B1YLD9 (B1YLD9_EXIS2) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
2,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP-Rule MF_01038
Short name=BPG-independent PGAM HAMAP-Rule MF_01038
Short name=Phosphoglyceromutase HAMAP-Rule MF_01038
Short name=iPGM HAMAP-Rule MF_01038
EC=5.4.2.1 HAMAP-Rule MF_01038

Gene names

Name:	gpmI HAMAP-Rule MF_01038
Ordered Locus Names:	Exig_2394 EMBL ACB61844.1

Organism

Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15) [Complete proteome] [HAMAP] EMBL ACB61844.1

Taxonomic identifier

262543 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillales incertae sedis › Bacillales Family XII. Incertae Sedis › Exiguobacterium › Exiguobacterium sibiricum

Protein attributes

Sequence length	515 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. HAMAP-Rule MF_01038 SAAS SAAS005995
Catalytic activity	2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01038 SAAS SAAS005995
Cofactor	Binds 2 manganese ions per subunit By similarity. HAMAP-Rule MF_01038 SAAS SAAS005995
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01038 SAAS SAAS005995
Subunit structure	Monomer By similarity. HAMAP-Rule MF_01038
Sequence similarities	Belongs to the BPG-independent phosphoglycerate mutase family. HAMAP-Rule MF_01038

Ontologies

Keywords
Biological process	Glycolysis HAMAP-Rule MF_01038 SAAS SAAS005995
Ligand	Manganese HAMAP-Rule MF_01038 SAAS SAAS005995 Metal-binding HAMAP-Rule MF_01038 SAAS SAAS005995
Molecular function	Isomerase HAMAP-Rule MF_01038 SAAS SAAS005995 EMBL ACB61844.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	62	1	Phosphoserine intermediate By similarity HAMAP-Rule MF_01038
	Metal binding	12	1	Manganese 2 By similarity HAMAP-Rule MF_01038
	Metal binding	62	1	Manganese 2 By similarity HAMAP-Rule MF_01038
	Metal binding	404	1	Manganese 1 By similarity HAMAP-Rule MF_01038
	Metal binding	408	1	Manganese 1 By similarity HAMAP-Rule MF_01038
	Metal binding	445	1	Manganese 2 By similarity HAMAP-Rule MF_01038
	Metal binding	446	1	Manganese 2 By similarity HAMAP-Rule MF_01038
	Metal binding	463	1	Manganese 1 By similarity HAMAP-Rule MF_01038

Sequences

	Sequence		Length	Mass (Da)
	B1YLD9 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: BFEEB2769B704B93	FASTA	515	56,839
	10 20 30 40 50 60 MKKRPVALII LDGFGMRDEE FGNAVTAANK PNFDRYWEQY PHTLLNAKGE YVGLPEGQMG 70 80 90 100 110 120 NSEVGHLNIG AGRVVYQSLS RINNAIKDRS FFSRQAMNDA AGHVKKYGSA LHIFGLVSDG 130 140 150 160 170 180 GIHSHINHLY AVLEFAKLHE IEKVYLHAFT DGRDCDPQSG AGFLRDAQAK MDELNVGQFA 190 200 210 220 230 240 SVSGRYYAMD RDNRWERVKK VYDVITFADG PTTKDPIAMV EASYKTDVTD EFIEPTVVVQ 250 260 270 280 290 300 EDGTPVAPIH DNDAIMFFNY RPDRAIQLAK TYKEKTGFTG FELPDNVPKN LLLVSMTKYS 310 320 330 340 350 360 DAIDTDIVFP PEDIKNTLGE TLSKQGLKQL RIAETEKYPH VTFFFNGQRE EPYEGEDRIL 370 380 390 400 410 420 IPSPKVATYD LKPEMSVYEV TEALVDAINS DKHDAIILNF ANPDMVGHSG MLEPTKKAIE 430 440 450 460 470 480 AVDKCLGQVV DLIISKGGAA IITADHGNAD KVLNADGSKM TAHTTEPVPC IVTVEDVELL 490 500 510 KPLTGVLADL APTVLDLLGA DQPAEMTGKS IVLKK

References

[1]

"Complete sequence of chromosome of Exiguobacterium sibiricum 255-15." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F. , Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T., Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P. Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 17290 / JCM 13490 / 255-15.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001022 Genomic DNA. Translation: ACB61844.1.
RefSeq	YP_001814861.1. NC_010556.1.
3D structure databases
ProteinModelPortal	B1YLD9.
SMR	B1YLD9. Positions 3-513.
ModBase	Search...
Protein-protein interaction databases
STRING	262543.Exig_2394.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACB61844; ACB61844; Exig_2394.
GeneID	6172955.
KEGG	esi:Exig_2394.
PATRIC	32138420. VBIExiSib53410_2432.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0696.
HOGENOM	HOG000223664.
KO	K15633.
OMA	NAEQMTD.
ProtClustDB	PRK05434.
Enzyme and pathway databases
BioCyc	ESIB262543:GHBP-2475-MONOMER.
UniPathway	UPA00109; UER00186.
Family and domain databases
Gene3D	3.40.1450.10. 1 hit. 3.40.720.10. 2 hits.
HAMAP	MF_01038. GpmI.
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]
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

B1YLD9_EXIS2

Accession

Primary (citable) accession number: B1YLD9

Entry history

Integrated into UniProtKB/TrEMBL:	May 20, 2008
Last sequence update:	May 20, 2008
Last modified:	May 29, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)