APGM_AERPE
ID APGM_AERPE Reviewed; 424 AA.
AC Q9YBI2;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 25-MAY-2022, entry version 116.
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=APE_1616.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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; BA000002; BAA80616.2; -; Genomic_DNA.
DR PIR; C72541; C72541.
DR AlphaFoldDB; Q9YBI2; -.
DR SMR; Q9YBI2; -.
DR STRING; 272557.APE_1616.1; -.
DR DNASU; 1446131; -.
DR EnsemblBacteria; BAA80616; BAA80616; APE_1616.1.
DR KEGG; ape:APE_1616.1; -.
DR PATRIC; fig|272557.25.peg.1092; -.
DR eggNOG; arCOG01696; Archaea.
DR OMA; YVHLKGP; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000002518; 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; Reference proteome.
FT CHAIN 1..424
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_0000138130"
SQ SEQUENCE 424 AA; 46200 MW; DB5F2C71ED894A71 CRC64;
MKILYIVLDG AADSPTSPRK TLEEASKPNI DSLGSHAVCG MVYTVKPGVA PQSDYATLSL
LGYNPDEYYP GRGPLEAFGA GIEMRRGDIA LRANFATVDP GTLRIIDRRV GRSLTSREAR
ELASAVDGME LEDGEGTALF RATIGHRGVL VLRHRSKPLS DAISNTDPAY ERRGRFSVAL
EKYEPFIKLS NPLVEDEAAV LAARMLNEFT LKAVEILDSH PVNLAREKRG LLKANAILSR
DAGGLPEEKP PSFQERFGLR GASIVEMVVE RGISRYIGLD DIRVEIEGRA REEVYREEAA
RAVEALETHD LVYVHLKGPD EPGHDGSFEG KIRAVEDIDK HFFAPLLDRL SSAGLEPAFV
VTSDHATPWD VGAHSGDPVP LMISHQSIQG SIGKFSETVC LRGRLGTIIG GYRIIPKTLS
LLAG