UniProtKB - Q81X77 (GPMI_BACAN)
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Protein
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Gene
gpmI
Organism
Bacillus anthracis
Status
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
: glycolysis Pathwayi
This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotationProteins known to be involved in the 5 steps of the subpathway in this organism are:
- no protein annotated in this organism
- Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk)
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 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-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA1), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
- Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno)
- Pyruvate kinase (pykA1), Pyruvate kinase (MCCC1A01412_07425), Pyruvate kinase (pyk), Pyruvate kinase (COJ30_11890), Pyruvate kinase (pyk2), Pyruvate kinase (COE56_07990), Pyruvate kinase (BVG01_09765), Pyruvate kinase (pyk), Pyruvate kinase (pyk), Pyruvate kinase (CN488_18960), Pyruvate kinase (CON16_24335), Pyruvate kinase (CN272_12880), Pyruvate kinase (pyk), Pyruvate kinase (pyk), Pyruvate kinase (pykA1), Pyruvate kinase (A9486_00415), Pyruvate kinase (CN907_26205), Pyruvate kinase (COK92_16395), Pyruvate kinase (pyk), Pyruvate kinase (CN286_13255), Pyruvate kinase (A9486_15570), Pyruvate kinase (CN504_15055), Pyruvate kinase (ABW01_15615), Pyruvate kinase (pyk), Pyruvate kinase (pyk)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 11 | Manganese 21 Publication | 1 | |
Active sitei | 61 | Phosphoserine intermediate1 Publication | 1 | |
Metal bindingi | 61 | Manganese 21 Publication | 1 | |
Binding sitei | 122 | SubstrateUniRule annotation | 1 | |
Binding sitei | 184 | SubstrateUniRule annotation | 1 | |
Binding sitei | 190 | SubstrateUniRule annotation | 1 | |
Binding sitei | 335 | SubstrateUniRule annotation | 1 | |
Metal bindingi | 402 | Manganese 11 Publication | 1 | |
Metal bindingi | 406 | Manganese 11 Publication | 1 | |
Metal bindingi | 443 | Manganese 21 Publication | 1 | |
Metal bindingi | 444 | Manganese 21 Publication | 1 | |
Metal bindingi | 461 | Manganese 11 Publication | 1 |
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
Keywordsi
Molecular function | Isomerase |
Biological process | Glycolysis, Sporulation |
Ligand | Manganese, Metal-binding |
Enzyme and pathway databases
BRENDAi | 5.4.2.12 634 |
UniPathwayi | UPA00109; 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 |
Organismi | Bacillus anthracis |
Taxonomic identifieri | 1392 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000212119 | 1 – 509 | 2,3-bisphosphoglycerate-independent phosphoglycerate mutaseAdd BLAST | 509 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 35 | PhosphotyrosineUniRule annotation | 1 |
Keywords - PTMi
PhosphoproteinInteractioni
Subunit structurei
Monomer.UniRule annotation
Protein-protein interaction databases
IntActi | Q81X77 16 interactors. |
STRINGi | 260799.BAS4986 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Beta strandi | 5 – 9 | Combined sources | 5 | |
Turni | 23 – 26 | Combined sources | 4 | |
Helixi | 30 – 38 | Combined sources | 9 | |
Beta strandi | 41 – 45 | Combined sources | 5 | |
Helixi | 48 – 51 | Combined sources | 4 | |
Helixi | 61 – 70 | Combined sources | 10 | |
Helixi | 77 – 86 | Combined sources | 10 | |
Turni | 90 – 92 | Combined sources | 3 | |
Helixi | 94 – 106 | Combined sources | 13 | |
Beta strandi | 110 – 115 | Combined sources | 6 | |
Helixi | 125 – 138 | Combined sources | 14 | |
