ID PHS2_ARATH Reviewed; 841 AA. AC Q9SD76; Q93ZL3; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 02-SEP-2026, entry version 157. DE RecName: Full=Alpha-glucan phosphorylase 2, cytosolic; DE Short=AtPHS2; DE EC=2.4.1.1; DE AltName: Full=Alpha-glucan phosphorylase, H isozyme; DE AltName: Full=Starch phosphorylase H; GN Name=PHS2; OrderedLocusNames=At3g46970; ORFNames=F13I12.20; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."; RL Nature 408:820-822(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=cv. Landsberg erecta; RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200; RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.; RT "Multidimensional protein identification technology (MudPIT) analysis of RT ubiquitinated proteins in plants."; RL Mol. Cell. Proteomics 6:601-610(2007). CC -!- FUNCTION: Phosphorylase is an important allosteric enzyme in CC carbohydrate metabolism. Enzymes from different sources differ in their CC regulatory mechanisms and in their natural substrates. However, all CC known phosphorylases share catalytic and structural properties (By CC similarity). {ECO:0000250}. 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 -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL133292; CAB61943.1; -; Genomic_DNA. DR EMBL; CP002686; AEE78225.1; -; Genomic_DNA. DR EMBL; OZ408685; CAO7043512.1; -; Genomic_DNA. DR EMBL; AY056807; AAL10498.1; -; mRNA. DR EMBL; AY090236; AAL90900.1; -; mRNA. DR EMBL; BT003012; AAO23577.1; -; mRNA. DR PIR; T45633; T45633. DR RefSeq; NP_190281.1; NM_114564.3. DR PDB; 4BQE; X-ray; 1.70 A; A/B=1-841. DR PDB; 4BQF; X-ray; 2.35 A; A/B=1-841. DR PDB; 4BQI; X-ray; 1.90 A; A/B=1-841. DR AlphaFoldDB; Q9SD76; -. DR SMR; Q9SD76; -. DR BioGRID; 9170; 1. DR FunCoup; Q9SD76; 2181. DR STRING; 3702.Q9SD76; -. DR CAZy; GT35; Glycosyltransferase Family 35. DR GlyGen; Q9SD76; 1 site. DR iPTMnet; Q9SD76; -. DR PaxDb; 3702-Q9SD76; -. DR ProteomicsDB; 236155; -. DR GeneID; 823850; -. DR KEGG; ath:AT3G46970; -. DR Araport; AT3G46970; -. DR TAIR; AT3G46970; PHS2. DR eggNOG; KOG2099; Eukaryota. DR HOGENOM; CLU_010198_2_0_1; -. DR InParanoid; Q9SD76; -. DR OMA; WLKQANP; -. DR PhylomeDB; Q9SD76; -. DR BioCyc; ARA:AT3G46970-MONOMER; -. DR BRENDA; 2.4.1.1; 399. DR CD-CODE; 4299E36E; Nucleolus. DR EvolutionaryTrace; Q9SD76; -. DR PRO; PR:Q9SD76; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9SD76; baseline and differential. DR GO; GO:0009507; C:chloroplast; HDA:TAIR. DR GO; GO:0005737; C:cytoplasm; ISM:TAIR. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IDA:TAIR. DR GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central. DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR. DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1. DR FunFam; 3.40.50.2000:FF:000002; Alpha-1,4 glucan phosphorylase; 1. DR FunFam; 3.40.50.2000:FF:000003; Alpha-1,4 glucan 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:SF4; ALPHA-GLUCAN PHOSPHORYLASE 2, CYTOSOLIC; 1. DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1. DR Pfam; PF00343; Phosphorylase; 1. DR PIRSF; PIRSF000460; Pprylas_GlgP; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. DR PROSITE; PS00102; PHOSPHORYLASE; 1. DR PDBsum; 4BQE; -. DR PDBsum; 4BQF; -. DR PDBsum; 4BQI; -. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Carbohydrate metabolism; Cytoplasm; KW Glycosyltransferase; Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1..841 FT /note="Alpha-glucan phosphorylase 2, cytosolic" FT /id="PRO_0000188541" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 687 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250" FT CONFLICT 31 FT /note="A -> P (in Ref. 4; AAL10498)" FT /evidence="ECO:0000305" FT HELIX 16..18 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 27..40 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 51..80 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 84..88 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 98..104 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 108..117 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 122..126 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 138..152 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 157..162 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 177..181 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 194..206 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 208..211 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 217..235 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 242..251 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 254..256 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 259..263 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 267..270 