Q9PI71 (GPMI_CAMJE) 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
Ordered Locus Names:	Cj0434

Organism

Campylobacter jejuni

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	492 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Manganese Metal-binding
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
flaG	Q0PAW9	1	EBI-1194767,EBI-1191365

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 492	492	2,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP MF_01038		PRO_0000212133
Sites
	Active site	61	1	Phosphoserine intermediate By similarity
	Metal binding	11	1	Manganese 2 By similarity
	Metal binding	61	1	Manganese 2 By similarity
	Metal binding	386	1	Manganese 1 By similarity
	Metal binding	390	1	Manganese 1 By similarity
	Metal binding	427	1	Manganese 2 By similarity
	Metal binding	428	1	Manganese 2 By similarity
	Metal binding	445	1	Manganese 1 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PI71 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 3A8DA60AD0D4C1BC	FASTA	492	55,721
	10 20 30 40 50 60 MKQKCVLIIT DGIGYNKNSK FNAFEAAKKP SYEKLFKEVP NSLLKTSGLA VGLPEGQMGN 70 80 90 100 110 120 SEVGHMCIGS GRIIYQNLVR INKAIENKEL EKNENLKKLL AKCKRVHIIG LYSDGGVHSM 130 140 150 160 170 180 DTHFKAMLEI CAKNGNEVFA HAITDGRDVS PKSGLNFIKD LKEFCENLGV HFATLCGRFY 190 200 210 220 230 240 AMDRDKRWDR VKEYYECLLG KAYKVPNLLE YLQKSYDENV TDEFIKAAQN ENYKGMREED 250 260 270 280 290 300 GIIFINFRND RMKQLVEVLN SKDFKEFERE KIFENLLTMS VYDDKFKLPV LFEKEKIENT 310 320 330 340 350 360 LAQVISKAGL SQLHTAETEK YAHVTFFFNG GKEELLENET RVLIPSPKVK TYDEKPQMSA 370 380 390 400 410 420 FEVCDAVKKG IEKGEDFIVV NFANGDMVGH TGDFNATIKA VEAVDTCLGE ILECAKKHDY 430 440 450 460 470 480 AFIITSDHGN CEAMQDEKGN LLTNHTTFDV FVFVQARGVS KIKDNMGLSN IAASVLKILD 490 LEIPKEMNEA LF

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL111168 Genomic DNA. Translation: CAL34584.1.
PIR	H81387.
RefSeq	YP_002343871.1. NC_002163.1.
3D structure databases
ProteinModelPortal	Q9PI71.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PI71. 35 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	904759.
GenomeReviews	Gene locus Cj0434 in contig AL111168_GR.
KEGG	cje:Cj0434.
PATRIC	20057791. VBICamJej33762_0424.
Phylogenomic databases
HOGENOM	HBG613255.
OMA	DHGNAEL.
ProtClustDB	PRK05434.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ0434-MONOMER.
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.
KO	K15633.
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_CAMJE

Accession

Primary (citable) accession number: Q9PI71
Secondary accession number(s): Q0PB76

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2003
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program