PHS1_ARATH
ID PHS1_ARATH Reviewed; 962 AA.
AC Q9LIB2;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Alpha-glucan phosphorylase 1;
DE Short=AtPHS1;
DE EC=2.4.1.1;
DE AltName: Full=Alpha-glucan phosphorylase, L isozyme;
DE AltName: Full=Starch phosphorylase L;
DE Flags: Precursor;
GN Name=PHS1; OrderedLocusNames=At3g29320; ORFNames=MUO10.17;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=15173560; DOI=10.1104/pp.103.032631;
RA Zeeman S.C., Thorneycroft D., Schupp N., Chapple A., Weck M., Dunstan H.,
RA Haldimann P., Bechtold N., Smith A.M., Smith S.M.;
RT "Plastidial alpha-glucan phosphorylase is not required for starch
RT degradation in Arabidopsis leaves but has a role in the tolerance of
RT abiotic stress.";
RL Plant Physiol. 135:849-858(2004).
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
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). May be not required for the degradation of starch, but the
CC phosphorolysis of starch may play an important role in water stress
CC tolerance. {ECO:0000250, ECO:0000269|PubMed:15173560}.
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: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18431481}.
CC -!- DISRUPTION PHENOTYPE: Small white lesions on the tips or margins of
CC fully expanded leaves. {ECO:0000269|PubMed:15173560}.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
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DR EMBL; AP001309; BAB02576.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77567.1; -; Genomic_DNA.
DR EMBL; AY049235; AAK83578.1; -; mRNA.
DR EMBL; BT003015; AAO23580.1; -; mRNA.
DR RefSeq; NP_189578.1; NM_113857.3.
DR AlphaFoldDB; Q9LIB2; -.
DR SMR; Q9LIB2; -.
DR BioGRID; 7919; 3.
DR IntAct; Q9LIB2; 1.
DR STRING; 3702.AT3G29320.1; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR iPTMnet; Q9LIB2; -.
DR PaxDb; Q9LIB2; -.
DR PRIDE; Q9LIB2; -.
DR ProMEX; Q9LIB2; -.
DR ProteomicsDB; 235063; -.
DR EnsemblPlants; AT3G29320.1; AT3G29320.1; AT3G29320.
DR GeneID; 822590; -.
DR Gramene; AT3G29320.1; AT3G29320.1; AT3G29320.
DR KEGG; ath:AT3G29320; -.
DR Araport; AT3G29320; -.
DR TAIR; locus:2093787; AT3G29320.
DR eggNOG; KOG2099; Eukaryota.
DR HOGENOM; CLU_010198_1_1_1; -.
DR InParanoid; Q9LIB2; -.
DR OMA; KHKRTFT; -.
DR OrthoDB; 240595at2759; -.
DR PhylomeDB; Q9LIB2; -.
DR BioCyc; ARA:AT3G29320-MON; -.
DR BioCyc; MetaCyc:AT3G29320-MON; -.
DR PRO; PR:Q9LIB2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIB2; baseline and differential.
DR Genevisible; Q9LIB2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; TAS:TAIR.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IMP: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:0009266; P:response to temperature stimulus; IEP:TAIR.
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 Allosteric enzyme; Carbohydrate metabolism; Chloroplast;
KW Glycosyltransferase; Plastid; Pyridoxal phosphate; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 64..962
FT /note="Alpha-glucan phosphorylase 1"
FT /id="PRO_0000420843"
FT REGION 525..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 808
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 962 AA; 108585 MW; 54B3C4BBB076CFA5 CRC64;
MDTMRISGVS TGAEVLIQCN SLSSLVSRRC DDGKWRTRMF PARNRDLRPS PTRRSFLSVK
SISSEPKAKV TDAVLDSEQE VFISSMNPFA PDAASVASSI KYHAEFTPLF SPEKFELPKA
FFATAQSVRD ALIMNWNATY EYYNRVNVKQ AYYLSMEFLQ GRALSNAVGN LGLNSAYGDA
LKRLGFDLES VASQEPDPAL GNGGLGRLAS CFLDSMATLN YPAWGYGLRY KYGLFKQRIT
KDGQEEAAED WLELSNPWEI VRNDVSYPIK FYGKVVFGSD GKKRWIGGED IVAVAYDVPI
PGYKTKTTIN LRLWSTKAPS EDFDLSSYNS GKHTEAAEAL FNAEKICFVL YPGDESTEGK
ALRLKQQYTL CSASLQDIVA RFETRSGGNV NWEEFPEKVA VQMNDTHPTL CIPELMRILM
DLKGLSWEDA WKITQRTVAY TNHTVLPEAL EKWSLELMEK LLPRHVEIIE KIDEELVRTI
VSEYGTADPD LLEEKLKAMR ILENVELPSA FADVIVKPVN KPVTAKDAQN GVKTEQEEEK
TAGEEEEDEV IPEPTVEPPK MVRMANLAVV GGHAVNGVAE IHSEIVKQDV FNDFVQLWPE
KFQNKTNGVT PRRWIRFCNP YLSDIITNWI GTEDWVLNTE KVAELRKFAD NEDLQSEWRA
AKKKNKLKVV SLIKERTGYT VSPDAMFDIQ IKRIHEYKRQ LLNILGIVYR YKKMKEMSAS
EREKAFVPRV CIFGGKAFAT YVQAKRIVKF ITDVASTINH DPEIGDLLKV IFVPDYNVSV
AELLIPASEL SQHISTAGME ASGTSNMKFS MNGCVLIGTL DGANVEIREE VGEENFFLFG
AKADQIVNLR KERAEGKFVP DPTFEEVKKF VGSGVFGSNS YDELIGSLEG NEGFGRADYF
LVGKDFPSYI ECQEKVDEAY RDQKRWTRMS IMNTAGSFKF SSDRTIHEYA KDIWNIKQVE
LP
