ID A0A2N0UTK1_9FIRM Unreviewed; 403 AA. AC A0A2N0UTK1; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 11-DEC-2019, entry version 7. 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; Clostridiales; Ruminococcaceae; 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 -!- 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NNBY01000031; PKD30334.1; -; Genomic_DNA. 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 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 4: Predicted; 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 //