GPMI_BACAN
ID GPMI_BACAN Reviewed; 509 AA.
AC Q81X77; Q6HR13; Q6KKD2;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000303|PubMed:17085493};
DE Short=BPG-independent PGAM {ECO:0000303|PubMed:17085493};
DE Short=Phosphoglyceromutase {ECO:0000303|PubMed:17085493};
DE Short=iPGM {ECO:0000303|PubMed:17085493};
DE EC=5.4.2.12 {ECO:0000269|PubMed:17085493};
GN Name=gpmI {ECO:0000255|HAMAP-Rule:MF_01038}; Synonyms=gpmA;
GN OrderedLocusNames=BA_5365, GBAA_5365, BAS4986;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 2-509 IN COMPLEX WITH MANGANESE,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND ACTIVE SITE.
RX PubMed=17085493; DOI=10.1529/biophysj.106.093872;
RA Nukui M., Mello L.V., Littlejohn J.E., Setlow B., Setlow P., Kim K.,
RA Leighton T., Jedrzejas M.J.;
RT "Structure and molecular mechanism of Bacillus anthracis cofactor-
RT independent phosphoglycerate mutase: a crucial enzyme for spores and
RT growing cells of Bacillus species.";
RL Biophys. J. 92:977-988(2007).
CC -!- FUNCTION: Essential for rapid growth and for sporulation. Catalyzes the
CC interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
CC {ECO:0000269|PubMed:17085493}.
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:0000269|PubMed:17085493};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17085493};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:17085493};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01038}.
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; AE016879; AAP29025.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT34499.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT57275.1; -; Genomic_DNA.
DR RefSeq; NP_847539.1; NC_003997.3.
DR RefSeq; WP_001231153.1; NZ_WXXJ01000012.1.
DR RefSeq; YP_031225.1; NC_005945.1.
DR PDB; 2IFY; X-ray; 2.38 A; A=2-509.
DR PDBsum; 2IFY; -.
DR AlphaFoldDB; Q81X77; -.
DR SMR; Q81X77; -.
DR IntAct; Q81X77; 16.
DR STRING; 260799.BAS4986; -.
DR DNASU; 1084903; -.
DR EnsemblBacteria; AAP29025; AAP29025; BA_5365.
DR EnsemblBacteria; AAT34499; AAT34499; GBAA_5365.
DR GeneID; 45024968; -.
DR KEGG; ban:BA_5365; -.
DR KEGG; bar:GBAA_5365; -.
DR KEGG; bat:BAS4986; -.
DR PATRIC; fig|198094.11.peg.5324; -.
DR eggNOG; COG0696; Bacteria.
DR HOGENOM; CLU_026099_2_0_9; -.
DR OMA; FMDGRDT; -.
DR BRENDA; 5.4.2.12; 634.
DR UniPathway; UPA00109; UER00186.
DR EvolutionaryTrace; Q81X77; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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: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 3D-structure; Glycolysis; Isomerase; Manganese; Metal-binding;
KW Phosphoprotein; Reference proteome; Sporulation.
FT CHAIN 1..509
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_0000212119"
FT ACT_SITE 61
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000269|PubMed:17085493"
FT BINDING 11
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17085493"
FT BINDING 61
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17085493"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 152..153
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 260..263
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 402
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17085493"
FT BINDING 406
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17085493"
FT BINDING 443
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17085493"
FT BINDING 444
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17085493"
FT BINDING 461
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17085493"
FT MOD_RES 35
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:2IFY"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:2IFY"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 194..205
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:2IFY"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 265..272
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 316..322
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:2IFY"
FT TURN 340..345
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 354..359
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:2IFY"
FT TURN 371..374
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 375..387
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 400..405
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 410..433
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:2IFY"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:2IFY"
FT HELIX 486..494
FT /evidence="ECO:0007829|PDB:2IFY"
SQ SEQUENCE 509 AA; 56281 MW; 37C82D810978B430 CRC64;
MRKPTALIIL DGFGLREETY GNAVAQAKKP NFDGYWNKFP HTTLTACGEA VGLPEGQMGN
SEVGHLNIGA GRIVYQSLTR VNVAIREGEF DKNETFQSAI KSVKEKGTAL HLFGLLSDGG
VHSHMNHMFA LLRLAAKEGV EKVYIHAFLD GRDVGPKTAQ SYIDATNEVI KETGVGQFAT
ISGRYYSMDR DKRWDRVEKC YRAMVNGEGP TYKSAEECVE DSYANGIYDE FVLPSVIVNE
DNTPVATIND DDAVIFYNFR PDRAIQIARV FTNGDFREFD RGEKVPHIPE FVCMTHFSET
VDGYVAFKPM NLDNTLGEVV AQAGLKQLRI AETEKYPHVT FFFSGGREAE FPGEERILIN
SPKVATYDLK PEMSIYEVTD ALVNEIENDK HDVIILNFAN CDMVGHSGMM EPTIKAVEAT
DECLGKVVEA ILAKDGVALI TADHGNADEE LTSEGEPMTA HTTNPVPFIV TKNDVELRED
GILGDIAPTM LTLLGVEQPK EMTGKTIIK
