GPMI_BACSU
ID GPMI_BACSU Reviewed; 511 AA.
AC P39773; O32250;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000303|PubMed:8021172};
DE Short=BPG-independent PGAM {ECO:0000303|PubMed:8021172};
DE Short=Phosphoglyceromutase {ECO:0000303|PubMed:8021172};
DE Short=iPGM {ECO:0000303|PubMed:8021172};
DE EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01038};
DE AltName: Full=Vegetative protein 107;
DE Short=VEG107;
GN Name=gpmI {ECO:0000255|HAMAP-Rule:MF_01038}; Synonyms=pgm;
GN OrderedLocusNames=BSU33910;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-25, FUNCTION, AND
RP COFACTOR.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8021172; DOI=10.1128/jb.176.13.3903-3910.1994;
RA Leyva-Vazquez M.A., Setlow P.;
RT "Cloning and nucleotide sequences of the genes encoding triose phosphate
RT isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis.";
RL J. Bacteriol. 176:3903-3910(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-18.
RC STRAIN=168 / IS58;
RX PubMed=9298659; DOI=10.1002/elps.1150180820;
RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT "First steps from a two-dimensional protein index towards a response-
RT regulation map for Bacillus subtilis.";
RL Electrophoresis 18:1451-1463(1997).
RN [4]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9830105; DOI=10.1139/w98-060;
RA Chander M., Setlow B., Setlow P.;
RT "The enzymatic activity of phosphoglycerate mutase from gram-positive
RT endospore-forming bacteria requires Mn2+ and is pH sensitive.";
RL Can. J. Microbiol. 44:759-767(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-36 AND SER-62, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
CC -!- FUNCTION: Essential for rapid growth and for sporulation. Catalyzes the
CC interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
CC {ECO:0000269|PubMed:8021172, ECO:0000269|PubMed:9830105}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.12; Evidence={ECO:0000255|HAMAP-Rule:MF_01038};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:8021172, ECO:0000269|PubMed:9830105};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:8021172,
CC ECO:0000269|PubMed:9830105};
CC -!- ACTIVITY REGULATION: Inhibited during sporulation by acidification of
CC the forespore, thus allowing accumulation of the spore's large depot of
CC 3-phosphoglyceric acid. {ECO:0000269|PubMed:9830105}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Very sensitive to pH. A pH change from 8 to 6 results in greater than
CC 30- to 200-fold decreases in its activity. However, deactivation at
CC pH 6 is reversed by shifting the enzyme to pH 7 or 8.
CC {ECO:0000269|PubMed:9830105};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01038}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000255|HAMAP-Rule:MF_01038}.
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DR EMBL; L29475; AAA21680.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15396.1; -; Genomic_DNA.
DR PIR; D69675; D69675.
DR RefSeq; NP_391271.1; NC_000964.3.
DR RefSeq; WP_003228330.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P39773; -.
DR SMR; P39773; -.
DR IntAct; P39773; 1.
DR MINT; P39773; -.
DR STRING; 224308.BSU33910; -.
DR iPTMnet; P39773; -.
DR jPOST; P39773; -.
DR PaxDb; P39773; -.
DR PRIDE; P39773; -.
DR EnsemblBacteria; CAB15396; CAB15396; BSU_33910.
DR GeneID; 938574; -.
DR KEGG; bsu:BSU33910; -.
DR PATRIC; fig|224308.179.peg.3676; -.
DR eggNOG; COG0696; Bacteria.
DR InParanoid; P39773; -.
DR OMA; FMDGRDT; -.
DR PhylomeDB; P39773; -.
DR BioCyc; BSUB:BSU33910-MON; -.
DR SABIO-RK; P39773; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR GO; GO:0043937; P:regulation of sporulation; IDA:UniProtKB.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd16010; iPGM; 1.
DR Gene3D; 3.40.1450.10; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR HAMAP; MF_01038; GpmI; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR011258; BPG-indep_PGM_N.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR036646; PGAM_B_sf.
DR InterPro; IPR005995; Pgm_bpd_ind.
DR PANTHER; PTHR31637; PTHR31637; 1.
DR Pfam; PF06415; iPGM_N; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR PIRSF; PIRSF001492; IPGAM; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR SUPFAM; SSF64158; SSF64158; 1.
DR TIGRFAMs; TIGR01307; pgm_bpd_ind; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycolysis; Isomerase; Manganese; Metal-binding;
KW Phosphoprotein; Reference proteome; Sporulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8021172,
FT ECO:0000269|PubMed:9298659"
FT CHAIN 2..511
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_0000212128"
FT ACT_SITE 62
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 12
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 153..154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 261..264
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 403
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 407
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 444
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 445
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 462
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT MOD_RES 36
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT CONFLICT 233
FT /note="V -> C (in Ref. 1; AAA21680)"
FT /evidence="ECO:0000305"
FT CONFLICT 432..433
FT /note="IL -> MV (in Ref. 1; AAA21680)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="H -> D (in Ref. 1; AAA21680)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 56309 MW; B2823B683D634891 CRC64;
MSKKPAALII LDGFGLRNET VGNAVALAKK PNFDRYWNQY PHQTLTASGE AVGLPEGQMG
NSEVGHLNIG AGRIVYQSLT RVNVAIREGE FERNQTFLDA ISNAKENNKA LHLFGLLSDG
GVHSHINHLF ALLKLAKKEG LTKVYIHGFL DGRDVGPQTA KTYINQLNDQ IKEIGVGEIA
SISGRYYSMD RDKRWDRVEK AYRAMAYGEG PSYRSALDVV DDSYANGIYD EFVIPSVITK
ENGEPVAKIQ DGDSVIFYNF RPDRAIQISN TFTNKDFRDF DRGENYPKNL YFVCLTHFSE
TVDGYVAFKP INLDNTVGEV LSQHGLKQLR IAETEKYPHV TFFMSGGREA EFPGEERILI
NSPKVATYDL KPEMSAYEVK DALVKEIEAD KHDAIILNFA NPDMVGHSGM VEPTIKAIEA
VDECLGEVVD AILAKGGHAI ITADHGNADI LITESGEPHT AHTTNPVPVI VTKEGITLRE
GGILGDLAPT LLDLLGVEKP KEMTGTSLIQ K
