APGM_SULIA
ID APGM_SULIA Reviewed; 414 AA.
AC C3MZ46;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=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=M1627_1803;
OS Sulfolobus islandicus (strain M.16.27).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=427318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.16.27;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(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; CP001401; ACP55678.1; -; Genomic_DNA.
DR RefSeq; WP_012711667.1; NC_012632.1.
DR AlphaFoldDB; C3MZ46; -.
DR SMR; C3MZ46; -.
DR EnsemblBacteria; ACP55678; ACP55678; M1627_1803.
DR GeneID; 7812467; -.
DR GeneID; 7940365; -.
DR KEGG; sim:M1627_1803; -.
DR HOGENOM; CLU_034906_2_0_2; -.
DR OMA; IAFRCNF; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000002307; 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_A; ApgM_A; 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..414
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_1000215191"
SQ SEQUENCE 414 AA; 45169 MW; 28CADD16D5089CD0 CRC64;
MKQYKILLII ADGLGDRPVS KLNGLTPLEA ANKPAISDLL KSSMIGLMDP ISPGVIPGSD
TSHLSIFGLD PHVYYRGRGA FEALGAGATL KHGDVAFRGN FATVNNDLVV VDRRAGRKLE
EGEELVKELN EKIKEINDVK IRFYKGTEHR VAVVLSGKGI SDKVSDTDPH YEGLKVLESK
PLEDSTEALR TAEIINILTR KVFDVLNSSE VNKRRIEQGE KPANIVLLRG AAHYVKLPSF
SSYTKLKAAA VSATALIKGI CRELGMNVVT PVGATGGIDT NYNAKAKAAI ELLKENDFVF
LHIKATDAAS HDGLVEEKVK AIERIDKVIG TIVDNVGRDN LILMFTGDHA TPVEVKEHSG
DPVPILLYVP YPIINDNVKD FNEKEARKGS LRIRGLDVTN ILLNYSNRAE KYGA
