENS
PTTQLICVGP VIDLYGRFAA IKLSKMMDMY PGRVFSKPQF TALPPYIFSG ADFALIPSRD
EPFGLVAVEF GRKGTLGVGS RVGGLGQMPG WWYTIESMTS KHLNRQFKQA IYEALNSNTS
DRAIMRAWSR RQRFPVAHWI ENLETLYVSS IAKHRKHSKQ ENPSRTNSMV RMSFSTISRS
SMQTPVQPME FLRQIGHYRG SASQRPEPHR RATSQAISLF SIEHGNSSTE ESSSQSADGH
ASIDQQWPLQ VPRSMTYPSS ETSEIPPTTR KGGNESSRNS TAPSIEGNGF QSTSVFDQIS
AVPEDAMSSG HLSLRDQNRN SSNLSLLSVD NIIREDRTFN LQKVNPFFTD SSGRYAQRFE
KRLKHLNFKN SEDQLCIEQF LSKSEKEWFK MYRDIKLGRS PSPSRAATPV LSTIAHITSS
DERTGGGIPT DTEKPLEGAN ISEEELKLPE GYVPPSGLKR FMLCRIGDWP IYSILLSFGQ
IIAANSYQIT LLNGEVGEPA EKLYLIATIY LIFSIVWWIV FRSFRSIFVL SVPFLLYGLA
FAFIGISPFV TVSTSRWWIQ NVATGLYSAA SSSGSIYFAL NFGDEGNTSV GSWVYRACII
QGTQQIYVSF LWYWGSRLAA ESQAGVTRNS LADSHPILLT GVGLGIAFIM WIVGTVIFLG
LPDYYAQSPG KVPAFYKSLP RRKIVLWFFY AVFIQNYWLS APYGRNWLYL WSSQHAHSWM
ITVMVVIFFI CIWAIVLWIL GILSKRHAWF VPIFAIGLGA PRWCQMLWST SNIGTYVPWA
GSAVASTLVG RGLWLWLGVL DALQGVGFGM ILLNTLTRLH IAFTLLAAQV IGSIGTILAR
ATAPDSTGPG DVFPDFSAGV HDALSKGDFW VCLLFLLSIN VLCFLFFRKE QLQKP
//
