ID A0A2K2ATL9_POPTR Unreviewed; 1011 AA.
AC A0A2K2ATL9; A0A2K2ATK7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 2.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=POPTR_004G123600 {ECO:0000313|EMBL:PNT40856.2};
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT40856.2, ECO:0000313|Proteomes:UP000006729};
RN [1] {ECO:0000313|EMBL:PNT40856.2, ECO:0000313|Proteomes:UP000006729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729}, and
RC Nisqually-1 {ECO:0000313|EMBL:PNT40856.2};
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
RN [2] {ECO:0000313|EMBL:PNT40856.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nisqually-1 {ECO:0000313|EMBL:PNT40856.2};
RA Tuskan G., Difazio S., Jansson S., Bohlmann J., Grigoriev I., Hellsten U.,
RA Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., Sterck L.,
RA Aerts A., Bhalerao R., Bhalerao R., Blaudez D., Boerjan W., Brun A.,
RA Brunner A., Busov V., Campbell M., Carlson J., Chalot M., Chapman J.,
RA Chen G., Cooper D., Coutinho P., Couturier J., Covert S., Cronk Q.,
RA Cunningham R., Davis J., Degroeve S., Dejardin A., Depamphilis C.,
RA Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J., Ellis B.,
RA Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L.,
RA Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., Holt R.,
RA Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., Jorgensen R.,
RA Joshi C., Kangasjarvi J., Karlsson J., Kelleher C., Kirkpatrick R.,
RA Kirst M., Kohler A., Kalluri U., Larimer F., Leebens-Mack J., Leple J.,
RA Locascio P., Lou Y., Lucas S., Martin F., Montanini B., Napoli C.,
RA Nelson D., Nelson C., Nieminen K., Nilsson O., Pereda V., Peter G.,
RA Philippe R., Pilate G., Poliakov A., Razumovskaya J., Richardson P.,
RA Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J., Schrader J.,
RA Segerman B., Shin H., Siddiqui A., Sterky F., Terry A., Tsai C.,
RA Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S., Yang G.,
RA Yin T., Douglas C., Marra M., Sandberg G., Van De Peer Y., Rokhsar D.;
RT "WGS assembly of Populus trichocarpa.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001275,
CC ECO:0000256|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; CM009293; PNT40856.2; -; Genomic_DNA.
DR EMBL; CM009293; PNT40858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K2ATL9; -.
DR STRING; 3694.A0A2K2ATL9; -.
DR InParanoid; A0A2K2ATL9; -.
DR Proteomes; UP000006729; Chromosome 4.
DR ExpressionAtlas; A0A2K2ATL9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468:SF28; ALPHA-GLUCAN PHOSPHORYLASE 1; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 2.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 2.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 522..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 857
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 1011 AA; 114712 MW; 221E64F7BF815923 CRC64;
MATTSSHFSP TSHWCSNGSS ISRLVDFGSK WRRKQQLFSM NSRRVVKRRS VSVSIKNVSS
SEPKQKLKDD ALIEEEEVPR ILNPSTPNAS SIASSIKYHA EFTPLFSPER FELPKAYYAT
AQSVRDALII NWNSTYESYE RLNAKQAYYL SMEFLQGRAL LNAIGNLELT GAYAEALSKL
GHSLENVACQ EPDAALGNGG LGRLASCFLD SLATLNYPAW GYGLRYKYGL FKQQITKDGQ
EEVAEDWLEM GNPWEILRND ISYPIKFYGK VVSGSDGKKH WIGGEDIKAV AYDVPIPGYK
TKTTINLRLW STKAPSEDLD LYAFNAGDHT KAYEALSNAE KICHILYPGD DSLEGKILRL
KQQYTLCSAS LQDIISCFER RSGSNIDWEK FPEKVAVQMN DTHPTLCIPE LMRILIDLKG
LSWKEAWNIT QRTVAYTNHT VLPEALEKWS LELMQKLLPR HVEIIELIDE ELICTIVSEY
GTEDSDLLEK KLKEMRILEN VDLPSAFAEL IVKPKQSSVG VTSEELENSD EETKLVYNSE
EETKRANDFE EETKRANDLE EETNLEEETK RANDFEEEME LVDEKDESKS KVTQKKEKIM
AEPPPKPPKM VRMANLAVVG GHAVNGVAEI HSEIVKDEVF NAFYKLWPDK FQNKTNGVTP
RRWIHFCNPG LSKIITDWIG MDDWVLNTEK LAELRKFSDN EDLQVQWKAA KRSNKMKVIS
FLKEKTGYSV SPDAMFDIQV KRIHEYKRQL LNILGIVYRY KKMKEMTAAE RKAKYVPRVC
IFGGKAFSTY VQAKRIVKFI TDVGATVNHD PEIGDLLKVV FVPDYNVSVA ELLIPASELS
QHISTAGMEA SGTSNMKFAM NGCILIGTLD GANVEIREEV GEDNFFLFGA RAHEIAGLRK
ERADGEFVPD PSFEEVKDFV KSGVFGPCNY DELIGSLEGN EGFGRADYFL VGKDFPSYIE
CQEEVDKAYH DQKTWTKMSI MNTAGSYKFS SDRTIHEYAR EIWNIEPVEL P
//
