ID A0A0S7X3X3_9BACT Unreviewed; 397 AA.
AC A0A0S7X3X3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Metalloenzyme domain-containing protein {ECO:0000259|Pfam:PF01676};
GN ORFNames=AMJ49_03455 {ECO:0000313|EMBL:KPJ56943.1};
OS Parcubacteria bacterium DG_74_2.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1703766 {ECO:0000313|EMBL:KPJ56943.1, ECO:0000313|Proteomes:UP000051668};
RN [1] {ECO:0000313|EMBL:KPJ56943.1, ECO:0000313|Proteomes:UP000051668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_74_2 {ECO:0000313|EMBL:KPJ56943.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ56943.1}.
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DR EMBL; LJNF01000007; KPJ56943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7X3X3; -.
DR Proteomes; UP000051668; 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 Gene3D; 3.30.70.2130; Metalloenzyme domain; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
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}.
FT DOMAIN 2..390
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 397 AA; 44704 MW; 4F1111742F7A7512 CRC64;
MKKILLIIID GLGDRLIPQL GKRTPLEAAK KPNLNFLAEN GICGLVKPFL FSKEKEPSSE
GTHLALFGYQ NYFLGRGPYE AAGIGIKMKK GDIILRANFG TVDENLRIID RRAGRIKKTQ
PLVNALKGIK INEVKILVRK SWGHRAILIL RGEDLSSKIS DGDPHKVRVK PKKILPLDKS
KKAKFTAEIL NQFLEKAHLI LKNHSFNKKR IKKGFLPGNY FLVRGAGKFK KIISFKKRYN
LKAAFIAGGA LYKGVAKILG MNKVSVKEAT GFANTNLKGK ISAAKRVIKK YDFLFLHIKA
TDIFAHDRDF QGKKKFIEKI DKELKPILKL KNVLITVTAD HSTCSLLKRH CKEPIPILIF
GNGKDKVKEF SEKACKKGKL GRIKQIDLMK KLLLYSK
//
