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Protein

2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1

Gene

PGM1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.By similarity

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Pathwayi: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolic (GAPC2), Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic (GAPC1)
  2. no protein annotated in this organism
  3. Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2 (At3g08590), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1 (PGM1)
  4. Enolase 1, chloroplastic (ENO1), Cytosolic enolase 3 (ENO3), Bifunctional enolase 2/transcriptional activator (ENO2)
  5. Pyruvate kinase (At5g08570), Pyruvate kinase (At5g56350), Pyruvate kinase (F1I16_60), Pyruvate kinase (At3g25960), Pyruvate kinase (At5g63680), Plastidial pyruvate kinase 3, chloroplastic (PKP3), Pyruvate kinase (At3g52990), Pyruvate kinase (At2g36580), Pyruvate kinase, Probable pyruvate kinase, cytosolic isozyme (At4g26390), Pyruvate kinase (F8J2_160), Pyruvate kinase (At3g52990), Plastidial pyruvate kinase 2 (PKP2), Pyruvate kinase (T11I18.16), Pyruvate kinase (F1I16_220), Plastidial pyruvate kinase 1, chloroplastic (PKP1), Pyruvate kinase (At5g63680), Pyruvate kinase, Plastidial pyruvate kinase 4, chloroplastic (PKP4)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Manganese 2By similarity
Active sitei80 – 801Phosphoserine intermediateBy similarity
Metal bindingi80 – 801Manganese 2By similarity
Binding sitei139 – 1391SubstrateBy similarity
Binding sitei205 – 2051SubstrateBy similarity
Binding sitei212 – 2121SubstrateBy similarity
Binding sitei360 – 3601SubstrateBy similarity
Metal bindingi429 – 4291Manganese 1By similarity
Metal bindingi433 – 4331Manganese 1By similarity
Metal bindingi470 – 4701Manganese 2By similarity
Metal bindingi471 – 4711Manganese 2By similarity
Metal bindingi500 – 5001Manganese 1By similarity

GO - Molecular functioni

  • 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity Source: TAIR
  • manganese ion binding Source: InterPro

GO - Biological processi

  • glucose catabolic process Source: InterPro
  • glycolytic process Source: UniProtKB-UniPathway
  • pollen development Source: TAIR
  • response to cadmium ion Source: TAIR
  • response to cold Source: TAIR
  • stomatal movement Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT1G09780-MONOMER.
BRENDAi5.4.2.12. 399.
UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1 (EC:5.4.2.12)
Short name:
BPG-independent PGAM 1
Short name:
Phosphoglyceromutase 1
Alternative name(s):
PGAM-I 1
Gene namesi
Name:PGM1
Ordered Locus Names:At1g09780
ORF Names:F21M12.16
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G09780.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • cytosol Source: TAIR
  • mitochondrial envelope Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 5575562,3-bisphosphoglycerate-independent phosphoglycerate mutase 1PRO_0000212108Add
BLAST

Proteomic databases

PaxDbiO04499.
PRIDEiO04499.

PTM databases

iPTMnetiO04499.

Expressioni

Gene expression databases

GenevisibleiO04499. AT.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi3702.AT1G09780.1.

Structurei

3D structure databases

ProteinModelPortaliO04499.
SMRiO04499. Positions 9-555.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni169 – 1702Substrate bindingBy similarity
Regioni285 – 2884Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4513. Eukaryota.
COG0696. LUCA.
HOGENOMiHOG000223664.
InParanoidiO04499.
KOiK15633.
OMAiWTLIKAH.
PhylomeDBiO04499.

