ID A0A1W9PE89_9BACT Unreviewed; 401 AA.
AC A0A1W9PE89;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:OQX56560.1};
GN ORFNames=B5M53_00850 {ECO:0000313|EMBL:OQX56560.1};
OS Candidatus Cloacimonas sp. 4484_209.
OC Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX NCBI_TaxID=1968525 {ECO:0000313|EMBL:OQX56560.1, ECO:0000313|Proteomes:UP000192614};
RN [1] {ECO:0000313|Proteomes:UP000192614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OQX56560.1}.
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DR EMBL; MZGI01000009; OQX56560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9PE89; -.
DR Proteomes; UP000192614; 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 InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
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..390
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 401 AA; 44685 MW; 41E86AD2CA32A11E CRC64;
MIPEEIYRDL SIKNEKKIVL LVMDGVGGLP INGMTPLEAA HTPNIDELTK KSCTGLTYPV
SLGITPGSGP AHLSLFGYDP LKYNIKRGVL EALGIDFDLQ REDIAIRGNF ATIDNDGLLK
DRRAGRITTD VNKELCDLLS SEIKVIDDVK IIIRSGKEHR FVIVLRGSGL SDSVTDTDPQ
KVGVQPKISR AIENTGSKTA SVINKLISRA KEVLKDKYPA NFILLRGISK HPDIPTMQDL
FKLTPAAIAT YPMYRGLAKL VGMEVLQTGT DISSEFDTLK QNWDKFDFFY LHIKKTDSYG
EDGNFEKKVS IIEEVDKYLP SLLAQKPDCL VITGDHSTPC RMKSHSWHPV PFLLYSAFNR
FDEAKRFTES ECRKGILGSF AAMEAMELML AHTLKLKKYG A
//
