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APGM_SULIK
ID   APGM_SULIK              Reviewed;         414 AA.
AC   C4KIC4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=M164_1734;
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3;
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; CP001402; ACR42338.1; -; Genomic_DNA.
DR   RefSeq; WP_012711667.1; NC_012726.1.
DR   AlphaFoldDB; C4KIC4; -.
DR   SMR; C4KIC4; -.
DR   EnsemblBacteria; ACR42338; ACR42338; M164_1734.
DR   GeneID; 7812467; -.
DR   GeneID; 7940365; -.
DR   KEGG; sid:M164_1734; -.
DR   HOGENOM; CLU_034906_2_0_2; -.
DR   OMA; IAFRCNF; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001479; 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_1000215192"
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
 
 
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