ID A0A0T5ZS50_9BACT Unreviewed; 407 AA.
AC A0A0T5ZS50;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Probable 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=bcpC {ECO:0000313|EMBL:KRT65636.1};
GN Synonyms=apgM {ECO:0000256|HAMAP-Rule:MF_01402};
GN ORFNames=XU11_C0022G0013 {ECO:0000313|EMBL:KRT65636.1};
OS Candidatus Dadabacteria bacterium CSP1-2.
OC Bacteria; Thermodesulfobacteriota; Candidatus Dadabacteria.
OX NCBI_TaxID=1640508 {ECO:0000313|EMBL:KRT65636.1, ECO:0000313|Proteomes:UP000051780};
RN [1] {ECO:0000313|EMBL:KRT65636.1, ECO:0000313|Proteomes:UP000051780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-2 {ECO:0000313|EMBL:KRT65636.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) 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|HAMAP-
CC 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}.
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:KRT65636.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDXN01000022; KRT65636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZS50; -.
DR STRING; 1640508.XU11_C0022G0013; -.
DR PATRIC; fig|1640508.3.peg.1373; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000051780; Unassembled WGS sequence.
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_B; ApgM_B; 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 15..397
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT REGION 174..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 44960 MW; 25CA57B25918CF78 CRC64;
MQEIIRDLLI PNDSKIVLCV LDGLGGLPLD GKTELEAAST PNLDELARRG ACGLHIPVAR
GITPGSGPSH LALFGYDPLK YEIGRGVLEA LGLGIELSPS EVAIRGNFAT AKYEGRKPIV
VDRRGGRIPT EENKRIAERI RERIQSIDGV RVSITSGMEH RFVLVLTFPE PLPPGADDIT
DTDPQKEGKA PLKPTPRRKE AQMVAHIAER FIELAAGVIK DEKVANYLLL RGFSLYPNLP
QFSQAYGLKA ATTAAYPMYR GVAKLVGMEV LEVEDTSIKS EIETLRRHFK EFDFFYFHVK
KTDSYGEDGN FWGKVKVIEE FDSFVPEILK LNPDVLVVTG DHSTPAVLKS HSWHPVPFLL
YSSYTRGGGS LGFSEKECLK GELGIFKATD AMTLMLSHAR RLQKFGA
//
