P58814 (APGM_PYRFU) 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=aPGAM
EC=5.4.2.1

Gene names

Name:	apgM
Ordered Locus Names:	PF1959

Organism

Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

Taxonomic identifier

186497 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. HAMAP MF_01402_A
Catalytic activity	2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01402_A
Cofactor	Magnesium Probable.
Enzyme regulation	Inhibited to approximately 20% by EDTA. HAMAP MF_01402_A
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP MF_01402_A
Subunit structure	Homotetramer Probable.
Sequence similarities	Belongs to the BPG-independent phosphoglycerate mutase family. A-PGAM subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 8.0. HAMAP MF_01402_A

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Magnesium
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metal 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
	Chain	1 – 411	411	2,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP MF_01402_A		PRO_0000138144

Sequences

	Sequence		Length	Mass (Da)
	P58814 [UniParc]. Last modified May 2, 2002. Version 1. Checksum: 870587E630C2B104	FASTA	411	45,314
	10 20 30 40 50 60 MKQRKGVLII LDGLGDRPIK ELGGKTPLEY ANTPTMDYLA KIGILGQQDP IKPGQPAGSD 70 80 90 100 110 120 TAHLSIFGYD PYKSYRGRGY FEALGVGLEL DEDDLAFRVN FATLENGVIT DRRAGRISTE 130 140 150 160 170 180 EAHELAKAIQ ENVDIPVDFI FKGATGHRAV LVLKGMAEGY KVGENDPHEA GKPPHPFTWE 190 200 210 220 230 240 DEASKKVAEI LEEFVKKAHE VLDKHPINEK RRKEGKPVAN YLLIRGAGTY PNIPMKFTEQ 250 260 270 280 290 300 WKVKAAAVVA VALVKGVAKA IGFDVYTPKG ATGEYNTDEM AKARKAVELL KDYDFVFIHF 310 320 330 340 350 360 KPTDAAGHDN NPKLKAELIE RADRMIKYIV DHVDLEDVVI AITGDHSTPC EVMNHSGDPV 370 380 390 400 410 PLLIAGGGVR ADYTEKFGER EAMRGGLGRI RGHDIVPIMM DLMNRTEKFG A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences." Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T. Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]	"Molecular characterization of phosphoglycerate mutase in archaea." van der Oost J., Huynen M.A., Verhees C.H. FEMS Microbiol. Lett. 212:111-120(2002) [PubMed: 12076796] [Abstract] Cited for: CHARACTERIZATION. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009950 Genomic DNA. Translation: AAL82083.1.
RefSeq	NP_579688.1. NC_003413.1.
3D structure databases
ProteinModelPortal	P58814.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBPYRT00000004646; EBPYRP00000004507; EBPYRG00000004646.
GeneID	1469841.
GenomeReviews	Gene locus PF1959 in contig AE009950_GR.
KEGG	pfu:PF1959.
NMPDR	fig|186497.1.peg.2011.
Phylogenomic databases
GeneTree	EBGT00050000023120.
HOGENOM	HBG463247.
OMA	DIAFRCN.
ProtClustDB	PRK04024.
Family and domain databases
HAMAP	MF_01402_A. ApgM_A. [Tree]
InterPro	IPR017849. Alkaline_Pase-like_a/b/a. IPR017850. Alkaline_phosphatase_core. IPR023665. ApgAM. IPR004456. BisP-indep_Pglycerate_Mutase. IPR006124. Metalloenzyme. [Graphical view]
Gene3D	G3DSA:3.40.720.10. Alk_phosphtse. 2 hits.
KO	K15635.
Pfam	PF01676. Metalloenzyme. 1 hit. PF10143. PhosphMutase. 1 hit. [Graphical view]
PIRSF	PIRSF006392. IPGAM_arch. 1 hit.
SUPFAM	SSF53649. Alkaline_phosphatase_core. 1 hit.
TIGRFAMs	TIGR00306. ApgM. 1 hit.
ProtoNet	Search...

Entry information

Entry name

APGM_PYRFU

Accession

Primary (citable) accession number: P58814

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	May 2, 2002
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program