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ADP-glucose phosphorylase (EC 2.7.7.-) (ADP-glucose:phosphate adenylyltransferase)

 AGLUP_ARATH             Reviewed;         351 AA.
Q9FK51; Q8LB75;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
05-DEC-2018, entry version 123.
RecName: Full=ADP-glucose phosphorylase;
EC=2.7.7.-;
AltName: Full=ADP-glucose:phosphate adenylyltransferase;
OrderedLocusNames=At5g18200; ORFNames=MRG7.16;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9734815; DOI=10.1093/dnares/5.3.203;
Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. VI.
Sequence features of the regions of 1,367,185 bp covered by 19
physically assigned P1 and TAC clones.";
DNA Res. 5:203-216(1998).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) IN COMPLEX WITH AMP AND ZINC
IONS, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, ACTIVE SITE, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16519510; DOI=10.1021/bi052232m;
McCoy J.G., Arabshahi A., Bitto E., Bingman C.A., Ruzicka F.J.,
Frey P.A., Phillips G.N. Jr.;
"Structure and mechanism of an ADP-glucose phosphorylase from
Arabidopsis thaliana.";
Biochemistry 45:3154-3162(2006).
[6]
X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
ZINC IONS, AND SUBUNIT.
McCoy J.G., Wesenberg G.E., Phillips G.N. Jr., Bitto E., Bingman C.A.;
"Crystal structure of an ADP-glucose phosphorylase from Arabidopsis
thaliana with bound ADP-glucose.";
Submitted (MAY-2006) to the PDB data bank.
[7]
X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) IN COMPLEX WITH AMP AND ZINC
IONS, ACTIVE SITE, AND SUBUNIT.
PubMed=17850744; DOI=10.1016/j.str.2007.06.019;
Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.;
"Ensemble refinement of protein crystal structures: validation and
application.";
Structure 15:1040-1052(2007).
-!- FUNCTION: Catalyzes the conversion of ADP-glucose and inorganic
phosphate (Pi) into glucose-1-phosphate and ADP. Does not possess
galactose-1-phosphate uridylyltransferase activity.
{ECO:0000269|PubMed:16519510}.
-!- CATALYTIC ACTIVITY:
Reaction=ADP + alpha-D-glucose 1-phosphate + H(+) = ADP-alpha-D-
glucose + phosphate; Xref=Rhea:RHEA:47708, ChEBI:CHEBI:15378,
ChEBI:CHEBI:43474, ChEBI:CHEBI:57498, ChEBI:CHEBI:58601,
ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16519510};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:16519510,
ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6};
Note=Binds 2 zinc ions per subunit. {ECO:0000269|PubMed:16519510,
ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6.9 uM for ADP-alpha-D-glucose (at pH 8.5 and 25 degrees
Celsius) {ECO:0000269|PubMed:16519510};
KM=90 uM for phosphate (at pH 8.5 and 25 degrees Celsius)
{ECO:0000269|PubMed:16519510};
Note=kcat is 2.7 sec(-1). {ECO:0000269|PubMed:16519510};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16519510,
ECO:0000269|PubMed:17850744, ECO:0000269|Ref.6}.
-!- MISCELLANEOUS: Functions by a double-displacement chemical
mechanism and ping-pong kinetics through a covalent nucleotidyl-
enzyme intermediate. {ECO:0000269|PubMed:16519510}.
-!- SIMILARITY: Belongs to the galactose-1-phosphate
uridylyltransferase type 1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB012246; BAB09478.1; -; Genomic_DNA.
EMBL; CP002688; AED92518.1; -; Genomic_DNA.
EMBL; BT005792; AAO64194.1; -; mRNA.
EMBL; AY087378; AAM64928.1; -; mRNA.
RefSeq; NP_197321.1; NM_121825.4.
UniGene; At.24598; -.
PDB; 1Z84; X-ray; 1.83 A; A/B=1-351.
PDB; 1ZWJ; X-ray; 2.30 A; A/B=1-351.
