ID A0A0S8FQF8_9BACT Unreviewed; 408 AA.
AC A0A0S8FQF8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Metalloenzyme domain-containing protein {ECO:0000259|Pfam:PF01676};
GN ORFNames=AMK73_06295 {ECO:0000313|EMBL:KPK62314.1};
OS Planctomycetes bacterium SM23_32.
OC Bacteria; Planctomycetota.
OX NCBI_TaxID=1704029 {ECO:0000313|EMBL:KPK62314.1, ECO:0000313|Proteomes:UP000052164};
RN [1] {ECO:0000313|EMBL:KPK62314.1, ECO:0000313|Proteomes:UP000052164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_32 {ECO:0000313|EMBL:KPK62314.1};
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:KPK62314.1}.
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DR EMBL; LJUE01000111; KPK62314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8FQF8; -.
DR PATRIC; fig|1704029.3.peg.1074; -.
DR Proteomes; UP000052164; 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 22..396
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT REGION 179..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 408 AA; 43827 MW; 14D26D7165F12E05 CRC64;
MNALQLAEQL VKRSEVAEGT RKIVLLVMDG VGDIRHPDNG FRTPLEVAQT PNLDRLAARS
ALGRIIPVDY GITPGSGPAH LGLFGYDPRE VEIGRGVLEV VGMDMPLKPG DVAARANFCT
VRDGVVTDRR AGRPATEVSA EKVKLLQRAV PRIDDVELVI RAGKGHRFGV VFRGPGLVGD
VSDTDPHEDG EPVRKAAPGS EGARKTAEVV NAFVRQAAEA LGGKEPINAV LTRGVSSRPD
IPGLAERFGL RCGAIATYPM YRGLASLVGM DLLETGQSVE EEFQCCLDNW EGYDFFFIHV
KPTDEAGEDG AHERKVAAIE AVDPHVPTLL EAGPEVLAVT GDHSTPCPMK LHSWHPVPLL
LHSPRCGADG RLRFTEADCN VGSLGIFRAM YLFPLMLANA GLLDKYGA
//
