ID A0A0S7WI85_9CHLR Unreviewed; 400 AA.
AC A0A0S7WI85;
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:KPJ49870.1};
GN ORFNames=AMJ38_02670 {ECO:0000313|EMBL:KPJ49870.1};
OS Dehalococcoidia bacterium DG_22.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703393 {ECO:0000313|EMBL:KPJ49870.1, ECO:0000313|Proteomes:UP000054105};
RN [1] {ECO:0000313|EMBL:KPJ49870.1, ECO:0000313|Proteomes:UP000054105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_22 {ECO:0000313|EMBL:KPJ49870.1};
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:KPJ49870.1}.
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; LIZQ01000049; KPJ49870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7WI85; -.
DR PATRIC; fig|1703393.3.peg.439; -.
DR Proteomes; UP000054105; 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; 2.
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 16..389
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 400 AA; 43750 MW; BA06251AE2DE4747 CRC64;
MDFDLIREVA IPAETKIVLL VMDGLGGLPE PRTGRTEMET ARIANLDRLA QEGICGMVYH
VGIGITPGSG PGHLALFGYD PLRYRIGRGA LEAVGIDFDL GPQDVAARGN FCTVDDGGLV
VDRRAGRIDT DTCARLCSEL RTIELPGAEL FVEPVREHRF LLVLRGDDLS DTLSETDPQQ
VGVPPVEVAA RAPEAQVTAG LVSAFVAGAR DRLRQHHPAN MVLLRGFARW PDLPSFPEVF
GLRAAAIAFY PMYRGLAKLV GMTALATGPS LSDSLAALRE HWEQFDFFFV HYKATDSTGE
DGNFQAKVAK LEEVDAIIPE LLNLKPDVIM VTGDHSTPST YRAHSWHPVP FALRSRWCQP
DRAEAFNERD CQRGSLGLFA ATEIMPLAMA HADRFTKYGA
//
