APGM_SULIL
ID APGM_SULIL Reviewed; 414 AA.
AC C3MQZ8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=LS215_1815;
OS Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=429572;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L.S.2.15 / Lassen #1;
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; CP001399; ACP35811.1; -; Genomic_DNA.
DR RefSeq; WP_012713908.1; NC_012589.1.
DR AlphaFoldDB; C3MQZ8; -.
DR SMR; C3MQZ8; -.
DR EnsemblBacteria; ACP35811; ACP35811; LS215_1815.
DR GeneID; 7807491; -.
DR GeneID; 8761778; -.
DR KEGG; sis:LS215_1815; -.
DR HOGENOM; CLU_034906_2_0_2; -.
DR OMA; IAFRCNF; -.
DR OrthoDB; 17268at2157; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001747; 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_1000215193"
SQ SEQUENCE 414 AA; 45239 MW; E2E3C9D93C441BCA CRC64;
MKQYKILLII ADGLGDRPVS KLNGLTPLEA ANKPAISDLL KNSMIGLMDP ISPGVIPGSD
TSHLSIFGLD PHVYYRGRGA FEALGAGATL KHGDVAFRGN FATVNNDLVV VDRRAGRKLE
EGEELVKELN EKIKEINDVK IRFYKGTEHR VAVVLSGKGI SDKVSDTDPH YEGLKVLESK
PLEDSTEALR TAEIINILTR KVFDVLNSSE VNKRRIEQGE KPANIVLLRG AAHYIKLPSF
SSYTKLKAAA VSATALIKGI CRELGMNVVT PVGATGGIDT DYNAKAKAAI ELLKENDFVF
LHIKATDAAS HDGLVEEKVK AIERIDKVIG TIVDNVGRDN LILMFTGDHA TPVEVKEHSG
DPVPILLYVP YPIINDNVRD FNEKEARKGS LRIRGLDVTN ILLNYSNRAE KYGA