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 272..280 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 291..318 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 323..325 FT /evidence="ECO:0007829|PDB:4BQF" FT HELIX 328..330 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 331..334 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 335..342 FT /evidence="ECO:0007829|PDB:4BQE" FT TURN 343..346 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 347..353 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 354..358 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 363..373 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 374..377 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 383..385 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 388..390 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 391..397 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 399..419 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 421..426 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 427..430 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 431..434 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 437..439 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 441..443 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 444..451 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 453..459 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 460..465 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 466..470 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 472..477 FT /evidence="ECO:0007829|PDB:4BQE" FT TURN 479..481 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 482..484 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 492..497 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 500..510 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 514..516 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 519..528 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 532..557 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 565..572 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 576..578 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 580..596 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 599..602 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 608..613 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 615..617 FT /evidence="ECO:0007829|PDB:4BQI" FT HELIX 621..638 FT /evidence="ECO:0007829|PDB:4BQE" FT TURN 641..646 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 647..652 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 657..666 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 668..672 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 683..690 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 694..697 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 702..710 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 712..714 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 715..717 FT /evidence="ECO:0007829|PDB:4BQE" FT TURN 722..724 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 725..733 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 741..751 FT /evidence="ECO:0007829|PDB:4BQE" FT TURN 752..755 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 761..764 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 765..767 FT /evidence="ECO:0007829|PDB:4BQE" FT STRAND 769..772 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 781..800 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 802..814 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 817..819 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 821..828 FT /evidence="ECO:0007829|PDB:4BQE" FT HELIX 829..833 FT /evidence="ECO:0007829|PDB:4BQE" SQ SEQUENCE 841 AA; 95159 MW; 4B50C195FBB3F7A7 CRC64; MANANGKAAT SLPEKISAKA NPEADDATEI AGNIVYHAKY SPHFSPLKFG PEQALYATAE SLRDRLIQLW NETYVHFNKV DPKQTYYLSM EYLQGRALTN AIGNLNLQGP YADALRTLGY ELEEIAEQEK DAALGNGGLG RLASCFLDSM ATLNLPAWGY GLRYRHGLFK QIITKKGQEE IPEDWLEKFS PWEIVRHDVV FPVRFFGKVQ VNPDGSRKWV DGDVVQALAY DVPIPGYGTK NTISLRLWEA KARAEDLDLF QFNEGEYELA AQLHSRAQQI CTVLYPGDAT ENGKLLRLKQ QFFLCSASLQ DIISRFHERS TTEGSRKWSE FPSKVAVQMN DTHPTLAIPE LMRLLMDDNG LGWDEAWDVT SKTVAYTNHT VLPEALEKWS QSLMWKLLPR HMEIIEEIDK RFVQTIRDTR VDLEDKISSL SILDNNPQKP VVRMANLCVV SSHTVNGVAQ LHSDILKAEL FADYVSIWPN KFQNKTNGIT PRRWLRFCSP ELSDIITKWL KTDKWITDLD LLTGLRQFAD NEELQSEWAS AKTANKKRLA QYIERVTGVS IDPTSLFDIQ VKRIHEYKRQ LMNILGVVYR FKKLKEMKPE ERKKTVPRTV MIGGKAFATY TNAKRIVKLV NDVGDVVNSD PEVNEYLKVV FVPNYNVTVA EMLIPGSELS QHISTAGMEA SGTSNMKFAL NGCLIIGTLD GANVEIREEV GEENFFLFGA TADQVPRLRK EREDGLFKPD PRFEEAKQFV KSGVFGSYDY GPLLDSLEGN TGFGRGDYFL VGYDFPSYMD AQAKVDEAYK DRKGWLKMSI LSTAGSGKFS SDRTIAQYAK EIWNIEACPV P //