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Database: UniProt/TrEMBL
Entry: B2B7J2_PODAN
LinkDB: B2B7J2_PODAN
Original site: B2B7J2_PODAN 
ID   B2B7J2_PODAN            Unreviewed;       701 AA.
AC   B2B7J2;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   30-AUG-2017, entry version 40.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=PODANS_2_11300 {ECO:0000313|EMBL:CAP73770.1};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Lasiosphaeriaceae;
OC   Podospora.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP73770.1};
RN   [1] {ECO:0000313|EMBL:CAP73770.1, ECO:0000313|Proteomes:UP000001197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC   {ECO:0000313|EMBL:CAP73770.1};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O.,
RA   Porcel B.M., Couloux A., Aury J.-M., Segurens B., Poulain J.,
RA   Anthouard V., Grossetete S., Khalili H., Coppin E.,
RA   Dequard-Chablat M., Picard M., Contamine V., Arnaise S., Bourdais A.,
RA   Berteaux-Lecellier V., Gautheret D., de Vries R.P., Battaglia E.,
RA   Coutinho P.M., Danchin E.G.J., Henrissat B., El Khoury R.,
RA   Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora
RT   anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|EMBL:CAP73770.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP73770.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000001197}
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E.,
RA   Benkhali J.A., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and
RT   its role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
RN   [4] {ECO:0000313|EMBL:CDP26171.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:CDP26171.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA   Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and
RT   its role in heterokaryosis in Podospora anserina.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC       reducing end of alpha-1,4-glucan. {ECO:0000256|RuleBase:RU363104}.
CC   -!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + ((1->4)-alpha-D-
CC       glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).
CC       {ECO:0000256|RuleBase:RU363104}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|RuleBase:RU363104}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000256|RuleBase:RU363104}.
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DR   EMBL; CU640366; CAP73770.1; -; Genomic_DNA.
DR   EMBL; FO904937; CDP26171.1; -; Genomic_DNA.
DR   RefSeq; XP_001911942.1; XM_001911907.1.
DR   STRING; 515849.XP_001911942.1; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   EnsemblFungi; CAP73770; CAP73770; PODANS_2_11300.
DR   GeneID; 6195463; -.
DR   KEGG; pan:PODANSg8987; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   eggNOG; COG0438; LUCA.
DR   KO; K00693; -.
DR   OrthoDB; EOG092C0XGC; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001197; Chromosome 2.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03793; GT1_Glycogen_synthase_GSY2_lik; 1.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176; PTHR10176; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001197};
KW   Glycogen biosynthesis {ECO:0000256|RuleBase:RU363104};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW   Transferase {ECO:0000256|RuleBase:RU363104,
KW   ECO:0000313|EMBL:CDP26171.1}.
SQ   SEQUENCE   701 AA;  80105 MW;  9A3D34CAEAFC6FFF CRC64;
     MADDGREPRE VRNHLLFEIA TEVAHRVGGI YSVIKSKAPV TTAEYGDRYT LIGPLNHQSA
     AVEVEAIEPT NPELAATIQS MRDRGIGILY GRWLIEGAPR VLLFDTKTAY HYLNEWKTDL
     WNVASIPSPD NDEETNEAVV FGYLVAWFLG EFVCHEKKKA VIAHFHEWLA GVALPLCKRR
     RIDVTTIFTT HATLLGRYLC AGSVDFYNNL QYFDVDAEAG KRGIYHRYCI ERASAHSCDV
     FTTVSHITAY ESEHLLKRKP DGVLPNGLNV TKFSAMHEFQ NLHQQSKEKI HDFVRGHFYG
     HYDFDPENTL YFFTAGRYEF RNKGVDMFIE SLARLNHRLK SSGSKTTVVA FIIMPAQTTS
     LTVEALKGQA VIKSLRDTVD TIERNIGRRI FERSLKWHDG EPMPDDKEIL TSQDRVLLRR
     RLFAMKRHGL PPIVTHNMIN DSEDPILNQI RRVQLFNHPS DRVKIIFHPE FLNSANPVLP
     LDYDDFVRGT HLGVFASYYE PWGYTPAECT VMGVPSITTN LSGFGCYMEE LIENSSDYGI
     YIVDRRNKGV DDSVNQLTSS MFDFTQKSRR QRINQRNRTE RLSDLLDWKR MGMEYVKARQ
     LALRRAYPTS FNGDEEEDYI PGPEQKISRP FSVPGSPRDR TGMMTPGDFA SLQEGREGLS
     TEDYVAWKLP EEEDPDEYPF PLTLRTKQPS GAATPPHVNG N
//
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