ID A0A151BQT3_9ARCH Unreviewed; 276 AA.
AC A0A151BQT3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:KYH42275.1};
DE Flags: Fragment;
GN ORFNames=AYL33_003160 {ECO:0000313|EMBL:KYH42275.1};
OS Candidatus Bathyarchaeota archaeon B63.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1779372 {ECO:0000313|EMBL:KYH42275.1, ECO:0000313|Proteomes:UP000075614};
RN [1] {ECO:0000313|EMBL:KYH42275.1, ECO:0000313|Proteomes:UP000075614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B63 {ECO:0000313|EMBL:KYH42275.1};
RA He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., Wang F.;
RT "Evidence for homoacetogenesis among multiple lineages of the archaeal
RT phylum Bathyarchaeota widespread in marine sediments.";
RL Submitted (FEB-2016) 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:KYH42275.1}.
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DR EMBL; LUCF01000024; KYH42275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151BQT3; -.
DR Proteomes; UP000075614; 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 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 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 SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152}.
FT DOMAIN 5..269
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT NON_TER 276
FT /evidence="ECO:0000313|EMBL:KYH42275.1"
SQ SEQUENCE 276 AA; 30614 MW; D707A0032D18E2B5 CRC64;
MTLRLIYIVI DGLGDLPIDE LGGETPLGYA ETPNLDLLAS RGKLGLMYAV GEGIAPESDV
AVISILGYDP FKYHVGRGPI EAFGADLSME DGDLALRCNF ATLGSDRRII DRRVGRTLTT
EEAAELSEAI NREVHLESHP AEFEFKSTLG HRAVLVIRGK GLRLSAEITN TDPAYERFEG
MGVAKPNFRM FLQRSVPLVE TEEARRAAQL LNEFTQKSHE VLDGHEVNRR REAEGKLKAN
VILSRDAGDR VPRFFSINER YGVRFACLAD MPVERG
//
