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2,3-bisphosphoglycerate-independent phosphoglycerate mutase (BPG-independent PGAM) (Phosphoglyceromutase) (iPGM) (EC 5.4.2.12)

 A0A0A3J1E3_9BACI        Unreviewed;       514 AA.
A0A0A3J1E3;
04-FEB-2015, integrated into UniProtKB/TrEMBL.
04-FEB-2015, sequence version 1.
07-NOV-2018, entry version 29.
RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01038};
Short=BPG-independent PGAM {ECO:0000256|HAMAP-Rule:MF_01038};
Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01038};
Short=iPGM {ECO:0000256|HAMAP-Rule:MF_01038};
EC=5.4.2.12 {ECO:0000256|HAMAP-Rule:MF_01038};
Name=gpmI {ECO:0000256|HAMAP-Rule:MF_01038};
ORFNames=CD30_09435 {ECO:0000313|EMBL:KGR90751.1};
Lysinibacillus massiliensis 4400831 = CIP 108448 = CCUG 49529.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
Lysinibacillus.
NCBI_TaxID=1211035 {ECO:0000313|EMBL:KGR90751.1, ECO:0000313|Proteomes:UP000030595};
[1] {ECO:0000313|EMBL:KGR90751.1, ECO:0000313|Proteomes:UP000030595}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CCUG 49529 {ECO:0000313|EMBL:KGR90751.1,
ECO:0000313|Proteomes:UP000030595};
Zhang F., Wang G., Zhang L.;
"Draft genome sequence of Lysinibacillus massiliensis CCUG 49529.";
Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
3-phosphoglycerate. {ECO:0000256|SAAS:SAAS00978404}.
-!- FUNCTION: Essential for rapid growth and for sporulation.
Catalyzes the interconversion of 2-phosphoglycerate and 3-
phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01038}.
-!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
{ECO:0000256|HAMAP-Rule:MF_01038, ECO:0000256|SAAS:SAAS00850944}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|HAMAP-Rule:MF_01038};
Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_01038};
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-
Rule:MF_01038, ECO:0000256|SAAS:SAAS00850947}.
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01038}.
-!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
family. {ECO:0000256|HAMAP-Rule:MF_01038,
ECO:0000256|SAAS:SAAS00850933}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KGR90751.1}.
-----------------------------------------------------------------------
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EMBL; JPVQ01000014; KGR90751.1; -; Genomic_DNA.
RefSeq; WP_036175666.1; NZ_JPVQ01000014.1.
ProteinModelPortal; A0A0A3J1E3; -.
EnsemblBacteria; KGR90751; KGR90751; CD30_09435.
UniPathway; UPA00109; UER00186.
Proteomes; UP000030595; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
CDD; cd16010; iPGM; 1.
Gene3D; 3.40.1450.10; -; 1.
Gene3D; 3.40.720.10; -; 1.
HAMAP; MF_01038; GpmI; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR011258; BPG-indep_PGM_N.
InterPro; IPR006124; Metalloenzyme.
InterPro; IPR036646; PGAM_B_sf.
InterPro; IPR005995; Pgm_bpd_ind.
PANTHER; PTHR31637; PTHR31637; 1.
Pfam; PF06415; iPGM_N; 1.
Pfam; PF01676; Metalloenzyme; 1.
PIRSF; PIRSF001492; IPGAM; 1.
SUPFAM; SSF53649; SSF53649; 1.
SUPFAM; SSF64158; SSF64158; 1.
TIGRFAMs; TIGR01307; pgm_bpd_ind; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000030595};
Glycolysis {ECO:0000256|HAMAP-Rule:MF_01038,
ECO:0000256|SAAS:SAAS00850939};
Isomerase {ECO:0000256|HAMAP-Rule:MF_01038,
ECO:0000256|SAAS:SAAS00850936};
Manganese {ECO:0000256|HAMAP-Rule:MF_01038,
ECO:0000256|SAAS:SAAS00456930};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01038,
ECO:0000256|SAAS:SAAS00456876};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01038};
Reference proteome {ECO:0000313|Proteomes:UP000030595};
Sporulation {ECO:0000256|HAMAP-Rule:MF_01038}.
DOMAIN 5 497 Metalloenzyme.
{ECO:0000259|Pfam:PF01676}.
DOMAIN 82 298 iPGM_N. {ECO:0000259|Pfam:PF06415}.
REGION 153 154 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01038}.
REGION 260 263 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01038}.
ACT_SITE 62 62 Phosphoserine intermediate.
{ECO:0000256|HAMAP-Rule:MF_01038}.
METAL 12 12 Manganese 2. {ECO:0000256|HAMAP-
Rule:MF_01038}.
METAL 62 62 Manganese 2. {ECO:0000256|HAMAP-
Rule:MF_01038}.
METAL 402 402 Manganese 1. {ECO:0000256|HAMAP-
Rule:MF_01038}.
METAL 406 406 Manganese 1. {ECO:0000256|HAMAP-
Rule:MF_01038}.
METAL 443 443 Manganese 2. {ECO:0000256|HAMAP-
Rule:MF_01038}.
METAL 444 444 Manganese 2. {ECO:0000256|HAMAP-
Rule:MF_01038}.
METAL 461 461 Manganese 1. {ECO:0000256|HAMAP-
Rule:MF_01038}.
BINDING 123 123 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01038}.
BINDING 185 185 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01038}.
BINDING 191 191 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01038}.
BINDING 335 335 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01038}.
MOD_RES 36 36 Phosphotyrosine. {ECO:0000256|HAMAP-
Rule:MF_01038}.
SEQUENCE 514 AA; 56877 MW; 75ACAADFAD85EFC4 CRC64;
MPKQPVALII LDGFAFRDEV FGNAVAQSSK PNFDRYWNQF PHSTLIASGE AVGLPDEQMG
NSEVGHLNIG AGRIVYQSLT RIHKSIREGD FFKNEKFIEA IEHVKANNSK LHLMGLLSDG
GVHSHYEHLF ALLKLAKQHG VEEVYVHGFL DGRDVGPTTA LGYIEETEKQ MNEIGVGKFA
SIHGRYYSMD RDKRWDRVHL SYNALVDGIG QTAPSAKLGI ENSYSREVYD EFVVPFVVTE
EGSPVATIDS NDAVIFFNFR PDRAIQLSTV FTNDSFVGFK LSEKHPQNLK FVSFTHYSAD
VNALVAFENI DLVNTVGEVI ARNGLTQLRI AETEKYPHVT FFMSGGREEK FPGEERILIP
SPKVATYDLK PEMSAYEVTE ALVSEIQADK FDAILLNFAN PDMVGHSGML EPTIKAIEAV
DECLGKVVDT ILEKGGAAII TADHGNSDEV VTLEGEPMTA HTTNPVPVIV TKQNIEMRDG
GILADLAPTM LKLLGLNQPQ EMTGKPLFEF EKSN


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