Beta strandi | 143 – 149 | Combined sources | 7 | |
Beta strandi | 151 – 154 | Combined sources | 4 | |
Helixi | 159 – 173 | Combined sources | 15 | |
Beta strandi | 177 – 183 | Combined sources | 7 | |
Helixi | 184 – 187 | Combined sources | 4 | |
Helixi | 194 – 205 | Combined sources | 12 | |
Beta strandi | 211 – 214 | Combined sources | 4 | |
Helixi | 215 – 224 | Combined sources | 10 | |
Helixi | 229 – 231 | Combined sources | 3 | |
Beta strandi | 235 – 238 | Combined sources | 4 | |
Beta strandi | 240 – 245 | Combined sources | 6 | |
Beta strandi | 253 – 256 | Combined sources | 4 | |
Turni | 262 – 264 | Combined sources | 3 | |
Helixi | 265 – 272 | Combined sources | 8 | |
Beta strandi | 291 – 295 | Combined sources | 5 | |
Beta strandi | 303 – 307 | Combined sources | 5 | |
Helixi | 316 – 322 | Combined sources | 7 | |
Beta strandi | 327 – 332 | Combined sources | 6 | |
Helixi | 333 – 335 | Combined sources | 3 | |
Helixi | 336 – 339 | Combined sources | 4 | |
Turni | 340 – 345 | Combined sources | 6 | |
Beta strandi | 354 – 359 | Combined sources | 6 | |
Beta strandi | 365 – 370 | Combined sources | 6 | |
Turni | 371 – 374 | Combined sources | 4 | |
Helixi | 375 – 387 | Combined sources | 13 | |
Beta strandi | 392 – 397 | Combined sources | 6 | |
Helixi | 400 – 405 | Combined sources | 6 | |
Helixi | 410 – 433 | Combined sources | 24 | |
Beta strandi | 437 – 441 | Combined sources | 5 | |
Beta strandi | 443 – 445 | Combined sources | 3 | |
Beta strandi | 466 – 470 | Combined sources | 5 | |
Helixi | 483 – 485 | Combined sources | 3 | |
Helixi | 486 – 494 | Combined sources | 9 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2IFY | X-ray | 2.38 | A | 2-509 | [»] | |
ProteinModelPortali | Q81X77 | |||||
SMRi | Q81X77 | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q81X77 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 152 – 153 | Substrate bindingUniRule annotation | 2 | |
Regioni | 260 – 263 | Substrate bindingUniRule annotation | 4 |
Sequence similaritiesi
Belongs to the BPG-independent phosphoglycerate mutase family.UniRule annotation
Phylogenomic databases
eggNOGi | ENOG4105CJI Bacteria COG0696 LUCA |
HOGENOMi | HOG000223664 |
KOi | K15633 |
OMAi | FMDGRDT |
Family and domain databases
CDDi | cd16010 iPGM, 1 hit |
Gene3Di | 3.40.1450.101 hit 3.40.720.102 hits |
HAMAPi | MF_01038 GpmI, 1 hit |
InterProi | View protein in InterPro IPR017849 Alkaline_Pase-like_a/b/a IPR017850 Alkaline_phosphatase_core_sf IPR011258 BPG-indep_PGM_N IPR006124 Metalloenzyme IPR036646 PGAM_B_sf IPR005995 Pgm_bpd_ind |
PANTHERi | PTHR31637 PTHR31637, 1 hit |
Pfami | View protein in Pfam PF06415 iPGM_N, 1 hit PF01676 Metalloenzyme, 1 hit |
PIRSFi | PIRSF001492 IPGAM, 1 hit |
SUPFAMi | SSF53649 SSF53649, 2 hits SSF64158 SSF64158, 1 hit |
TIGRFAMsi | TIGR01307 pgm_bpd_ind, 1 hit |
i Sequence
Sequence statusi: Complete.
Q81X77-1 [UniParc]FASTAAdd to basket
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
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 |
RefSeqi | NP_847539.1, NC_003997.3 WP_001231153.1, NZ_NRJB01000007.1 YP_031225.1, NC_005945.1 |
Genome annotation databases
EnsemblBacteriai | AAP29025; AAP29025; BA_5365 AAT34499; AAT34499; GBAA_5365 AAT57275; AAT57275; BAS4986 |
GeneIDi | 1084903 2851858 |
KEGGi | ban:BA_5365 bar:GBAA_5365 bat:BAS4986 |
PATRICi | fig|198094.11.peg.5324 |
Similar proteinsi
Entry informationi
Entry namei | GPMI_BACAN | |
Accessioni | Q81X77Primary (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: | April 25, 2018 | |
This is version 121 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |