ID A0A1G1P4J9_9BACT Unreviewed; 400 AA.
AC A0A1G1P4J9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Cofactor-independent phosphoglycerate mutase {ECO:0000313|EMBL:OGX36825.1};
GN ORFNames=A3C36_02335 {ECO:0000313|EMBL:OGX36825.1};
OS Omnitrophica WOR_2 bacterium RIFCSPHIGHO2_02_FULL_52_10.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801858 {ECO:0000313|EMBL:OGX36825.1, ECO:0000313|Proteomes:UP000177305};
RN [1] {ECO:0000313|EMBL:OGX36825.1, ECO:0000313|Proteomes:UP000177305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGX36825.1}.
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DR EMBL; MHGR01000048; OGX36825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1P4J9; -.
DR Proteomes; UP000177305; 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..377
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 400 AA; 43710 MW; E4BBB24B461D892F CRC64;
MKYIVIVPDG MADNPVEELG NRTPLEAAVT TNMDYLARSG TTGLVKTIPD QMSPGSDIGN
MAILGYDPRT CHTGRAPLEA ANLNIVLADN EVAFRCNLVT VTNDEMADYS AGHIRTNEAS
LLIDALNGDI GLKGAKFYAG KGYRHVLVLA VEDPKAYCAI KTTPPHDILG KNITPYLPKG
PEAGILLKLM DMSKEVFEHS AVNQVRIDLG ENPANMIWLW GQGTRPNLPL FHKKFGLKGS
IISAVDLVNG IGRLAGLDVI NVPGATGYYD TNYLGKAEYA LESLKTKDFV YIHIEATDEA
GHNGDIKAKV NAIEQIDKHI VGTILNHYNE HDNVRILVLP DHPTPVKLRT HTADPVCFVM
YGKGIPHDGS QEFNENTARE KGLKFDSGEA LLNHFITKYL
//
