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Database: UniProt
Entry: A6RBU7_AJECN
LinkDB: A6RBU7_AJECN
Original site: A6RBU7_AJECN 
ID   A6RBU7_AJECN            Unreviewed;      2591 AA.
AC   A6RBU7;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-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=HCAG_07105 {ECO:0000313|EMBL:EDN10644.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN10644.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602640-2};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR602640-
CC       2};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000256|ARBA:ARBA00006122}.
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DR   EMBL; CH476662; EDN10644.1; -; Genomic_DNA.
DR   STRING; 339724.A6RBU7; -.
DR   VEuPathDB; FungiDB:HCAG_07105; -.
DR   HOGENOM; CLU_000488_0_0_1; -.
DR   OMA; NIGPGPI; -.
DR   OrthoDB; 141134at2759; -.
DR   Proteomes; UP000009297; 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:0004064; F:arylesterase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR002640; Arylesterase.
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; PF01731; Arylesterase; 1.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR602640-2};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009297};
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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..2591
FT                   /note="alpha-1,3-glucan synthase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002699960"
FT   TRANSMEM        1896..1913
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1920..1943
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1955..1975
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1987..2007
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2096..2116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2123..2145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2165..2187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2224..2243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          65..488
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   BINDING         2334
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         2398
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         2445
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         2446
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
SQ   SEQUENCE   2591 AA;  292788 MW;  3035789924EA9AAD CRC64;
     MRRWLVGVLL ALLAARATSW PYDPQFEGYN LNENKSAISP ADYYGEWSGH QYHPSPDNWR
     FPFYSLFLDR FVNGDPTNDN INGTSYEHDL NSNQMRHGGD VAGLMDTLDY LQGMGIKHFG
     TIESFRMTIT EIHRRGMYVI MDNTLATLGD LIGFKGHLNG TTPFDTNEHQ VVWKSSRRYA
     DFRIGNEYNE TCDYPRFYWE NGYPVGTDVT DQLIGCYDSD FDQYGDIEAF GVYPDWQRQL
     SKFASVQDRL REWIPSVRER LMRHSCILMR QLDIDGFRYD KALQATVDAL GDMSEHYREC
