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Protein

2,3-bisphosphoglycerate-independent phosphoglycerate mutase

Gene

gpmI

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.1 Publication

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.1 Publication

Cofactori

Mn2+1 PublicationNote: Binds 2 manganese ions per subunit.1 Publication

Pathwayi: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA1)
  4. Enolase (eno), Enolase (eno)
  5. Pyruvate kinase (pykA1), Pyruvate kinase (pyk), Pyruvate kinase (pyk2), Pyruvate kinase (ABW01_15615), Pyruvate kinase (pyk)
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)DescriptionActionsGraphical viewLength
Metal bindingi11Manganese 21 Publication1
Active sitei61Phosphoserine intermediate1 Publication1
Metal bindingi61Manganese 21 Publication1
Binding sitei122SubstrateUniRule annotation1
Binding sitei184SubstrateUniRule annotation1
Binding sitei190SubstrateUniRule annotation1
Binding sitei335SubstrateUniRule annotation1
Metal bindingi402Manganese 11 Publication1
Metal bindingi406Manganese 11 Publication1
Metal bindingi443Manganese 21 Publication1
Metal bindingi444Manganese 21 Publication1
Metal bindingi461Manganese 11 Publication1

GO - Molecular functioni

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

GO - Biological processi

  • glucose catabolic process Source: InterPro
  • glycolytic process Source: TIGR
  • regulation of sporulation Source: UniProtKB
  • sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Glycolysis, Sporulation

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciANTHRA:GPMA-MONOMER.
BRENDAi5.4.2.12. 634.
UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-bisphosphoglycerate-independent phosphoglycerate mutase1 Publication (EC:5.4.2.121 Publication)
Short name:
BPG-independent PGAM1 Publication
Short name:
Phosphoglyceromutase1 Publication
Short name:
iPGM1 Publication
Gene namesi
Name:gpmIUniRule annotation
Synonyms:gpmA
Ordered Locus Names:BA_5365, GBAA_5365, BAS4986
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002121191 – 5092,3-bisphosphoglycerate-independent phosphoglycerate mutaseAdd BLAST509

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei35PhosphotyrosineUniRule annotation1

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

IntActiQ81X77. 16 interactors.
STRINGi198094.BA_5365.

Structurei

Secondary structure

1509
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Turni23 – 26Combined sources4
Helixi30 – 38Combined sources9
Beta strandi41 – 45Combined sources5
Helixi48 – 51Combined sources4
Helixi61 – 70Combined sources10
Helixi77 – 86Combined sources10
Turni90 – 92Combined sources3
Helixi94 – 106Combined sources13
Beta strandi110 – 115Combined sources6
Helixi125 – 138Combined sources14
Beta strandi143 – 149Combined sources7
Beta strandi151 – 154Combined sources4
Helixi159 – 173Combined sources15
Beta strandi177 – 183Combined sources7
Helixi184 – 187Combined sources4
Helixi194 – 205Combined sources12
Beta strandi211 – 214Combined sources4
Helixi215 – 224Combined sources10
Helixi229 – 231Combined sources3
Beta strandi235 – 238Combined sources4
Beta strandi240 – 245Combined sources6
Beta strandi253 – 256Combined sources4
Turni262 – 264Combined sources3
Helixi265 – 272Combined sources8
Beta strandi291 – 295Combined sources5
Beta strandi303 – 307Combined sources5
Helixi316 – 322Combined sources7
Beta strandi327 – 332Combined sources6
Helixi333 – 335Combined sources3
Helixi336 – 339Combined sources4
Turni340 – 345Combined sources6
Beta strandi354 – 359Combined sources6
Beta strandi365 – 370Combined sources6
Turni371 – 374Combined sources4
Helixi375 – 387Combined sources13
Beta strandi392 – 397Combined sources6
Helixi400 – 405Combined sources6
Helixi410 – 433Combined sources24
Beta strandi437 – 441Combined sources5
Beta strandi443 – 445Combined sources3
Beta strandi466 – 470Combined sources5
Helixi483 – 485Combined sources3
Helixi486 – 494Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IFYX-ray2.38A2-509[»]
ProteinModelPortaliQ81X77.
SMRiQ81X77.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ81X77.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni152 – 153Substrate bindingUniRule annotation2
Regioni260 – 263Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the BPG-independent phosphoglycerate mutase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CJI. Bacteria.
COG0696. LUCA.
HOGENOMiHOG000223664.
KOiK15633.
OMAiLHIATMT.

