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Database: UniProt
Entry: X0H5V4_FUSOX
LinkDB: X0H5V4_FUSOX
Original site: X0H5V4_FUSOX 
ID   X0H5V4_FUSOX            Unreviewed;      2361 AA.
AC   X0H5V4;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE            EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN   ORFNames=FOPG_16561 {ECO:0000313|EMBL:EXL67316.1};
OS   Fusarium oxysporum f. sp. conglutinans race 2 54008.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089457 {ECO:0000313|EMBL:EXL67316.1};
RN   [1] {ECO:0000313|EMBL:EXL67316.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54008 {ECO:0000313|EMBL:EXL67316.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW808.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXL67316.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=54008 {ECO:0000313|EMBL:EXL67316.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Annotation of Fusarium oxysporum PHW808.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; JH658968; EXL67316.1; -; Genomic_DNA.
DR   HOGENOM; CLU_000488_0_0_1; -.
DR   Proteomes; UP000030676; 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; 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}; 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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..2361
FT                   /note="alpha-1,3-glucan synthase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004940498"
FT   TRANSMEM        1062..1088
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1938..1958
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1970..1989
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2001..2020
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2032..2050
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2062..2082
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2106..2127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2148..2165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2185..2206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2232..2254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2260..2280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2287..2309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2334..2353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          64..523
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1385..1413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1873..1911
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1390..1413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1897..1911
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2361 AA;  264394 MW;  3296B049E52701B8 CRC64;
     MAPMKLLFSF LLATLAQGLH YDPSEIDYNL NTNKQAKSPL EYSGARKNHD YWPSPANWRM
     PFYTLFLDRY ANGDPSNDDI NGTVYEQDIT SNQLRHGGDL QGLVDSLDYI QGMGVKAIYI
     AGCPFINFPW GVDSYSPLDF TVLDHHFGAI MDWQNMVDEA HSRGMYVILD HTFSTMGDLL
     AFKGFENNTA IFSTKEHDVL YKTGRQYLDF APSNDYNQTC DYPRFYLDTG YPVGTNVTDQ
     LVGCFNSDFD QYGDIEAFGV HPDWQRSLAK FASVQDRLRE WVPSVRERLE RFSCITIQQL
     DIDGFRFDKA TQITVDALGN HSAAVRDCAS RLGKKNFFLP GEITGGNNYG SIYLGRGRTA
     DKYLDDVATA MNLTTKKKDE LANSTTRDLG QNALDAAAFH YSVYRFLTRF LGMSGNLEAG
     FDLPLNWVDM WSQMVLTNDL VNANTGKFDP RHMYGTSNQD VFRWPSIAQG IERLLMGFFI
     TTLHMPGLPL LLYGEEQAFY IIDSTADNYI FGRQAFTASQ GWRMHGCYTG TSTQYVNWPI
     EAARHGCTDE MAAYDHRDPS HPVRNILKSM YAMRENFDTF SEAWLLQPIG NQTFHTILSG
     SNTTGTEFGI WSVARAFQPT VQGEFASSPV WLVYHNQNVS TTYRFDCEDE DKAFYAPFDQ
     KSTVKNLFYP WDKITLGTST KSWHFSGSSK NSGCISEITM APFEFRAYVP KSDWKGPPPM
     ITKFTPGHDV PLLSSSVNGE VDITFEFSKV MDCDGLNEAI SITSVTENGN NVTVTRAKCK
     TLASDKPVAS YAGSIPSKFR YSATLTNVDD GVHRITIKNA STKADHEAMN SVDHFLLRVG
     AADNPIVFPT SANYSKTLVI NDSNKLFVNH SASGANKWRF STNWGSTWSN WTAYTGGIRE
     ITRLPWSGTS LQSWSGDHVM VQYWSQLHSS SSFMQAGDSS NQFERRFPHL FVEGTFNKFG
     FDAGVANQMS QISDGVWQMH LMDEWPTQFQ LNVWGMNPDG KPDASWVYGD VDFDGILDRM
     PPTSLALNVL NATNPPPLPY LSYQLLFNDA TLTFTKQPQG SMWIQIIMFI LLAVLPVVGG
     LTAVWIFLGS FYKVKVNKVG FKKQGLNPFG KLANRLSSVS FENFRHGELG AVPLKRRKVL
     IATIEYNIDD WNIKIKIGGL GVMAQLMGKA LKHQDLIWVV PCVGGVEYPV DQRAEPMYIL
     SIGKMYEIDV QYHQVQNITY VLLDAPIFRQ QTKSDPYPPR MDDINSAIYY SAWNYCIAEV
     IRRFDPTLYH INDYHGAAAP LHLLPERTIP CILSLHNAEF QGLWPMRTAE GFKEVCEVFD
     LDPKIVKEYV QFGSVFNLLH AGASYLRVHQ KGFGAVGVSK KYGDRSYARY PIFWGLSKVG
     QLPNPDPSDM AEWTRDEEAQ EKDADVNMET ESKRGDLRKQ AQEWAGLEIN PNAELFVFVG
     RWSIQKGVDL IADIFPSILE KHKDVQLICI GPVIDLYGKF AALKLAKLME KYPKRVYSKP
     EFTALPPYIF SGAEFALIPS RDEPFGLVAV EFGRQGALGV GARVGGLGQM PGFWYTIEST
     APQHLLQQFC EAITRALESK AKMRQKMRAW SAKQRFPVAQ WVEDVDKLQS MAIRIHNREA
     KKRRRITSGS LLSVPFNVVL HAPGGSRPSL DDSGIEAPLH SAHQSHTSNL SIPNIIETDY
     DVEASRRAIS NPLINTAHLA AAPTLGTPGA PPISATTDSA DEPALPRNPM FLNQSASCSV
     SSLATITNEP GSRLGVDTFA MHMMSPDESE TRPQAFGLHS PQSPPDASLN FQHDDQWRSS
     RLSVENVIGE RNDLKLQIVQ PFFTDVTGEY YKAFEQKLVG LTSKNSDTDL CIEDYLKESE
     KEWFKHFHNA KLGRSRSPSR TRSPAPSMSG ETLAPLDDDM QHGEWQNRPD SDDEFLLGTG
     YKPPKGFKKW LSIRIGDWPI YSFILAIGQI MASNSYQIVL LAGEASQTAA QLYIIAGTYG
     VTSILWWLTF RRLSTVYTLS LPWLFYGFAF VLLGVAPFML ENDRGRLHDT ATAMYAAGAS
     SGSMFFAMNF GDEAGAPTSV WIFRAAIIQG IQQLYVVGLW YWGSLISSKT SLVNGMVTSK
     TGPKTLVITI PIAVILWFLG VVSFVGLPDC YRQSPDKIPS FYMSLLRRHI VPWFLFSVAG
     QSYWLSAPYG RNWQFLFSAK AVTGWAVMLL ILGFFVILWL IGLWIFSMFS KTHPWIVPLF
     AIGLGVPRWA QMLWGISGIG LYLPWVGGAV ASAIVSRCLW LWLGVLDTIQ GVGLGMVLLL
     TLTRQHVAAT LIGAQILGSG FIILARATAP DKIGPGPVFP DLSEGIMPGI AQPWFWVALC
     LQLILPIGFF KFFRKEQVAK P
//
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