ID V4LVF6_9CREN Unreviewed; 419 AA.
AC V4LVF6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archaeal form {ECO:0000313|EMBL:ESQ22986.1};
GN ORFNames=MGAcid_08050 {ECO:0000313|EMBL:ESQ22986.1};
OS uncultured Acidilobus sp. MG.
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC Acidilobus; environmental samples.
OX NCBI_TaxID=1410573 {ECO:0000313|EMBL:ESQ22986.1, ECO:0000313|Proteomes:UP000017902};
RN [1] {ECO:0000313|EMBL:ESQ22986.1, ECO:0000313|Proteomes:UP000017902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jay Z.J., Rusch D.B., Tringe S.G., Bailey C., Jennings R.M., Inskeep W.P.;
RT "Predominant Acidilobus-like populations from geothermal environments of
RT Yellowstone National Park exhibit similar metabolic potential in different
RT hypoxic microbial communities.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000256|ARBA:ARBA00002315}.
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 -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000256|ARBA:ARBA00005524}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESQ22986.1}.
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DR EMBL; AYMA01000002; ESQ22986.1; -; Genomic_DNA.
DR AlphaFoldDB; V4LVF6; -.
DR STRING; 1410573.MGAcid_08050; -.
DR PATRIC; fig|1410573.3.peg.762; -.
DR Proteomes; UP000017902; Unassembled WGS sequence.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd16011; iPGM_like; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.30.70.2130; Metalloenzyme domain; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
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}.
FT DOMAIN 1..399
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 419 AA; 45257 MW; 2AC4DDDD22FA52F9 CRC64;
MDGAADGSNP VKSSLATAFK PNIDLLATTA HCGLVYTVSQ GVAPESDEAV ISILGYDPEK
YYTGRGPLEA LGAGVDFKEG QVALRANFAT VDPKTYRILD RRAGRGVTKS EALELARAVD
GMKLDNGLGE AKFIPTVGHR GVLVLSHRDV KLSANITNTD PAYERVGLIS KARASFEPYV
QLSKPLDERD PGAVKAAQLL NEFTRKAIDL LSSHPVNQQR TSKGLLPANA ILARDAGDRL
PAAPPITSLF GLRFASVTEM PVERGIAKAL GLTDLHYEVE GKTKEQILVE EADLVADNLD
KFDAFYVHLK GPDEPGHDGN FEAKVAAIEL IDRHFFSRLL SRVSRDEALF IVTSDHATPW
TLKSHSDDPV PIMLSNPQLG KGPGKFDERS CSGGKLGLLR KGVEILPLAI KYLRELSSS
//
