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

 GPMI_PSESM              Reviewed;         510 AA.
P52832;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
28-FEB-2018, entry version 121.
RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01038};
Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01038};
Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01038};
Short=iPGM {ECO:0000255|HAMAP-Rule:MF_01038};
EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01038, ECO:0000269|PubMed:7896694};
Name=gpmI {ECO:0000255|HAMAP-Rule:MF_01038};
Synonyms=gpmA {ECO:0000312|EMBL:AAO58753.1},
pgm {ECO:0000303|PubMed:7896694}; OrderedLocusNames=PSPTO_5327;
Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=223283;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
DISRUPTION PHENOTYPE.
STRAIN=ATCC BAA-871 / DC3000;
PubMed=7896694; DOI=10.1128/jb.177.7.1727-1733.1995;
Morris V.L., Jackson D.P., Grattan M., Ainsworth T., Cuppels D.A.;
"Isolation and sequence analysis of the Pseudomonas syringae pv.
tomato gene encoding a 2,3-diphosphoglycerate-independent
phosphoglyceromutase.";
J. Bacteriol. 177:1727-1733(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-871 / DC3000;
PubMed=12928499; DOI=10.1073/pnas.1731982100;
Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F.,
Madupu R., Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H.,
Nelson W.C., Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q.,
Khouri H.M., Fedorova N.B., Tran B., Russell D., Berry K.J.,
Utterback T.R., Van Aken S.E., Feldblyum T.V., D'Ascenzo M.,
Deng W.-L., Ramos A.R., Alfano J.R., Cartinhour S., Chatterjee A.K.,
Delaney T.P., Lazarowitz S.G., Martin G.B., Schneider D.J., Tang X.,
Bender C.L., White O., Fraser C.M., Collmer A.;
"The complete genome sequence of the Arabidopsis and tomato pathogen
Pseudomonas syringae pv. tomato DC3000.";
Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
-!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
3-phosphoglycerate. Essential for the growth and pathogenicity on
the host plant. {ECO:0000269|PubMed:7896694}.
-!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
{ECO:0000255|HAMAP-Rule:MF_01038, ECO:0000269|PubMed:7896694}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|HAMAP-Rule:MF_01038};
Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
Rule:MF_01038};
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
Rule:MF_01038}.
-!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01038}.
-!- DISRUPTION PHENOTYPE: Cannot use, as a sole carbon and/or energy
source, a wide variety of hexoses and intermediates of hexose
catabolism. {ECO:0000269|PubMed:7896694}.
-!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
family. {ECO:0000255|HAMAP-Rule:MF_01038}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U12776; AAA77677.1; -; Genomic_DNA.
EMBL; AE016853; AAO58753.1; -; Genomic_DNA.
PIR; A56142; A56142.
RefSeq; NP_795058.1; NC_004578.1.
RefSeq; WP_011105426.1; NC_004578.1.
ProteinModelPortal; P52832; -.
SMR; P52832; -.
STRING; 223283.PSPTO_5327; -.
PRIDE; P52832; -.
EnsemblBacteria; AAO58753; AAO58753; PSPTO_5327.
GeneID; 1187012; -.
KEGG; pst:PSPTO_5327; -.
PATRIC; fig|223283.9.peg.5454; -.
eggNOG; ENOG4105CJI; Bacteria.
eggNOG; COG0696; LUCA.
HOGENOM; HOG000223664; -.
KO; K15633; -.
OMA; FMDGRDT; -.
OrthoDB; POG091H01EL; -.
PhylomeDB; P52832; -.
BioCyc; PSYR223283:G1G0D-5397-MONOMER; -.
UniPathway; UPA00109; UER00186.
Proteomes; UP000002515; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro.
GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
CDD; cd16010; iPGM; 1.
Gene3D; 3.40.1450.10; -; 1.
Gene3D; 3.40.720.10; -; 2.
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; 2.
SUPFAM; SSF64158; SSF64158; 1.
TIGRFAMs; TIGR01307; pgm_bpd_ind; 1.
1: Evidence at protein level;
Complete proteome; Glycolysis; Isomerase; Manganese; Metal-binding;
Reference proteome.
CHAIN 1 510 2,3-bisphosphoglycerate-independent
phosphoglycerate mutase.
/FTId=PRO_0000212193.
REGION 155 156 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01038}.
REGION 259 262 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01038}.
ACT_SITE 64 64 Phosphoserine intermediate.
{ECO:0000255|HAMAP-Rule:MF_01038}.
METAL 14 14 Manganese 2. {ECO:0000255|HAMAP-
Rule:MF_01038}.
METAL 64 64 Manganese 2. {ECO:0000255|HAMAP-
Rule:MF_01038}.
METAL 399 399 Manganese 1. {ECO:0000255|HAMAP-
Rule:MF_01038}.
METAL 403 403 Manganese 1. {ECO:0000255|HAMAP-
Rule:MF_01038}.
METAL 440 440 Manganese 2. {ECO:0000255|HAMAP-
Rule:MF_01038}.
METAL 441 441 Manganese 2. {ECO:0000255|HAMAP-
Rule:MF_01038}.
METAL 459 459 Manganese 1. {ECO:0000255|HAMAP-
Rule:MF_01038}.
BINDING 125 125 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01038}.
BINDING 187 187 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01038}.
BINDING 193 193 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01038}.
BINDING 332 332 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01038}.
SEQUENCE 510 AA; 55603 MW; D8FD7BCCF3C0F038 CRC64;
MTATPKPLVL IILDGFGHSE SHEGNAILAA KMPVMDRLYK TMPNGLISGS GMDVGLPDGQ
MGNSEVGHMN LGAGRVVYQD FTRVTKAIRD GEFFENPTIC AAVDKAVSAG KAVHIMGLLS
DGGVHSHQDH LVAMAELAVR RGADKIYLHA FLDGRDTPPR SAKKSLELMD ETFARLGKGR
IATIIGRYFA MDRDNRWDRV STAYNLIVDS SAEFHAATGV AGLEAAYARD ENDEFVKATR
IGEPANVEDG DAVVFMNFRA DRARELTRVF VEDDFKDFER ARQPKVNYVM LTQYAASIPA
PSAFAAGSLK NVLGEYLADN GKTQLRIAET EKYAHVTFFF SGGREEPFPG EERILIPSPK
VATYDLQPEM SAPEVTDKIV DAIEHQRYDV IIVNYANGDM VGHSGIMEAA IKAVEYLDVC
VGRITDALEK VGGEALITAD HGNVEQMTDD ATGQAHTAHT SEPVPFVYVG KRQLKVREGG
VLADVAPTML QLLGMEKPQE MTGHSILVEE


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