PDB; 2H39; X-ray; 2.23 A; A/B=1-351.
PDB; 2Q4H; X-ray; 1.83 A; A/B=1-351.
PDB; 2Q4L; X-ray; 2.30 A; A/B=1-351.
PDBsum; 1Z84; -.
PDBsum; 1ZWJ; -.
PDBsum; 2H39; -.
PDBsum; 2Q4H; -.
PDBsum; 2Q4L; -.
ProteinModelPortal; Q9FK51; -.
SMR; Q9FK51; -.
STRING; 3702.AT5G18200.1; -.
iPTMnet; Q9FK51; -.
PaxDb; Q9FK51; -.
PRIDE; Q9FK51; -.
DNASU; 831938; -.
EnsemblPlants; AT5G18200.1; AT5G18200.1; AT5G18200.
GeneID; 831938; -.
Gramene; AT5G18200.1; AT5G18200.1; AT5G18200.
KEGG; ath:AT5G18200; -.
Araport; AT5G18200; -.
TAIR; locus:2172359; AT5G18200.
eggNOG; KOG2958; Eukaryota.
eggNOG; COG1085; LUCA.
HOGENOM; HOG000230491; -.
InParanoid; Q9FK51; -.
KO; K00965; -.
OMA; HAIYYPP; -.
OrthoDB; EOG09360GMF; -.
PhylomeDB; Q9FK51; -.
BioCyc; ARA:AT5G18200-MONOMER; -.
Reactome; R-ATH-70370; Galactose catabolism.
SABIO-RK; Q9FK51; -.
EvolutionaryTrace; Q9FK51; -.
PRO; PR:Q9FK51; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FK51; baseline and differential.
Genevisible; Q9FK51; AT.
GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
GO; GO:0047345; F:ribose-5-phosphate adenylyltransferase activity; NAS:TAIR.
GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; TAS:TAIR.
GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IEA:InterPro.
GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0080040; P:positive regulation of cellular response to phosphate starvation; IDA:TAIR.
CDD; cd00608; GalT; 1.
Gene3D; 3.30.428.10; -; 2.
InterPro; IPR001937; GalP_UDPtransf1.
InterPro; IPR005849; GalP_Utransf_N.
InterPro; IPR036265; HIT-like_sf.
Pfam; PF01087; GalP_UDP_transf; 1.
PIRSF; PIRSF000808; GalT; 1.
SUPFAM; SSF54197; SSF54197; 2.
TIGRFAMs; TIGR00209; galT_1; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Complete proteome;
Glucose metabolism; Metal-binding; Nucleotidyltransferase;
Reference proteome; Transferase; Zinc.
CHAIN 1 351 ADP-glucose phosphorylase.
/FTId=PRO_0000169887.
REGION 41 44 ADP-alpha-D-glucose binding.
{ECO:0000269|Ref.6}.
REGION 72 74 ADP-alpha-D-glucose binding.
{ECO:0000269|Ref.6}.
REGION 179 182 ADP-alpha-D-glucose binding.
{ECO:0000269|Ref.6}.
REGION 325 326 ADP-alpha-D-glucose binding.
{ECO:0000269|Ref.6}.
ACT_SITE 186 186 Tele-AMP-histidine intermediate.
{ECO:0000269|PubMed:16519510,
ECO:0000269|PubMed:17850744}.
METAL 63 63 Zinc 1. {ECO:0000269|PubMed:16519510,
ECO:0000269|PubMed:17850744,
ECO:0000269|Ref.6}.
METAL 66 66 Zinc 1. {ECO:0000269|PubMed:16519510,
ECO:0000269|PubMed:17850744,
ECO:0000269|Ref.6}.
METAL 133 133 Zinc 1; via pros nitrogen.
{ECO:0000269|PubMed:16519510,
ECO:0000269|PubMed:17850744,
ECO:0000269|Ref.6}.
METAL 184 184 Zinc 1; via pros nitrogen.
