Q9X519 (GPMI_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Short name=BPG-independent PGAM
Short name=Phosphoglyceromutase
Short name=iPGM
EC=5.4.2.1

Gene names

Name:	gpmI
Synonyms:	pgm

Organism

Geobacillus stearothermophilus (Bacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	511 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	Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. HAMAP MF_01038
Catalytic activity	2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01038
Cofactor	Binds 2 manganese ions per subunit.
Enzyme regulation	Activity is extremely sensitive to pH. HAMAP MF_01038
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP MF_01038
Subunit structure	Monomer.
Sequence similarities	Belongs to the BPG-independent phosphoglycerate mutase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Manganese Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	manganese ion binding Inferred from electronic annotation. Source: InterPro phosphoglycerate mutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 511

510

2,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP MF_01038

PRO_0000212127

Sites

Active site

62

1

Phosphoserine intermediate

Metal binding

12

1

Manganese 2

Metal binding

62

1

Manganese 2

Metal binding

403

1

Manganese 1

Metal binding

407

1

Manganese 1

Metal binding

444

1

Manganese 2

Metal binding

445

1

Manganese 2

Metal binding

462

1

Manganese 1

Amino acid modifications

Modified residue

36

1

Phosphotyrosine By similarity

Experimental info

Mutagenesis

12

1

D → N: Loss of activity.

Mutagenesis

42

1

H → N: Decrease in activity.

Mutagenesis

62

1

S → A: Loss of activity.

Mutagenesis

66

1

H → N: Strong decrease in activity.

Mutagenesis

123

1

H → N: Strong decrease in activity.

Mutagenesis

125

1

H → N: Decrease in activity.

Mutagenesis

128

1

H → N: 5-fold decrease in activity.

Mutagenesis

261

1

R → L: Loss of activity.

Mutagenesis

407

1

H → N: Loss of activity.

Mutagenesis

445

1

H → N: 5-fold decrease in activity.

Mutagenesis

462

1

H → N: Strong decrease in activity.

Secondary structure

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511

Helix Strand Turn

Details...

Beta strand

6 – 11

6

Helix

24 – 27

4

Helix

31 – 39

9

Beta strand

42 – 46

5

Helix

49 – 52

4

Helix

62 – 71

10

Helix

78 – 87

10

Helix

91 – 93

3

Helix

95 – 107

13

Beta strand

111 – 116

6

Helix

126 – 138

13

Beta strand

144 – 150

7

Beta strand

152 – 155

4

Helix

160 – 174

15

Beta strand

178 – 184

7

Helix

185 – 188

4

Helix

195 – 207

13

Beta strand

212 – 215

4

Helix

216 – 225

10

Helix

230 – 232

3

Beta strand

236 – 239

4

Beta strand

243 – 246

4

Beta strand

254 – 257

4

Turn

263 – 265

3

Helix

266 – 273

8

Beta strand

291 – 296

6

Beta strand

304 – 308

5

Helix

317 – 323

7

Beta strand

328 – 333

6

Helix

334 – 336

3

Helix

337 – 340

4

Turn

341 – 346

6

Beta strand

355 – 360

6

Helix

368 – 370

3

Turn

372 – 375

4

Helix

376 – 388

13

Beta strand

393 – 399

7

Helix

401 – 406

6

Turn

407 – 409

3

Helix

411 – 434

24

Beta strand

438 – 442

5

Beta strand

444 – 447

4

Beta strand

467 – 471

5

Beta strand

480 – 483

4

Helix

484 – 486

3

Helix

487 – 495

9

Sequences

	Sequence		Length	Mass (Da)
	Q9X519 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 45E4F5CEE457A04B	FASTA	511	57,003
	10 20 30 40 50 60 MSKKPVALII LDGFALRDET YGNAVAQANK PNFDRYWNEY PHTTLKACGE AVGLPEGQMG 70 80 90 100 110 120 NSEVGHLNIG AGRIVYQSLT RINIAIREGE FDRNETFLAA MNHVKQHGTS LHLFGLLSDG 130 140 150 160 170 180 GVHSHIHHLY ALLRLAAKEG VKRVYIHGFL DGRDVGPQTA PQYIKELQEK IKEYGVGEIA 190 200 210 220 230 240 TLSGRYYSMD RDKRWDRVEK AYRAMVYGEG PTYRDPLECI EDSYKHGIYD EFVLPSVIVR 250 260 270 280 290 300 EDGRPVATIQ DNDAIIFYNF RPDRAIQISN TFTNEDFREF DRGPKHPKHL FFVCLTHFSE 310 320 330 340 350 360 TVKGYVAFKP TNLDNTIGEV LSQHGLRQLR IAETEKYPHV TFFMSGGREE KFPGEDRILI 370 380 390 400 410 420 NSPKVPTYDL KPEMSAYEVT DALLKEIEAD KYDAIILNYA NPDMVGHSGK LEPTIKAVEA 430 440 450 460 470 480 VDECLGKVVD AILAKGGIAI ITADHGNADE VLTPDGKPQT AHTTNPVPVI VTKKGIKLRD 490 500 510 GGILGDLAPT MLDLLGLPQP KEMTGKSLIV K

References

[1]	"Structural studies on a 2,3-diphosphoglycerate independent phosphoglycerate mutase from Bacillus stearothermophilus." Chander M., Setlow P., Lamani E., Jedrzejas M.J. J. Struct. Biol. 126:156-165(1999) [PubMed: 10388626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8, CHARACTERIZATION.
[2]	"Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus." Jedrzejas M.J., Chander M., Setlow P., Krishnasamy G. EMBO J. 19:1419-1431(2000) [PubMed: 10747010] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MUTAGENESIS.
[3]	"Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate." Jedrzejas M.J., Chander M., Setlow P., Krishnasamy G. J. Biol. Chem. 275:23146-23153(2000) [PubMed: 10764795] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF120091 Genomic DNA. Translation: AAD26328.1.

PIR

T46865.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EJJ	X-ray	1.90	A	1-511	[»]
1EQJ	X-ray	1.70	A	1-511	[»]
1O98	X-ray	1.40	A	1-511	[»]
1O99	X-ray	2.65	A	1-511	[»]

ProteinModelPortal

Q9X519.

SMR

Q9X519. Positions 2-510.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

5.4.2.1. 623.

Family and domain databases

HAMAP

MF_01038. GpmI.
[Tree]

InterPro

IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR011258. BPG-indep_PGM_N.
IPR006124. Metalloenzyme.
IPR005995. Pgm_bpd_ind.
[Graphical view]

Gene3D

G3DSA:3.40.720.10. Alk_phosphtse. 2 hits.
G3DSA:3.40.1450.10. BPG-indep_PGM_N. 1 hit.

Pfam

PF06415. iPGM_N. 1 hit.
PF01676. Metalloenzyme. 1 hit.
[Graphical view]

PIRSF

PIRSF001492. IPGAM. 1 hit.

SUPFAM

SSF53649. Alkaline_phosphatase_core. 1 hit.
SSF64158. BPG-indep_PGM_N. 1 hit.

TIGRFAMs

TIGR01307. Pgm_bpd_ind. 1 hit.

ProtoNet

Search...

Entry information

Entry name

GPMI_GEOSE

Accession

Primary (citable) accession number: Q9X519

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2003
Last sequence update:	January 23, 2007
Last modified:	May 31, 2011
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program