Family and domain databases

Gene3Di3.40.1450.10. 1 hit.
3.40.720.10. 2 hits.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR011258. BPG-indep_PGM_N.
IPR006124. Metalloenzyme.
IPR005995. Pgm_bpd_ind.
[Graphical view]
PfamiPF06415. iPGM_N. 1 hit.
PF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF001492. IPGAM. 1 hit.
SUPFAMiSSF53649. SSF53649. 2 hits.
SSF64158. SSF64158. 1 hit.
TIGRFAMsiTIGR01307. pgm_bpd_ind. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O04499-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSSAWKLD DHPKLPKGKT IAVIVLDGWG ESAPDQYNCI HNAPTPAMDS
60 70 80 90 100
LKHGAPDTWT LIKAHGTAVG LPSEDDMGNS EVGHNALGAG RIFAQGAKLC
110 120 130 140 150
DQALASGKIF EGEGFKYVSE SFETNTLHLV GLLSDGGVHS RLDQLQLLIK
160 170 180 190 200
GSAERGAKRI RVHILTDGRD VLDGSSVGFV ETLEADLVAL RENGVDAQIA
210 220 230 240 250
SGGGRMYVTL DRYENDWEVV KRGWDAQVLG EAPHKFKNAV EAVKTLRKEP
260 270 280 290 300
GANDQYLPPF VIVDESGKAV GPIVDGDAVV TFNFRADRMV MHAKALEYED
310 320 330 340 350
FDKFDRVRYP KIRYAGMLQY DGELKLPSRY LVSPPEIDRT SGEYLTHNGV
360 370 380 390 400
STFACSETVK FGHVTFFWNG NRSGYFNEKL EEYVEIPSDS GISFNVQPKM
410 420 430 440 450
KALEIGEKAR DAILSGKFDQ VRVNIPNGDM VGHTGDIEAT VVACEAADLA
460 470 480 490 500
VKMIFDAIEQ VKGIYVVTAD HGNAEDMVKR DKSGKPALDK EGKLQILTSH
510 520 530 540 550
TLKPVPIAIG GPGLAQGVRF RKDLETPGLA NVAATVMNLH GFVAPSDYEP

TLIEVVE
Length:557
Mass (Da):60,580
Last modified:April 30, 2003 - v3
Checksum:iD5FC3D06A963B9AB
GO

Sequence cautioni

The sequence AAB60731.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC000132 Genomic DNA. Translation: AAB60731.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28491.1.
AY150432 mRNA. Translation: AAN12974.1.
BT000773 mRNA. Translation: AAN31912.1.
AY086182 mRNA. Translation: AAM64261.1.
PIRiG86231.
RefSeqiNP_563852.1. NM_100850.2.
UniGeneiAt.24465.

Genome annotation databases

EnsemblPlantsiAT1G09780.1; AT1G09780.1; AT1G09780.
GeneIDi837507.
GrameneiAT1G09780.1; AT1G09780.1; AT1G09780.
KEGGiath:AT1G09780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC000132 Genomic DNA. Translation: AAB60731.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28491.1.
AY150432 mRNA. Translation: AAN12974.1.
BT000773 mRNA. Translation: AAN31912.1.
AY086182 mRNA. Translation: AAM64261.1.
PIRiG86231.
RefSeqiNP_563852.1. NM_100850.2.
UniGeneiAt.24465.

3D structure databases

ProteinModelPortaliO04499.
SMRiO04499. Positions 9-555.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G09780.1.

PTM databases

iPTMnetiO04499.

Proteomic databases

PaxDbiO04499.
PRIDEiO04499.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G09780.1; AT1G09780.1; AT1G09780.
GeneIDi837507.
GrameneiAT1G09780.1; AT1G09780.1; AT1G09780.
KEGGiath:AT1G09780.

Organism-specific databases

TAIRiAT1G09780.

Phylogenomic databases

eggNOGiKOG4513. Eukaryota.
COG0696. LUCA.
HOGENOMiHOG000223664.
InParanoidiO04499.
KOiK15633.
OMAiWTLIKAH.
PhylomeDBiO04499.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciARA:AT1G09780-MONOMER.
BRENDAi5.4.2.12. 399.

Miscellaneous databases

PROiO04499.

Gene expression databases

GenevisibleiO04499. AT.

Family and domain databases

Gene3Di3.40.1450.10. 1 hit.
3.40.720.10. 2 hits.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR011258. BPG-indep_PGM_N.
IPR006124. Metalloenzyme.
IPR005995. Pgm_bpd_ind.
[Graphical view]
PfamiPF06415. iPGM_N. 1 hit.
PF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF001492. IPGAM. 1 hit.
SUPFAMiSSF53649. SSF53649. 2 hits.
SSF64158. SSF64158. 1 hit.
TIGRFAMsiTIGR01307. pgm_bpd_ind. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiPMG1_ARATH
AccessioniPrimary (citable) accession number: O04499
Secondary accession number(s): Q8LD62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: April 30, 2003
Last modified: February 17, 2016
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.