APGM_THEM4
ID APGM_THEM4 Reviewed; 402 AA.
AC A6LMV5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01402};
DE Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01402};
DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01402};
DE Short=aPGAM {ECO:0000255|HAMAP-Rule:MF_01402};
DE EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01402};
GN Name=apgM {ECO:0000255|HAMAP-Rule:MF_01402}; OrderedLocusNames=Tmel_1409;
OS Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX NCBI_TaxID=391009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12029 / CIP 104789 / BI429;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermosipho melanesiensis BI429.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01402}.
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_01402};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01402}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01402}.
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DR EMBL; CP000716; ABR31256.1; -; Genomic_DNA.
DR RefSeq; WP_012057615.1; NC_009616.1.
DR AlphaFoldDB; A6LMV5; -.
DR SMR; A6LMV5; -.
DR STRING; 391009.Tmel_1409; -.
DR EnsemblBacteria; ABR31256; ABR31256; Tmel_1409.
DR KEGG; tme:Tmel_1409; -.
DR eggNOG; COG3635; Bacteria.
DR HOGENOM; CLU_034906_2_0_0; -.
DR OMA; IAFRCNF; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001110; Chromosome.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16011; iPGM_like; 1.
DR Gene3D; 3.30.70.2130; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR HAMAP; MF_01402_B; ApgM_B; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR023665; ApgAM_prokaryotes.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
DR PANTHER; PTHR31209; PTHR31209; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR Pfam; PF10143; PhosphMutase; 1.
DR PIRSF; PIRSF006392; IPGAM_arch; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR TIGRFAMs; TIGR00306; apgM; 1.
PE 3: Inferred from homology;
KW Glycolysis; Isomerase.
FT CHAIN 1..402
FT /note="Probable 2,3-bisphosphoglycerate-independent
FT phosphoglycerate mutase"
FT /id="PRO_1000068385"
SQ SEQUENCE 402 AA; 44645 MW; 9AA35C950778BD4B CRC64;
MIDRQQILNE LISPNSSKIV LLVMDGIGDI PGEDGLTPLQ KANTPKLDEL AKQSDLGQTI
PVLPGITPGS GPGHLGIFGY DPLKYQIGRG ILEALGIDVE VGEKDLVARG NFATLEGDII
VDRRAGRPSS EESAKVVEIL NENIHKIEDV EVKFYPGKEH RFVVKLTGEG LYDKLEDADP
QKEGKPIKYT KALDESSKKS EKIINILIDR IKEVLKDQQK MNFALLRGFS KYPNLPSFGD
VYKLRPAAIA VYPMYKGLAK LVGMEILKTG QTIEDEFKTV KENWEKYDFF YVHVKKTDSY
GEDGNFESKV KVIEEVDKNL GLLLELKPDV LIVTGDHSTP CAMKGHSFHP VPLMIYSKFT
RKGLSKLYNE FECARGTLGT IPAVDVMSLA LAYAGRLEKY GA
