ID   A0A2N0UTK1_9FIRM        Unreviewed;       403 AA.
AC   A0A2N0UTK1;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   SubName: Full=Cofactor-independent phosphoglycerate mutase {ECO:0000313|EMBL:PKD30334.1};
GN   ORFNames=RB5AMG_00739 {ECO:0000313|EMBL:PKD30334.1};
OS   Ruminococcus bromii.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=40518 {ECO:0000313|EMBL:PKD30334.1, ECO:0000313|Proteomes:UP000233562};
RN   [1] {ECO:0000313|EMBL:PKD30334.1, ECO:0000313|Proteomes:UP000233562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AMG {ECO:0000313|EMBL:PKD30334.1,
RC   ECO:0000313|Proteomes:UP000233562};
RX   PubMed=29159997;
RA   Mukhopadhya I., Morais S., Laverde-Gomez J., Sheridan P.O., Walker A.W.,
RA   Kelly W., Klieve A.V., Ouwerkerk D., Duncan S.H., Louis P., Koropatkin N.,
RA   Cockburn D., Kibler R., Cooper P.J., Sandoval C., Crost E., Juge N.,
RA   Bayer E.A., Flint H.J.;
RT   "Sporulation capability and amylosome conservation among diverse human
RT   colonic and rumen isolates of the keystone starch-degrader Ruminococcus
RT   bromii.";
RL   Environ. Microbiol. 0:0-0(2017).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000256|ARBA:ARBA00002315}.
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:PKD30334.1}.
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DR   EMBL; NNBY01000031; PKD30334.1; -; Genomic_DNA.
DR   EnsemblBacteria; PKD30334; PKD30334; RB5AMG_00739.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000233562; 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; 3.30.70.2130; -; 1.
DR   Gene3D; 3.40.720.10; -; 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   PANTHER; PTHR31209; PTHR31209; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   Pfam; PF10143; PhosphMutase; 1.
DR   PIRSF; PIRSF006392; IPGAM_arch; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
DR   TIGRFAMs; TIGR00306; apgM; 1.
DR   TIGRFAMs; TIGR02535; hyp_Hser_kinase; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235}.
FT   DOMAIN          1..380
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
SQ   SEQUENCE   403 AA;  44585 MW;  0415FC3A5975CB13 CRC64;
     MKYLVMLCDG MADEPNAQLD NSTPMAKAVK PCMDYLASKG EVGMVKTVAE GLKPGSDVAN
     LSVLGYEPAV YYSGRSPLEA ASIGIDLKDT DVTLRCNLVT LSDEENYEDK SMVDYCAGDI
     STEEARELIN YVEEKLGNDI FKFYSGVAYR HCLVWKNGNP HPGELTPPHD ISGRVIKEYI
     PKGDDTAALY DLMKKSYDLL KDHHVNKARV EKGLRPANSI WLWGEGTKPA LDSFFGKFGK
     KGSMISAVDL LKGIAICAGM KSVDVEGATG YIDTNFDGKC KAAIDEFKNG ADFVYIHVEA
     PDECGHRGEI ENKVKAIELI DEHILKPVTD FLRTFDDFAV LVCPDHPTPL SIRTHTSNPV
     PYLIYDSKNE VDSGVSKFCE EEAKKTGNYI EKGFTMMDYF LSK
//