ID A0A1C8ZRB8_9CREN Unreviewed; 415 AA.
AC A0A1C8ZRB8;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01402};
DE Short=BPG-independent PGAM {ECO:0000256|HAMAP-Rule:MF_01402};
DE Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01402};
DE Short=aPGAM {ECO:0000256|HAMAP-Rule:MF_01402};
DE EC=5.4.2.12 {ECO:0000256|HAMAP-Rule:MF_01402};
GN Name=apgM {ECO:0000256|HAMAP-Rule:MF_01402};
GN ORFNames=BFU36_03725 {ECO:0000313|EMBL:AOL15978.1};
OS Sulfolobus sp. A20.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=1891280 {ECO:0000313|EMBL:AOL15978.1, ECO:0000313|Proteomes:UP000094286};
RN [1] {ECO:0000313|Proteomes:UP000094286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A20 {ECO:0000313|Proteomes:UP000094286};
RA Dai X.;
RT "Genome sequencing of Sulfolobus sp. A20 from Costa Rica and comparative
RT analyses of central carbon, nitrogen and sulfur metabolism in various
RT Sulfolobus strains.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000256|ARBA:ARBA00002315, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00000370,
CC ECO:0000256|HAMAP-Rule:MF_01402};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798,
CC ECO:0000256|HAMAP-Rule:MF_01402}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000256|ARBA:ARBA00005524,
CC ECO:0000256|HAMAP-Rule:MF_01402}.
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DR EMBL; CP017006; AOL15978.1; -; Genomic_DNA.
DR RefSeq; WP_069282333.1; NZ_CP017006.1.
DR AlphaFoldDB; A0A1C8ZRB8; -.
DR STRING; 1891280.BFU36_03725; -.
DR GeneID; 28694938; -.
DR KEGG; sula:BFU36_03725; -.
DR OrthoDB; 52918at2157; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000094286; 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; Alkaline Phosphatase, subunit A; 2.
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 NCBIfam; TIGR00306; apgM; 1.
DR PANTHER; PTHR31209; COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31209:SF0; METALLOENZYME DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR Pfam; PF10143; PhosphMutase; 1.
DR PIRSF; PIRSF006392; IPGAM_arch; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_01402};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01402}.
FT DOMAIN 6..405
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 415 AA; 45770 MW; 2B493F853438CC17 CRC64;
MKKEYKLVLV IADGLGDRPV NKLNGLTPLE AANKPNIKEL LKNSIVGLMD PISPGVIAGS
DTSHLSIFGL DPHKYYRGRG AFEALGAGAE LNDGDVAFRG NFATVNNDLI VTDRRAGRKI
EEGEELVKEL NEKIKEIDGI RIKFYKGTEH RVAVVLSGKE LSDKISDTDP HQEGLKLFQS
RPLDNDFKSL RTAEIVNKLT RKIYEVLNDS EINKKRIDRG EKPANIILLR GPSYYIKLPK
LESYTGLKAA AVSATALIKG ICKELGMNVV TPPGATGGID TDYNAKANAT IDLLKDYDFV
FLHIKATDAA SHDGLIEEKV KAIERIDSVI GKIVDKVGRD SLVLAFTGDH TTPVEFKEHT
GDPVPIMIYV PYPIVYDSVN DFNEKEVRKG SLRIRGLDVL NILLNYSNRA EKYGA
//
