AGLUP_ARATH
ID AGLUP_ARATH Reviewed; 351 AA.
AC Q9FK51; Q8LB75;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=ADP-glucose phosphorylase;
DE EC=2.7.7.-;
DE AltName: Full=ADP-glucose:phosphate adenylyltransferase;
GN OrderedLocusNames=At5g18200; ORFNames=MRG7.16;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) IN COMPLEX WITH AMP AND ZINC IONS,
RP FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, ACTIVE SITE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=16519510; DOI=10.1021/bi052232m;
RA McCoy J.G., Arabshahi A., Bitto E., Bingman C.A., Ruzicka F.J., Frey P.A.,
RA Phillips G.N. Jr.;
RT "Structure and mechanism of an ADP-glucose phosphorylase from Arabidopsis
RT thaliana.";
RL Biochemistry 45:3154-3162(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ZINC
RP IONS, AND SUBUNIT.
RA McCoy J.G., Wesenberg G.E., Phillips G.N. Jr., Bitto E., Bingman C.A.;
RT "Crystal structure of an ADP-glucose phosphorylase from Arabidopsis
RT thaliana with bound ADP-glucose.";
RL Submitted (MAY-2006) to the PDB data bank.
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) IN COMPLEX WITH AMP AND ZINC IONS,
RP ACTIVE SITE, AND SUBUNIT.
RX PubMed=17850744; DOI=10.1016/j.str.2007.06.019;
RA Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.;
RT "Ensemble refinement of protein crystal structures: validation and
RT application.";
RL Structure 15:1040-1052(2007).
CC -!- FUNCTION: Catalyzes the conversion of ADP-glucose and inorganic
CC phosphate (Pi) into glucose-1-phosphate and ADP. Does not possess
CC galactose-1-phosphate uridylyltransferase activity.
CC {ECO:0000269|PubMed:16519510}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + alpha-D-glucose 1-phosphate + H(+) = ADP-alpha-D-glucose
CC + phosphate; Xref=Rhea:RHEA:47708, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57498, ChEBI:CHEBI:58601,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16519510};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16519510, ECO:0000269|PubMed:17850744,
CC ECO:0000269|Ref.6};
CC Note=Binds 2 zinc ions per subunit. {ECO:0000269|PubMed:16519510,
CC ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.9 uM for ADP-alpha-D-glucose (at pH 8.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:16519510};
CC KM=90 uM for phosphate (at pH 8.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:16519510};
CC Note=kcat is 2.7 sec(-1). {ECO:0000269|PubMed:16519510};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16519510,
CC ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6}.
CC -!- MISCELLANEOUS: Functions by a double-displacement chemical mechanism
CC and ping-pong kinetics through a covalent nucleotidyl-enzyme
CC intermediate. {ECO:0000269|PubMed:16519510}.
CC -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC type 1 family. {ECO:0000305}.
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DR EMBL; AB012246; BAB09478.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92518.1; -; Genomic_DNA.
DR EMBL; BT005792; AAO64194.1; -; mRNA.
DR EMBL; AY087378; AAM64928.1; -; mRNA.
DR RefSeq; NP_197321.1; NM_121825.4.
DR PDB; 1Z84; X-ray; 1.83 A; A/B=1-351.
DR PDB; 1ZWJ; X-ray; 2.30 A; A/B=1-351.
DR PDB; 2H39; X-ray; 2.23 A; A/B=1-351.
DR PDB; 2Q4H; X-ray; 1.83 A; A/B=1-351.
DR PDB; 2Q4L; X-ray; 2.30 A; A/B=1-351.
DR PDBsum; 1Z84; -.
DR PDBsum; 1ZWJ; -.
DR PDBsum; 2H39; -.
DR PDBsum; 2Q4H; -.
DR PDBsum; 2Q4L; -.
DR AlphaFoldDB; Q9FK51; -.
DR SMR; Q9FK51; -.
DR STRING; 3702.AT5G18200.1; -.
DR iPTMnet; Q9FK51; -.
DR PaxDb; Q9FK51; -.
DR PRIDE; Q9FK51; -.