     ARSLGKHNFF LPGEITGGNT LGAIYIGRGR QPNMLPDSLE AAVKMTHRSN ENYFIREQGK
     SALDAGAFHY SVYRSLTRFL GMDGNLAAGF DTPVNWVDAW NEMILTNDFV NSQGHFDPRH
     MFGATNQDVF RWPTIREGTQ RMLLAFYITT LHLPGIPLLL WGEEQAFYVL DNTAQNYIFG
     RQAMSPATAW QTHGCYKLGS QQYYQWPIES GKYGCHDETV SYDHRDPSHP VRNILKTMYQ
     MRENYRTLND GFFIQQLSNQ TWQIFLPGSN NTPTETGMWS VHRGRFETAQ DFGKESNLPV
     WLVYQNYNKT HKYEFDCSDE KKALISNFDS GTTVKNLFFP FDELTLKRGP KKLGIEQSRE
     FNGCLDSLEL KPWDFRAYVP RERFIRPRPM VTKFSPGHDA RLLSTVSPDK DERVPIELYY
     SEAMDCNSVT ASITLNSTTD NGKIPSIDYS TVQCQSLNPQ PTKYIGELPN FWRWSATLVG
     VYNGVHQLSI KDALSADRRT NTSSMDHFLF RIGQSDNPMV FTRAANYSSS FLHTDKRGSL
     YVSHHAAGAD LYRYSLNWGS SFSDWLPYTG GNTTLERQPW SGTKLQRWKG EHVIVEYWNR
     MTGSSSHVQH GDLDWPHNKP RRFPHLYWNG PYNQYGYDAG LRNHMVQDDK GIWRFRFMTE
     WPALAQVNVW GINPDGKPDQ TFVFGDIDGD SVLDRLPPSS LSNIVINITN PPPHPYLSWL
     FLLNDGTLHF ELYPIGNQYH QLALYILLWV IPILTAAIGI YVFKKSFYQV KFNQVGISDK
     RGFIPLAIRR KFNKRVLEES HSMNPLVKLA NKSRFLQSTS ALVADSGSRR TTLIATLEYH
     IQDWGIKIKI GGLGVMAQLM GEHLGHQNLI WVIPCVSGID YPIDQVAEPM TVTVLGNPYE
     VKVQYHVVRN ITYVLLDAPV FRQQTSAEPY PARMDDLDSA IYYSAWNQCI AFAIKRFPVD
     LYHINDYHGS LAPIYLLPQT IPICLSLHNA EFQGLVHPLC QFGSIQLLHA GASYLRIHQQ
     GFGAVGVSKK YGKRSYARYP IFWGLKKVGT LPNPDPSDTG EWNGELPNKS DIDVNPQFEA
     DRLELKRQAQ EWAGLDQNPN ADLLVFVGRW SMQKGIDLIA DVFPAILEAR KDVQLLCVGP
     IIDLYGKFAA LKLDKLMKLY PGRVFSRPQF TALPPFIFSG AEFALIPSRD EPFGLVAVEF
     GRKGALGIGA RVGGLGQMPG WWYTVESTTT SHLLNQFKLA IDSALNSKYE TRAMMRARSA
     KQRFPVAQWV EDLEILQSTA IRIHNKESAK STGQPHYTPS AYSSSGILGS PIGLGSMTPV
     SPMSQSRNQS CINTNRLSAF GPQARNTVVY HQEVCPGADI DNENQPTGLS RKLSLGVRSG
     PGHTRAAPRM PRKLRKILAP MDLPENVHEN EPDRLGVAVT TDVDDDSDDD TVAQYFGDDE
     YTLTREQAEA GRGNDMSPFH PGFNELRIPG ESRPPSPAGM EGFLSPSRAL ADSANCFGST
     SVLSLGSVVG GKRDFKLQKV DPFFTDSNGE FYRAFEKKLE DLNSHNSESD LCIEDYLVKS
     EKKWFNRFRD ARLRPPPRQS RSHCSLVKLA QSATKLYAVA TTYLITSIIW WFIFRWFKSV
     IPLSLPFFFY GLAFMFIGVA HFAPTDDGVG WIQNIGAALY AAASSSGSIF FALNFGDESG
     APVKDWVFRA CVIQGTQQIY VVALWYWGSK LTKNIALGII DPDPISSTWK LTIFFSAHLT
     VETGPYPPTA TDVWLIIAIY LGAPRWAQIW WGTSGIGQHV PWAGGYLPGA LISRSLWLWL
     GVLDSMQGVG FGMILLQTLT RFHICFTLLA AQFLGSIATM CARAFSPNRI GPGDVHPDIS
     GGIDTIWNAW FWICLFCQLA LCSLLFYPQL TLFVPRKDLS QVTSTSVVQA VMAISVIGKF
     NYQIAATFAI IIGTISTVFY KPLVTKIHTL HNLPGEWHPF DGGSADIRFS DTIKFSEDIV
     IDNDRGIAII SFDPGRSGWN TVMVNTVFDI DYDLYQAKYI TTVSDNNETI VSPNSIAPVS
     YTQFYVTNDH HYLARTRPLL NKIETYFSMP WGWVTFVDFS STEHLKCEIV ATNISFANGI
     VMTPTGKEVV VASSGHDAVY IYQRDSETNS LSSTHETVHV NFHPDNVNFD HSLVISDPTV
     FDADGRFLRG LTVGGHPSII KLVQAVHNPE SVKAPSWVAE IRRGAGVDPA PCPAAPQQPK
     FYARTLYQSN GSAFFDQRYR GSRFQTRPFT DCFFIRERWK RLSRGDSALA RGLFKWNWSD
     LDSKATADHV F
//
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