ID A0A0Q0VKK3_9BACT Unreviewed; 402 AA.
AC A0A0Q0VKK3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:KQC08109.1};
GN ORFNames=APR54_05030 {ECO:0000313|EMBL:KQC08109.1};
OS Candidatus Cloacimonas sp. SDB.
OC Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX NCBI_TaxID=1732214 {ECO:0000313|EMBL:KQC08109.1, ECO:0000313|Proteomes:UP000052007};
RN [1] {ECO:0000313|EMBL:KQC08109.1, ECO:0000313|Proteomes:UP000052007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDB {ECO:0000313|EMBL:KQC08109.1};
RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA Suflita J.M., Callaghan A.V.;
RT "Methanogenic Paraffin-Utilizing Consortium.";
RL Submitted (OCT-2015) 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:KQC08109.1}.
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DR EMBL; LKUH01000282; KQC08109.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q0VKK3; -.
DR Proteomes; UP000052007; 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; 2.
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..391
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 402 AA; 44090 MW; F8A14D0897A07D7E CRC64;
MKYIIILGDG MADRKIASLG NKTPLMVADI PAIDNICRLG RTGLYQSVPL DMPPGSEVAN
LAVLGYDVRK VYEGRGVLEA ASLGIPLDQN DLTMRCNLIC IENGKIKNHS AGHISTQESA
VLIDYLNEHL ADDLIRFYTG FSFRHVLVVK GGNNDLKFTP PHDVPGTPFR DVMIIPSSPK
GEKTAQVLNK LILKSQELLQ DHPVNLQRIK AGKDPANSVW FWSSGYKPRM NTLPENFGIS
GAVISAVDII KGLGILAGMD VIEVEGATGL SDTNYEGKAE AAVEALKNHD LVYVHVEATD
EAGHAGDIEL KIKSLEYLDS RLVKLIFNQV KKLDDEITIA ILPDHSTPCE VRSHTHDPVP
FIIYDPQKAA DSVQKYDEVS CKKGSFGLVK EDEFIRILLG KL
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