PHS2_ARATH
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 03-AUG-2022, entry version 142.
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 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 [4]
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; 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 PDBsum; 4BQE; -.
DR PDBsum; 4BQF; -.
DR PDBsum; 4BQI; -.
DR AlphaFoldDB; Q9SD76; -.
DR SMR; Q9SD76; -.
DR BioGRID; 9170; 1.
DR STRING; 3702.AT3G46970.1; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR iPTMnet; Q9SD76; -.
DR PaxDb; Q9SD76; -.
DR PRIDE; Q9SD76; -.
DR ProteomicsDB; 236155; -.
DR EnsemblPlants; AT3G46970.1; AT3G46970.1; AT3G46970.
DR GeneID; 823850; -.
DR Gramene; AT3G46970.1; AT3G46970.1; AT3G46970.
DR KEGG; ath:AT3G46970; -.
DR Araport; AT3G46970; -.
DR TAIR; locus:2075576; AT3G46970.
DR eggNOG; KOG2099; Eukaryota.
DR HOGENOM; CLU_010198_2_0_1; -.
DR InParanoid; Q9SD76; -.
DR OMA; HCACSVA; -.
DR OrthoDB; 240595at2759; -.
DR PhylomeDB; Q9SD76; -.
DR BioCyc; ARA:AT3G46970-MON; -.
DR BRENDA; 2.4.1.1; 399.
DR PRO; PR:Q9SD76; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SD76; baseline and differential.
DR Genevisible; Q9SD76; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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 GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR PANTHER; PTHR11468; PTHR11468; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR TIGRFAMs; TIGR02093; P_ylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
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. 3; AAL10498)"
FT /evidence="ECO:0000305"
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 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..356
FT /evidence="ECO:0007829|PDB:4BQE"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:4BQI"
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..468
FT /evidence="ECO:0007829|PDB:4BQE"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:4BQE"
FT HELIX 472..477
FT /evidence="ECO:0007829|PDB:4BQE"
FT STRAND 481..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 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..831
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
