Reviewed, UniProtKB/Swiss-Prot Q9SCY0 (PGMP_ARATH)

Names and origin

Protein names

Recommended name:
    Phosphoglucomutase, chloroplastic
      Short name=PGM
    EC=5.4.2.2
Alternative name(s):
    Glucose phosphomutase

Gene names

Name:	PGMP
Synonyms:	PGM
Ordered Locus Names:	At5g51820
ORF Names:	MIO24.4

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	623 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This enzyme participates in both the breakdown and synthesis of glucose By similarity.
Catalytic activity	Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Subcellular location	Plastid › chloroplast.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	detection of gravity Inferred from mutant phenotype. Source: TAIR glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW response to cold Inferred from expression pattern. Source: TAIR starch biosynthetic process Ref.1 Ref.2 Inferred from mutant phenotype. Source: TAIR
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast envelope Inferred from direct assay. Source: TAIR chloroplast stroma Ref.2 Inferred from direct assay. Source: TAIR stromule Inferred from direct assay. Source: TAIR
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglucomutase activity Ref.1 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 63	63	Chloroplast Potential
	Chain	64 – 623	560	Phosphoglucomutase, chloroplastic		PRO_0000023895
Sites
	Active site	181	1	Phosphoserine intermediate By similarity
	Metal binding	181	1	Magnesium; via phosphate group By similarity
	Metal binding	346	1	Magnesium By similarity
	Metal binding	348	1	Magnesium By similarity
	Metal binding	350	1	Magnesium By similarity
Amino acid modifications
	Modified residue	181	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	439	1	G → V in CAB64725. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9SCY0-1 [UniParc]. Last modified January 24, 2001. Version 2. Checksum: 3D4A0D8132EF90F1	FASTA	623	67,989
	10 20 30 40 50 60 MTSTYTRFDT VFLFSRFAGA KYSPLLPSPS FTLSTSGIHI RTKPNSRFHS IIASSSSSSV 70 80 90 100 110 120 VAGTDSIEIK SLPTKPIEGQ KTGTSGLRKK VKVFMEDNYL ANWIQALFNS LPLEDYKNAT 130 140 150 160 170 180 LVLGGDGRYF NKEASQIIIK IAAGNGVGQI LVGKEGILST PAVSAVIRKR KANGGFIMSA 190 200 210 220 230 240 SHNPGGPEYD WGIKFNYSSG QPAPETITDK IYGNTLSISE IKVAEIPDID LSQVGVTKYG 250 260 270 280 290 300 NFSVEVIDPV SDYLELMEDV FDFDLIRGLL SRSDFGFMFD AMHAVTGAYA KPIFVDNLGA 310 320 330 340 350 360 KPDSISNGVP LEDFGHGHPD PNLTYAKDLV DVMYRDNGPD FGAASDGDGD RNMVLGNKFF 370 380 390 400 410 420 VTPSDSVAII AANAQEAIPY FRAGPKGLAR SMPTSGALDR VAEKLKLPFF EVPTGWKFFG 430 440 450 460 470 480 NLMDAGKLSI CGEESFGTGS DHIREKDGIW AVLAWLSILA HRNKDTKPGD KLVSVADVVK 490 500 510 520 530 540 EYWATYGRNF FSRYDYEECE SEGANKMIEY LREILSKSKA GDVYGNYVLQ FADDFSYTDP 550 560 570 580 590 600 VDGSVASKQG VRFVFTDGSR IIFRLSGTGS AGATVRIYIE QFEPDVSKHD VDAQIALKPL 610 620 IDLALSVSKL KDFTGREKPT VIT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The plastidic phosphoglucomutase from Arabidopsis. A reversible enzyme reaction with an important role in metabolic control." Periappuram C., Steinhauer L., Barton D.L., Taylor D.C., Chatson B., Zou J. Plant Physiol. 122:1193-1199(2000) [PubMed: 10759515] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Molecular characterisation of a new mutant allele of the plastid phosphoglucomutase in Arabidopsis, and complementation of the mutant with the wild-type cDNA." Kofler H., Haeusler R.E., Schulz B., Groener F., Fluegge U.-I., Weber A. Mol. Gen. Genet. 263:978-986(2000) [PubMed: 10954083] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones." Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S. DNA Res. 5:41-54(1998) [PubMed: 9628582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, MASS SPECTROMETRY. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ242601 mRNA. Translation: CAB64725.1. AF216580 mRNA. Translation: AAG44095.1. AB010074 Genomic DNA. Translation: BAB11251.1. AY099708 mRNA. Translation: AAM20559.1. AY128901 mRNA. Translation: AAM91301.1.
IPI	IPI00526843.
PIR	T52656.
RefSeq	NP_199995.1.
UniGene	At.1528
3D structure databases
HSSP	HSSP built from PDB template 3PMG based on UniProtKB P00949.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9SCY0.
Proteomic databases
PRIDE	Q9SCY0.
Genome annotation databases
GeneID	835257.
GenomeReviews	Gene locus AT5G51820 in contig BA000015_GR.
KEGG	ath:AT5G51820.
NMPDR	fig|3702.1.peg.27055.
Organism-specific databases
TAIR	At5g51820.
Phylogenomic databases
OMA	RNMIVGR.
Enzyme and pathway databases
BRENDA	5.4.2.2. 302.
Gene expression databases
ArrayExpress	Q9SCY0.
Genevestigator	Q9SCY0.
GermOnline	AT5G51820. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR005844. A-D-PHexomutase_a/b/a-I. IPR016055. A-D-PHexomutase_a/b/a-I/II/III. IPR005845. A-D-PHexomutase_a/b/a-II. IPR005846. A-D-PHexomutase_a/b/a-III. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. IPR005841. A-D-PHexomutase_N. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
Pfam	PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF02880. PGM_PMM_III. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view]
PRINTS	PR00509. PGMPMM.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGMP_ARATH

Accession

Primary (citable) accession number: Q9SCY0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	January 24, 2001
Last modified:	November 3, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)