DR ProteomicsDB; 244771; -.
DR DNASU; 831938; -.
DR EnsemblPlants; AT5G18200.1; AT5G18200.1; AT5G18200.
DR GeneID; 831938; -.
DR Gramene; AT5G18200.1; AT5G18200.1; AT5G18200.
DR KEGG; ath:AT5G18200; -.
DR Araport; AT5G18200; -.
DR TAIR; locus:2172359; AT5G18200.
DR eggNOG; KOG2958; Eukaryota.
DR HOGENOM; CLU_029960_1_0_1; -.
DR InParanoid; Q9FK51; -.
DR OMA; HAIYYPP; -.
DR OrthoDB; 1135699at2759; -.
DR PhylomeDB; Q9FK51; -.
DR BioCyc; ARA:AT5G18200-MON; -.
DR SABIO-RK; Q9FK51; -.
DR EvolutionaryTrace; Q9FK51; -.
DR PRO; PR:Q9FK51; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK51; baseline and differential.
DR Genevisible; Q9FK51; AT.
DR GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047345; F:ribose-5-phosphate adenylyltransferase activity; NAS:TAIR.
DR GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:TAIR.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0080040; P:positive regulation of cellular response to phosphate starvation; IDA:TAIR.
DR CDD; cd00608; GalT; 1.
DR Gene3D; 3.30.428.10; -; 2.
DR InterPro; IPR001937; GalP_UDPtransf1.
DR InterPro; IPR005849; GalP_Utransf_N.
DR InterPro; IPR036265; HIT-like_sf.
DR Pfam; PF01087; GalP_UDP_transf; 1.
DR PIRSF; PIRSF000808; GalT; 1.
DR SUPFAM; SSF54197; SSF54197; 2.
DR TIGRFAMs; TIGR00209; galT_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glucose metabolism; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase; Zinc.
FT CHAIN 1..351
FT /note="ADP-glucose phosphorylase"
FT /id="PRO_0000169887"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 186
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000269|PubMed:16519510,
FT ECO:0000269|PubMed:17850744"
FT BINDING 41..44
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16519510,
FT ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16519510,
FT ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6"
FT BINDING 72..74
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 94
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16519510,
FT ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6"
FT BINDING 173
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 179..182
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16519510,
FT ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6"
FT BINDING 188
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16519510,
FT ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16519510,
FT ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16519510,
FT ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16519510,
FT ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6"
FT BINDING 321
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 325..326
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000269|Ref.6"
FT CONFLICT 148
FT /note="I -> V (in Ref. 4; AAM64928)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="S -> N (in Ref. 4; AAM64928)"
FT /evidence="ECO:0000305"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:1Z84"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1Z84"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:2H39"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1Z84"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1Z84"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1Z84"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:1Z84"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1Z84"
FT HELIX 142..159
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:1Z84"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:1Z84"
FT HELIX 197..213
FT /evidence="ECO:0007829|PDB:1Z84"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:1Z84"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:1Z84"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1Z84"
FT HELIX 264..284
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:1Z84"
FT HELIX 303..308
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:1Z84"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:1Z84"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:1Z84"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:1Z84"
SQ SEQUENCE 351 AA; 39005 MW; 3C62EFE9129C67A7 CRC64;
MTSPSHASDR GGGDGDSVEN QSPELRKDPV TNRWVIFSPA RAKRPTDFKS KSPQNPNPKP
SSCPFCIGRE QECAPELFRV PDHDPNWKLR VIENLYPALS RNLETQSTQP ETGTSRTIVG
FGFHDVVIES PVHSIQLSDI DPVGIGDILI AYKKRINQIA QHDSINYIQV FKNQGASAGA
SMSHSHSQMM ALPVVPPTVS SRLDGTKDYF EETGKCCLCE AKSKHFVIDE SSHFVSVAPF
AATYPFEIWI IPKDHSSHFH HLDDVKAVDL GGLLKLMLQK IAKQLNDPPY NYMIHTSPLK
VTESQLPYTH WFLQIVPQLS GVGGFEIGTG CYINPVFPED VAKVMREVSL T