Family and domain databases

Gene3Di3.40.1450.10. 1 hit.
3.40.720.10. 2 hits.
HAMAPiMF_01038. GpmI. 1 hit.
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.

Q81X77-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKPTALIIL DGFGLREETY GNAVAQAKKP NFDGYWNKFP HTTLTACGEA
60 70 80 90 100
VGLPEGQMGN SEVGHLNIGA GRIVYQSLTR VNVAIREGEF DKNETFQSAI
110 120 130 140 150
KSVKEKGTAL HLFGLLSDGG VHSHMNHMFA LLRLAAKEGV EKVYIHAFLD
160 170 180 190 200
GRDVGPKTAQ SYIDATNEVI KETGVGQFAT ISGRYYSMDR DKRWDRVEKC
210 220 230 240 250
YRAMVNGEGP TYKSAEECVE DSYANGIYDE FVLPSVIVNE DNTPVATIND
260 270 280 290 300
DDAVIFYNFR PDRAIQIARV FTNGDFREFD RGEKVPHIPE FVCMTHFSET
310 320 330 340 350
VDGYVAFKPM NLDNTLGEVV AQAGLKQLRI AETEKYPHVT FFFSGGREAE
360 370 380 390 400
FPGEERILIN SPKVATYDLK PEMSIYEVTD ALVNEIENDK HDVIILNFAN
410 420 430 440 450
CDMVGHSGMM EPTIKAVEAT DECLGKVVEA ILAKDGVALI TADHGNADEE
460 470 480 490 500
LTSEGEPMTA HTTNPVPFIV TKNDVELRED GILGDIAPTM LTLLGVEQPK

EMTGKTIIK
Length:509
Mass (Da):56,281
Last modified:June 1, 2003 - v1
Checksum:i37C82D810978B430
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP29025.1.
AE017334 Genomic DNA. Translation: AAT34499.1.
AE017225 Genomic DNA. Translation: AAT57275.1.
RefSeqiNP_847539.1. NC_003997.3.
WP_001231153.1. NZ_LHUO01000001.1.
YP_031225.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP29025; AAP29025; BA_5365.
AAT34499; AAT34499; GBAA_5365.
AAT57275; AAT57275; BAS4986.
GeneIDi1084903.
2851858.
KEGGiban:BA_5365.
bar:GBAA_5365.
bat:BAS4986.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP29025.1.
AE017334 Genomic DNA. Translation: AAT34499.1.
AE017225 Genomic DNA. Translation: AAT57275.1.
RefSeqiNP_847539.1. NC_003997.3.
WP_001231153.1. NZ_LHUO01000001.1.
YP_031225.1. NC_005945.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IFYX-ray2.38A2-509[»]
ProteinModelPortaliQ81X77.
SMRiQ81X77.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ81X77. 16 interactors.
STRINGi198094.BA_5365.

Protocols and materials databases

DNASUi1084903.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP29025; AAP29025; BA_5365.
AAT34499; AAT34499; GBAA_5365.
AAT57275; AAT57275; BAS4986.
GeneIDi1084903.
2851858.
KEGGiban:BA_5365.
bar:GBAA_5365.
bat:BAS4986.

Phylogenomic databases

eggNOGiENOG4105CJI. Bacteria.
COG0696. LUCA.
HOGENOMiHOG000223664.
KOiK15633.
OMAiLHIATMT.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciANTHRA:GPMA-MONOMER.
BRENDAi5.4.2.12. 634.

Miscellaneous databases

EvolutionaryTraceiQ81X77.

Family and domain databases

Gene3Di3.40.1450.10. 1 hit.
3.40.720.10. 2 hits.
HAMAPiMF_01038. GpmI. 1 hit.
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...

Entry informationi

Entry nameiGPMI_BACAN
AccessioniPrimary (citable) accession number: Q81X77
Secondary accession number(s): Q6HR13, Q6KKD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.