GPMI_LEPIN
ID GPMI_LEPIN Reviewed; 548 AA.
AC P59173;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000250|UniProtKB:Q9X519};
DE Short=BPG-independent PGAM {ECO:0000250|UniProtKB:Q9X519};
DE Short=Phosphoglyceromutase {ECO:0000250|UniProtKB:Q9X519};
DE Short=iPGM {ECO:0000250|UniProtKB:Q9X519};
DE EC=5.4.2.12 {ECO:0000250|UniProtKB:Q9X519};
GN Name=gpmI; Synonyms=pmgI; OrderedLocusNames=LA_0439;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000250|UniProtKB:Q9X519}.
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:0000250|UniProtKB:Q9X519};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9X519};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:Q9X519};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000250|UniProtKB:Q9X519}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9X519}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000250|UniProtKB:Q9X519}.
CC -!- CAUTION: Seems to be more closely related to protozoan and plant gpmI
CC than to bacterial orthologs. {ECO:0000305}.
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DR EMBL; AE010300; AAN47638.2; -; Genomic_DNA.
DR RefSeq; NP_710620.2; NC_004342.2.
DR RefSeq; WP_001973414.1; NC_004342.2.
DR AlphaFoldDB; P59173; -.
DR SMR; P59173; -.
DR STRING; 189518.LA_0439; -.
DR EnsemblBacteria; AAN47638; AAN47638; LA_0439.
DR KEGG; lil:LA_0439; -.
DR PATRIC; fig|189518.3.peg.446; -.
DR HOGENOM; CLU_026099_3_1_12; -.
DR InParanoid; P59173; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
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-UniPathway.
DR CDD; cd16010; iPGM; 1.
DR Gene3D; 3.40.1450.10; -; 1.
DR Gene3D; 3.40.720.10; -; 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..548
FT /note="Probable 2,3-bisphosphoglycerate-independent
FT phosphoglycerate mutase"
FT /id="PRO_0000212160"
FT ACT_SITE 73
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 20
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 73
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 164..165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 279..282
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 422
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 426
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 463
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 464
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
FT BINDING 493
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9X519"
SQ SEQUENCE 548 AA; 61053 MW; FE0119878DDD046C CRC64;
MKLSKKYTFR SRKVLLIILD GVGYSPKGPE SGNAIAGAKL PFLNRVWNQF PTLHIQAHGK
AVGMPSDDDM GNSEVGHNVL GSGRIFDQGA KLVSNSIASG DIFNGQAWKE VIGNSKKNNS
TLHLLGLFSD GNVHSHIDHT KALISQAILE KVPKIRLHIL LDGRDVPEKS ALDYLNPFET
WLDSLRKSGT DIRIASGGGR MTITMDRYEA DWSMVERGWK VHVKGEGRYF SSAKEAIETF
RSENPKIIDQ YLPSFVISDN GKPVGKIQDG DSVVFTNFRG DRAIEISLAF TEKNFDKFDR
GPLPNVLYAG IMQYDGDLKL PERFLVAPPA IDRTLGEYMA SSNIPQYALS ETQKYGHVTY
FWNGNKSGYF DQNSEEYREI LSDVIPFDQS PEMKALLITE ALEKALNENK QDFYRVNYAN
GDMVGHTGNY LATVQAMEFL DGCVERLWKT CEKQNIVLLV TADHGNADEM FQLDKKGNVE
KDSHGNPIPK TSHTLNPVPI SILDPENKIR FNSKLSNPGL ANVAATILDV MGYETPEGYH
PSLIQNES
