SWISSPROT: Q47SE3_THEFY

ID   Q47SE3_THEFY            Unreviewed;       873 AA.
AC   Q47SE3;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 94.
DE   SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:AAZ54624.1};
DE            EC=2.4.1.1 {ECO:0000313|EMBL:AAZ54624.1};
GN   OrderedLocusNames=Tfu_0586 {ECO:0000313|EMBL:AAZ54624.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54624.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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DR   EMBL; CP000088; AAZ54624.1; -; Genomic_DNA.
DR   RefSeq; WP_011291033.1; NC_007333.1.
DR   STRING; 269800.Tfu_0586; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   EnsemblBacteria; AAZ54624; AAZ54624; Tfu_0586.
DR   KEGG; tfu:Tfu_0586; -.
DR   eggNOG; ENOG4107R76; Bacteria.
DR   eggNOG; COG0058; LUCA.
DR   HOGENOM; HOG000229798; -.
DR   KO; K00688; -.
DR   OMA; NLRWSWH; -.
DR   OrthoDB; 137158at2; -.
DR   BioCyc; TFUS269800:G1G4Q-596-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR   GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR011834; Agluc_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   Pfam; PF11897; DUF3417; 1.
DR   Pfam; PF00343; Phosphorylase; 2.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   TIGRFAMs; TIGR02094; more_P_ylases; 1.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
PE   4: Predicted;
DR   PRODOM; Q47SE3.
DR   SWISS-2DPAGE; Q47SE3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Glycosyltransferase {ECO:0000313|EMBL:AAZ54624.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000313|EMBL:AAZ54624.1}.
FT   DOMAIN       13    124       DUF3417. {ECO:0000259|Pfam:PF11897}.
FT   MOD_RES     614    614       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR000460-1}.
SQ   SEQUENCE   873 AA;  97172 MW;  A3F6F648CDFD1106 CRC64;
     MKAIRRFTVR TVLPDELAAL CTLAANLRWT WHAPTRAVFA AVEPRLWEAV GRDPIRLLGE
     VTPERLRELA ADAEFRARLD AAAADLDRYL TAPLWYQQLT DSSDTPPPAA IAYFSAEYGL
     DATLPQYSGG LGILAGDHLK SASDLGIPVI GVGLLYRHGY FSQTLSPDGW QLERYPEIDP
     HCLPMTRLED RGTPVRITVD LPENRTLTAH VWIVRVGRVP LLLLDTYHDD NDLDLRGVTD
     RLYGGGTEQR LRQELLLGIG GLRAVRAYCL RTGYPEPEVF HMNEGHAGFL GLERLREYIE
     TAGLDFDQAL EATRSGTVFT THTPVPAGID RFPKELVERH FSGPVALPGL PVERVMALGA
     ETYPGGDPNV FNMAVMGMRL AQRVNGVSAL HGAVSREMFG GLWPGFDVDE VPITSITNGV
     HAATWMAEEA WDAAQAMGLG LEELETPAGW QRLVERDAEE LWRMRRALRE RLIIEARKRL
     RASWRQRGAT DAELAWIDEA LDPEVLTVGF ARRVPSYKRL TLMLRDPERL TALLRHPERP
     IQIIIAGKAH PADEGGKRLI QEMVRFSDDP RVRDRIVFLP DYDMALAALL VQGCDVWLNN
     PLRPLEACGT SGMKSALNGG LNLSIRDGWW DEWFDGSNGW AIPTADGVDD PDRRDDIEAA
     ALYELFEEQV APLFYERDDH GLPRRWLETV KHTMVSLGPK VQATRMVREY VDQLYQPAAL
     AMRRLAADNY RGARELAAWK QRVQHAWPGV RIEHVETSMN GDTPQVGGEL EVRATLVLGG
     LDPDDVCVEV VLGLVNDDDE LINPTTTELV PLPASDVVYP LVRFGGTVPL DRAGTCGYTV
     RIRPRHRLLT HPAEAGMAVV AEPTMGIGTL VPH
//