ID B0S0D3_FINM2 Unreviewed; 411 AA.
AC B0S0D3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000313|EMBL:BAG07892.1};
GN OrderedLocusNames=FMG_0474 {ECO:0000313|EMBL:BAG07892.1};
OS Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS (Peptostreptococcus magnus).
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Finegoldia.
OX NCBI_TaxID=334413 {ECO:0000313|EMBL:BAG07892.1, ECO:0000313|Proteomes:UP000001319};
RN [1] {ECO:0000313|EMBL:BAG07892.1, ECO:0000313|Proteomes:UP000001319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29328 / DSM 20472 / WAL 2508
RC {ECO:0000313|Proteomes:UP000001319};
RX PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT pathogen.";
RL DNA Res. 15:39-47(2008).
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 ---------------------------------------------------------------------------
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; AP008971; BAG07892.1; -; Genomic_DNA.
DR RefSeq; WP_012290427.1; NC_010376.1.
DR AlphaFoldDB; B0S0D3; -.
DR STRING; 334413.FMG_0474; -.
DR KEGG; fma:FMG_0474; -.
DR eggNOG; COG3635; Bacteria.
DR HOGENOM; CLU_034906_2_0_9; -.
DR Proteomes; UP000001319; Chromosome.
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 HAMAP; MF_01402_A; ApgM_A; 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 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};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000001319}.
FT DOMAIN 4..398
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 411 AA; 44207 MW; 7EEDEA67B23913C0 CRC64;
MNRKVILAVA DGVGDRPCEI LGGKTPLEYA STPNLDKLAS VGTTGIMDVH GAGIPVGTDL
GHMILFGYGL EDYPGRGPIE AFGREIELQA GDVAFRSNFA TVNENLCVVD RRAGRIRENT
NLLAQSLNNI EIDGIKVIFK EATEHRAVLI LRGPGLSANI TDTDPKVAGV DVNYKKCQSK
DGKPDSIFTA EIVNKFLLKA NEILSKHSVN EERISKGLLP ANFILTRGAG IMPKLEKISE
KLNIKGACVA AEGTVLGVAR LAGFTALTAP TMTGNIDTDV NAKAQMAIDA LKDHDFVLVN
LKATDLFGHD GNPEKKAQAV EVFDKFIGLL LEANLENTII AVTADHSTPC ERMEHSGDPV
PVLIAGPGIR QDRVTKFDEI SCSYGGLCRI KGKDLSNTLY DFLEKTKKQG N
//
