APGM_THEAB
ID APGM_THEAB Reviewed; 402 AA.
AC B7IDT4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=THA_1725;
OS Thermosipho africanus (strain TCF52B).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX NCBI_TaxID=484019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCF52B;
RX PubMed=19124572; DOI=10.1128/jb.01448-08;
RA Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT the Firmicutes and Archaea.";
RL J. Bacteriol. 191:1974-1978(2009).
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; CP001185; ACJ76161.1; -; Genomic_DNA.
DR RefSeq; WP_012580374.1; NC_011653.1.
DR AlphaFoldDB; B7IDT4; -.
DR SMR; B7IDT4; -.
DR STRING; 484019.THA_1725; -.
DR PRIDE; B7IDT4; -.
DR EnsemblBacteria; ACJ76161; ACJ76161; THA_1725.
DR KEGG; taf:THA_1725; -.
DR eggNOG; COG3635; Bacteria.
DR HOGENOM; CLU_034906_2_0_0; -.
DR OMA; IAFRCNF; -.
DR OrthoDB; 1293048at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000002453; 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; 3.40.720.10; -; 2.
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 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; Reference proteome.
FT CHAIN 1..402
FT /note="Probable 2,3-bisphosphoglycerate-independent
FT phosphoglycerate mutase"
FT /id="PRO_1000145451"
SQ SEQUENCE 402 AA; 44498 MW; A1C9F344008E31C0 CRC64;
MIDRQKVISE LISPNTSKIV LLVMDGIGDI PNEEGLTPLQ KANTPNLDAL AKKSDLGQTI
PVLPGITPGS GPGHLGLFGY DPLKYQIGRG ILEALGINVE VGENDLVARG NFATIDGDII
VDRRAGRPSS EESAKVVEIL NENIKEIEDV KITFYPGKEH RFVVKFTGEG LMDKLEDADP
QKEGKPIKYT KALDESSKKS ERIVNILLDK IKEVLKDQPK MNFALLRGFS KHPDMPKFGD
VFKLKPAAVA VYPMYKGLAK LVGMEVVEAG QTIEDEFNTV KKLWNEYDFF YVHIKKTDSY
GEDGNFDSKV KVIEEVDKFL PILLELNPDV LIVTGDHSTP CVMKGHSFHP VPLMIYAKNT
RRGLSKLFNE FECARGSLGT IHAVDVMPLA LAYAGRLEKY GA