{ECO:0000269|PubMed:16519510,
ECO:0000269|PubMed:17850744,
ECO:0000269|Ref.6}.
METAL 216 216 Zinc 2. {ECO:0000269|PubMed:16519510,
ECO:0000269|PubMed:17850744,
ECO:0000269|Ref.6}.
METAL 219 219 Zinc 2. {ECO:0000269|PubMed:16519510,
ECO:0000269|PubMed:17850744,
ECO:0000269|Ref.6}.
METAL 255 255 Zinc 2; via pros nitrogen.
{ECO:0000269|PubMed:16519510,
ECO:0000269|PubMed:17850744,
ECO:0000269|Ref.6}.
METAL 310 310 Zinc 2; via pros nitrogen.
{ECO:0000269|PubMed:16519510,
ECO:0000269|PubMed:17850744,
ECO:0000269|Ref.6}.
BINDING 94 94 ADP-alpha-D-glucose. {ECO:0000269|Ref.6}.
BINDING 173 173 ADP-alpha-D-glucose. {ECO:0000269|Ref.6}.
BINDING 188 188 ADP-alpha-D-glucose. {ECO:0000269|Ref.6}.
BINDING 321 321 ADP-alpha-D-glucose; via carbonyl oxygen.
{ECO:0000269|Ref.6}.
CONFLICT 148 148 I -> V (in Ref. 4; AAM64928).
{ECO:0000305}.
CONFLICT 349 349 S -> N (in Ref. 4; AAM64928).
{ECO:0000305}.
STRAND 24 28 {ECO:0000244|PDB:1Z84}.
TURN 29 32 {ECO:0000244|PDB:1Z84}.
STRAND 33 37 {ECO:0000244|PDB:1Z84}.
HELIX 39 43 {ECO:0000244|PDB:2H39}.
HELIX 45 47 {ECO:0000244|PDB:1Z84}.
HELIX 70 72 {ECO:0000244|PDB:1Z84}.
STRAND 76 81 {ECO:0000244|PDB:1Z84}.
STRAND 88 93 {ECO:0000244|PDB:1Z84}.
STRAND 98 100 {ECO:0000244|PDB:1Z84}.
HELIX 101 103 {ECO:0000244|PDB:1Z84}.
TURN 104 106 {ECO:0000244|PDB:1Z84}.
STRAND 117 119 {ECO:0000244|PDB:1Z84}.
STRAND 123 128 {ECO:0000244|PDB:1Z84}.
STRAND 131 134 {ECO:0000244|PDB:1Z84}.
HELIX 137 139 {ECO:0000244|PDB:1Z84}.
HELIX 142 159 {ECO:0000244|PDB:1Z84}.
STRAND 167 175 {ECO:0000244|PDB:1Z84}.
HELIX 176 178 {ECO:0000244|PDB:1Z84}.
STRAND 186 194 {ECO:0000244|PDB:1Z84}.
HELIX 197 213 {ECO:0000244|PDB:1Z84}.
TURN 217 220 {ECO:0000244|PDB:1Z84}.
HELIX 221 224 {ECO:0000244|PDB:1Z84}.
STRAND 225 230 {ECO:0000244|PDB:1Z84}.
STRAND 232 238 {ECO:0000244|PDB:1Z84}.
STRAND 248 254 {ECO:0000244|PDB:1Z84}.
HELIX 259 261 {ECO:0000244|PDB:1Z84}.
HELIX 264 284 {ECO:0000244|PDB:1Z84}.
STRAND 290 295 {ECO:0000244|PDB:1Z84}.
HELIX 303 308 {ECO:0000244|PDB:1Z84}.
STRAND 312 317 {ECO:0000244|PDB:1Z84}.
HELIX 324 329 {ECO:0000244|PDB:1Z84}.
STRAND 333 336 {ECO:0000244|PDB:1Z84}.
HELIX 338 347 {ECO:0000244|PDB:1Z84}.
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


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