Reviewed, UniProtKB/Swiss-Prot Q74LL9 (GPMA1_LACJO)

Names and origin

Protein names

Recommended name:
    2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1
      Short name=Phosphoglyceromutase 1
      Short name=PGAM 1
      Short name=BPG-dependent PGAM 1
      Short name=dPGM 1
    EC=5.4.2.1

Gene names

Name:	gpmA1
Ordered Locus Names:	LJ_0164

Organism

Lactobacillus johnsonii [Complete proteome] [HAMAP]

Taxonomic identifier

33959 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	230 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 – 230	230	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1 HAMAP MF_01039		PRO_0000179883
Sites
	Active site	9	1	Tele-phosphohistidine intermediate By similarity
	Active site	182	1	By similarity
	Site	60	1	Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q74LL9-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 80548C8D2DE13021	FASTA	230	26,609
	10 20 30 40 50 60 MSKLVLIRHG QSEWNLSNQF TGWVDVNLSE KGVEEAKKAG RLIKEHGLEF DQAYTSLLTR 70 80 90 100 110 120 AIKTLHYALE ESDQLWIPET KTWRLNERHY GALQGLNKKD TAEKYGDEQV HIWRRSYDVL 130 140 150 160 170 180 PPAIDDDNEY SQAHDRRYAN LDPHIVPKAE NLHVTLDRVM PFWEDHIAPD LLDGKNVIIA 190 200 210 220 230 AHGNSLRALT KYIENISDDD IMDLEMKTGE PVVYTFDDKL DVVNKEKLDD

References

[1]

"The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533." Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C., Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R., Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A. Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004) [PubMed: 14983040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCC 533.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017198 Genomic DNA. Translation: AAS08146.1.
RefSeq	NP_964180.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2742757.
GenomeReviews	Gene locus LJ_0164 in contig AE017198_GR.
KEGG	ljo:LJ0164.
NMPDR	fig|257314.1.peg.166.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q74LL9.
OMA	FMLWRRS.
Enzyme and pathway databases
BioCyc	LJOH257314:LJ_0164-MON.
BRENDA	5.4.2.1. 141476.
Family and domain databases
HAMAP	MF_01039. [Tree]
InterPro	IPR001345. PG/BPGM_mutase_AC. 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

GPMA1_LACJO

Accession

Primary (citable) accession number: Q74LL9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 5, 2004
Last modified:	November 3, 2009
This is version 36 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)