ID Q04P95_LEPBJ Unreviewed; 546 AA.
AC Q04P95;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 106.
DE RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-independent) {ECO:0000256|ARBA:ARBA00012026};
DE EC=5.4.2.12 {ECO:0000256|ARBA:ARBA00012026};
GN Name=gpmI {ECO:0000313|EMBL:ABJ77275.1};
GN OrderedLocusNames=LBJ_2872 {ECO:0000313|EMBL:ABJ77275.1};
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=355277 {ECO:0000313|EMBL:ABJ77275.1, ECO:0000313|Proteomes:UP000000656};
RN [1] {ECO:0000313|EMBL:ABJ77275.1, ECO:0000313|Proteomes:UP000000656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB197 {ECO:0000313|EMBL:ABJ77275.1,
RC ECO:0000313|Proteomes:UP000000656};
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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:0000256|ARBA:ARBA00000370};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000256|ARBA:ARBA00008819}.
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DR EMBL; CP000350; ABJ77275.1; -; Genomic_DNA.
DR RefSeq; WP_011669266.1; NC_008510.1.
DR AlphaFoldDB; Q04P95; -.
DR KEGG; lbj:LBJ_2872; -.
DR PATRIC; fig|355276.3.peg.245; -.
DR HOGENOM; CLU_026099_3_1_12; -.
DR OMA; FMDGRDT; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000000656; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
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; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.40.1450.10; BPG-independent phosphoglycerate mutase, domain B; 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 NCBIfam; TIGR01307; pgm_bpd_ind; 1.
DR PANTHER; PTHR31637; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31637:SF0; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF06415; iPGM_N; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR PIRSF; PIRSF001492; IPGAM; 1.
DR SUPFAM; SSF64158; 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR001492-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001492-3}.
FT DOMAIN 13..534
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT DOMAIN 93..315
FT /note="BPG-independent PGAM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06415"
FT ACT_SITE 73
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-1"
FT BINDING 20
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 73
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 164..165
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 279..282
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 422
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 426
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 463
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 464
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 493
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
SQ SEQUENCE 546 AA; 61205 MW; 075B752C8B994B3F CRC64;
MKLSKKYTFR SRKVLLVILD GVGYSPKGPE FGNAIAGAKL PFLNQVWNQF PTLHIQAHGK
FVGMPSDEDM GNSEVGHNVL GSGRIFDQGA KLVSNSIASG DIFQGQAWKE VIDNTKKNKS
TLHLLGLFSD GNVHAHIDHT KALISRAISE KVTKIRLHIL LDGRDVPEKS ALDYLNPFET
WLDSFRKNGI DIRIASGGGR MTITMDRYEA DWSMVERGWT IHVKGEGRKF SSAKEAIETF
RAEDPKVIDQ YLPSFVIAEN GNPIGKIQDG DSVVFTNFRG DRAIEISLAF TEKNFDKFNR
GPLPDIVYAG IMQYDGDLKL PERFLVAPPA IDRTLGEYMA NSKIAQYALS ETQKYGHVTY
FWNGNKSGYF DQNSEEYREI QSDVIPFDQS PEMKAFLITE TLEKALNENK QDFYRVNYAN
GDMVGHTGNY PATVQAMEFL DGCLERLWKA CEKQNIVLLI TADHGNADEM YQLDKKGNVE
KNSQGNPIPK TSHTLNPVPF SILDPERKIQ LNSNFLNPSL ANIAATILDV MGYETPEGYH
SSLIQN
//