ID   A0A101W378_9FIRM        Unreviewed;       375 AA.
AC   A0A101W378;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:KUO65817.1};
GN   ORFNames=APF84_00745 {ECO:0000313|EMBL:KUO65817.1};
OS   Gracilibacter sp. BRH_c7a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Gracilibacteraceae;
OC   Gracilibacter.
OX   NCBI_TaxID=1734398 {ECO:0000313|EMBL:KUO65817.1, ECO:0000313|Proteomes:UP000053404};
RN   [1] {ECO:0000313|EMBL:KUO65817.1, ECO:0000313|Proteomes:UP000053404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c7a {ECO:0000313|EMBL:KUO65817.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
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:KUO65817.1}.
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DR   EMBL; LOEZ01000019; KUO65817.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101W378; -.
DR   STRING; 1734398.APF84_00745; -.
DR   Proteomes; UP000053404; 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   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   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   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152}.
FT   DOMAIN          1..355
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
SQ   SEQUENCE   375 AA;  42023 MW;  860CC0ED7EEE018D CRC64;
     MKTMMIILDG LADEPIKDLE YKTSYDYANH ENLDRLAAQG IKGYFNACPQ GYLPESMNCI
     LNLLGIPQES FPKSRAALEL LAHGHALGED EVVLRCNLVA VEDKKLISFN GGGLTKQEMK
     KVSEQEAGRT SDIDFIHLSG YRNLLVMNKK DFNSFDCLTY PPHEFLGEDI ERLLGELCKS
     SEVLHDFVSS NEFKINGEDG KQYRYLFYPW GIAEKSKLPT FKQKYGKAGA AVCGAEIAKG
     IALALGLYVP KMEGLTADID TNLRLKAEGA CSLLEEYDFV FVHINGLDEA SHRYDVNEKI
     KFIEKIDREF IAYVDNNLNS QINILICADH ATSPLTGKHS ALDVPYIIRS QSLQNRTGIE
     SIPTGEILKY LLSFR
//