ID A0A0S8EQ43_9BACT Unreviewed; 396 AA.
AC A0A0S8EQ43;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:KPK50130.1};
GN ORFNames=AMK72_02925 {ECO:0000313|EMBL:KPK50130.1};
OS Planctomycetes bacterium SM23_25.
OC Bacteria; Planctomycetota.
OX NCBI_TaxID=1704028 {ECO:0000313|EMBL:KPK50130.1, ECO:0000313|Proteomes:UP000052058};
RN [1] {ECO:0000313|EMBL:KPK50130.1, ECO:0000313|Proteomes:UP000052058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_25 {ECO:0000313|EMBL:KPK50130.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK50130.1}.
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DR EMBL; LJTY01000034; KPK50130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8EQ43; -.
DR Proteomes; UP000052058; Unassembled WGS sequence.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
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; IPR023665; ApgAM_prokaryotes.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
DR NCBIfam; TIGR00306; apgM; 1.
DR NCBIfam; TIGR02535; hyp_Hser_kinase; 1.
DR PANTHER; PTHR31209:SF4; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31209; COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 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};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235}.
FT DOMAIN 1..373
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 396 AA; 43050 MW; 8F53C5F96B32E908 CRC64;
MKYAIVIPDG AADRPVDSLG GRTPFEVARL PNMDYIATEG RLGTVKTISA GVAPGSDVAV
LSLLGYDPVR TYTGRGPLEA AARGIQARPD DWIFRCNLVT VADGKMVDYS AGHITTQEAE
VLIRSLEDQF GSDTLRFYPG IGYRHLLVIR GESFKVRTTP PHDIMGLPIR KHLPKGTNAA
RLRQLMDASG EVLADHPVNQ VRGDLGENPA SQIWLWGEGQ KPALTPFRER WGLGGAAITA
VDLVRGIARL IGWDVIEVEG ATGYYDTNYA GKAHAAIDAL NDHDIVVVHV EATDEAGHNG
DAREKIRALE AVDREIVGPL LKALQAIDLP WRILVAPDHE TPLAVRTHES RPVPFAMMGD
GLESGGRERA MTEAAARKTG MHVAVGHELM EYFLTR
//
