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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), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
  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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi11 – 111Manganese 21 Publication
Active sitei61 – 611Phosphoserine intermediate1 Publication
Metal bindingi61 – 611Manganese 21 Publication
Binding sitei122 – 1221SubstrateUniRule annotation
Binding sitei184 – 1841SubstrateUniRule annotation
Binding sitei190 – 1901SubstrateUniRule annotation
Binding sitei335 – 3351SubstrateUniRule annotation
Metal bindingi402 – 4021Manganese 11 Publication
Metal bindingi406 – 4061Manganese 11 Publication
Metal bindingi443 – 4431Manganese 21 Publication
Metal bindingi444 – 4441Manganese 21 Publication
Metal bindingi461 – 4611Manganese 11 Publication

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.
BANT260799:GJAJ-5060-MONOMER.
BANT261594:GJ7F-5236-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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5095092,3-bisphosphoglycerate-independent phosphoglycerate mutasePRO_0000212119Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351PhosphotyrosineUniRule annotation

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

IntActiQ81X77. 16 interactions.
STRINGi198094.BA_5365.

Structurei

Secondary structure

1
509
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Turni23 – 264Combined sources
Helixi30 – 389Combined sources
Beta strandi41 – 455Combined sources
Helixi48 – 514Combined sources
Helixi61 – 7010Combined sources
Helixi77 – 8610Combined sources
Turni90 – 923Combined sources
Helixi94 – 10613Combined sources
Beta strandi110 – 1156Combined sources
Helixi125 – 13814Combined sources
Beta strandi143 – 1497Combined sources
Beta strandi151 – 1544Combined sources
Helixi159 – 17315Combined sources
Beta strandi177 – 1837Combined sources
Helixi184 – 1874Combined sources
Helixi194 – 20512Combined sources
Beta strandi211 – 2144Combined sources
Helixi215 – 22410Combined sources
Helixi229 – 2313Combined sources
Beta strandi235 – 2384Combined sources
Beta strandi240 – 2456Combined sources
Beta strandi253 – 2564Combined sources
Turni262 – 2643Combined sources
Helixi265 – 2728Combined sources
Beta strandi291 – 2955Combined sources
Beta strandi303 – 3075Combined sources
Helixi316 – 3227Combined sources
Beta strandi327 – 3326Combined sources
Helixi333 – 3353Combined sources
Helixi336 – 3394Combined sources
Turni340 – 3456Combined sources
Beta strandi354 – 3596Combined sources
Beta strandi365 – 3706Combined sources
Turni371 – 3744Combined sources
Helixi375 – 38713Combined sources
Beta strandi392 – 3976Combined sources
Helixi400 – 4056Combined sources
Helixi410 – 43324Combined sources
Beta strandi437 – 4415Combined sources
Beta strandi443 – 4453Combined sources
Beta strandi466 – 4705Combined sources
Helixi483 – 4853Combined sources
Helixi486 – 4949Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ81X77.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni152 – 1532Substrate bindingUniRule annotation
Regioni260 – 2634Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CJI. Bacteria.
COG0696. LUCA.
HOGENOMiHOG000223664.
KOiK15633.
OMAiLHIATMT.
OrthoDBiEOG6HJ22X.

Family and domain databases

Gene3Di3.40.1450.10. 1 hit.
3.40.720.10. 2 hits.
HAMAPiMF_01038. GpmI.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
2IFYX-ray2.38A2-509[»]
ProteinModelPortaliQ81X77.
SMRiQ81X77. Positions 2-509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ81X77. 16 interactions.
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.
OrthoDBiEOG6HJ22X.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciANTHRA:GPMA-MONOMER.
BANT260799:GJAJ-5060-MONOMER.
BANT261594:GJ7F-5236-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.
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. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
    Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
    , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
    Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames / isolate Porton.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestor.
  3. "Complete genome sequence of Bacillus anthracis Sterne."
    Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sterne.
  4. "Structure and molecular mechanism of Bacillus anthracis cofactor-independent phosphoglycerate mutase: a crucial enzyme for spores and growing cells of Bacillus species."
    Nukui M., Mello L.V., Littlejohn J.E., Setlow B., Setlow P., Kim K., Leighton T., Jedrzejas M.J.
    Biophys. J. 92:977-988(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.

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: March 16, 2016
This is version 104 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.