GPMI_SHIDS
ID GPMI_SHIDS Reviewed; 514 AA.
AC Q329P2;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01038};
DE Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01038};
DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01038};
DE Short=iPGM {ECO:0000255|HAMAP-Rule:MF_01038};
DE EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01038};
GN Name=gpmI {ECO:0000255|HAMAP-Rule:MF_01038}; OrderedLocusNames=SDY_4045;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01038}.
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:0000255|HAMAP-Rule:MF_01038};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01038};
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; CP000034; ABB63963.1; -; Genomic_DNA.
DR RefSeq; WP_005016722.1; NC_007606.1.
DR RefSeq; YP_405454.1; NC_007606.1.
DR AlphaFoldDB; Q329P2; -.
DR SMR; Q329P2; -.
DR STRING; 300267.SDY_4045; -.
DR EnsemblBacteria; ABB63963; ABB63963; SDY_4045.
DR KEGG; sdy:SDY_4045; -.
DR PATRIC; fig|300267.13.peg.4761; -.
DR HOGENOM; CLU_026099_2_0_6; -.
DR OMA; FMDGRDT; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000002716; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Glycolysis; Isomerase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..514
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_0000212203"
FT ACT_SITE 64
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 14
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 155..156
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 263..266
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 463
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
SQ SEQUENCE 514 AA; 56155 MW; D95B22B591F67A43 CRC64;
MSVSKKPMVL VILDGYGYRE EQQDNAIFSA KTPVMDALWA NRPHTLIDAS GLEVGLPDRQ
MGNSEVGHVN LGAGRIVYQD LTRLDVEIKD RVFFANPVLT GAVDKAKSAG KAVHIMGLLS
AGGVHSHEDH IMAMVELAAE RGAEKIYLHA FLDGRDTPPR SAESSLKKFE EKFAALGKGR
VASIIGRYYA MDRDNRWDRV EKAYDLLTLA QGEFQADTAV AGLQAAYARD ENDEFVKATV
IRAEGQPDAA MEDGDALIFM NFRADRAREI TRAFVNADFD GFARKKVVNV DFVMLTEYAA
DIKTAVAYPP ASLVNTFGEW MAKNDKTQLR ISETEKYAHV TFFFNGGVEE SFKGEDRILI
NSPKVATYDL QPEMSSAELT EKLVAAIKSG KYDTIICNYP NGDMVGHTGV MEAAVKAVEA
LDHCVDEVAK AVESVGGQLL ITADHGNAEQ MRDPATGQAH TAHTNLPVPL IYVGDKNVKA
VEGGKLSDIA PTMLSLMGME IPQEMTGKPL FIVE
