ID A0A1F5FPJ5_9BACT Unreviewed; 501 AA.
AC A0A1F5FPJ5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01038};
DE Short=BPG-independent PGAM {ECO:0000256|HAMAP-Rule:MF_01038};
DE Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01038};
DE Short=iPGM {ECO:0000256|HAMAP-Rule:MF_01038};
DE EC=5.4.2.12 {ECO:0000256|HAMAP-Rule:MF_01038};
GN Name=gpmI {ECO:0000256|HAMAP-Rule:MF_01038};
GN ORFNames=A2572_04290 {ECO:0000313|EMBL:OGD81575.1};
OS Candidatus Collierbacteria bacterium RIFOXYD1_FULL_40_9.
OC Bacteria; Candidatus Collierbacteria.
OX NCBI_TaxID=1817731 {ECO:0000313|EMBL:OGD81575.1, ECO:0000313|Proteomes:UP000179237};
RN [1] {ECO:0000313|EMBL:OGD81575.1, ECO:0000313|Proteomes:UP000179237}
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|HAMAP-Rule:MF_01038}.
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 ECO:0000256|HAMAP-Rule:MF_01038};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01038};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01038};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798,
CC ECO:0000256|HAMAP-Rule:MF_01038}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01038}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000256|ARBA:ARBA00008819, ECO:0000256|HAMAP-
CC Rule:MF_01038}.
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:OGD81575.1}.
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DR EMBL; MFAQ01000041; OGD81575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5FPJ5; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000179237; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd16010; iPGM; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.40.1450.10; BPG-independent phosphoglycerate mutase, domain B; 1.
DR HAMAP; MF_01038; GpmI; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR011258; BPG-indep_PGM_N.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR036646; PGAM_B_sf.
DR InterPro; IPR005995; Pgm_bpd_ind.
DR NCBIfam; TIGR01307; pgm_bpd_ind; 1.
DR PANTHER; PTHR31637; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31637:SF0; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF06415; iPGM_N; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR PIRSF; PIRSF001492; IPGAM; 1.
DR SUPFAM; SSF64158; 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_01038};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01038};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01038};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01038}.
FT DOMAIN 4..490
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT DOMAIN 82..287
FT /note="BPG-independent PGAM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06415"
FT ACT_SITE 62
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-1"
FT BINDING 12
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 153..154
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 259..262
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 391
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 395
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 432
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 433
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 451
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT ECO:0000256|PIRSR:PIRSR001492-3"
SQ SEQUENCE 501 AA; 55458 MW; 8B88F430C09FA1D1 CRC64;
MSNKKCILCI LDGWGIAPDS AGNAITKANP QVYKFLLENF PNTTLKASGP AVGLPEEMDG
NSETGHLNLG AGRTVYQDLS LINMSIADGS FFTNQTLLGT ARHIKSFDSD LHLLGLIGAS
GVHASNDHLF ALMLFAKKQG INNVYLHLIT DGRDSPPDDA INQIKKVEEK INEIGIGQIA
SIMGRYYAMD RDLRLDRTQA AYNCLLQGDE NTGLSSEDFI TSQYAKSIFD EFIKPTAITS
NFKNTRVKAS DAVCFFNFRT DRPRQLTQMF LEHPLPNQKF VTMTPYKKEF GNPTIFGSTT
VTKTLGQIIS EKNYKQLRMA ETEKIAMVSY FFNGQSEEVF VGEERQYIDS PKVTTYDLIP
AMSTEELVKK FSENFKTTDY IFGLLNIACP DMVAHTGKIE KTIEAIKAAD LALSELINLA
KETNSYLVIT ADHGNAEELI NHDTGNIDTE HSASPVPLII YHPADNQFKL NPGKLGDVAP
TILKLLNIEK PVEMTGNNLI S
//