Reviewed, UniProtKB/Swiss-Prot Q1LTL3 (GPMA_BAUCH)

Names and origin

Protein names

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

Gene names

Name:	gpmA
Ordered Locus Names:	BCI_0251

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	237 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity.
Catalytic activity	2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01039
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP MF_01039
Sequence similarities	Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Ontologies

Keywords
Biological process	Glycolysis
Molecular function	Isomerase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: HAMAP
Molecular function	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 237	237	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP MF_01039		PRO_1000064031
Sites
	Active site	11	1	Tele-phosphohistidine intermediate By similarity
	Active site	184	1	By similarity
	Site	62	1	Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1LTL3-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 0CFFDEFBF8DCCFF9	FASTA	237	27,619
	10 20 30 40 50 60 MTLNKLVLIR HGESKWNNEN RFTGWTDIDL SDQGRIEAKN AGQLLKQAGF IFDFAYTSVL 70 80 90 100 110 120 KRAIHTLWYI LDELDQAWLP VEKSWRLNER HYGALQGLNK KKITVEYGEE QVQQWRRSLN 130 140 150 160 170 180 ITPPELSDND KRLPIYDIRY AKLSLDQLPK AESLAMTINR IIPYWKGEIL PRINNGERVI 190 200 210 220 230 IAAHGNSIRA IITLLDQLSE NELIQLNIPT GVPIIYEFNS QIKTIKHYYL SIVNKDY

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000238 Genomic DNA. Translation: ABF13818.1.
RefSeq	YP_588701.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4056147.
GenomeReviews	Gene locus BCI_0251 in contig CP000238_GR.
KEGG	bci:BCI_0251.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1LTL3.
OMA	Q1LTL3. FMLWRRS.
Family and domain databases
HAMAP	MF_01039. [Tree]
InterPro	IPR001345. PG/BPGM_mutase. IPR013078. PG_mutase. IPR005952. Phosphogly_mut1. [Graphical view]
PANTHER	PTHR11931. Phosphogly_mut1. 1 hit.
Pfam	PF00300. PGAM. 1 hit. [Graphical view]
TIGRFAMs	TIGR01258. pgm_1. 1 hit.
PROSITE	PS00175. PG_MUTASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPMA_BAUCH

Accession

Primary (citable) accession number: Q1LTL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	May 30, 2006
Last modified:	June 16, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)