ID A0A855KWQ2_9BACI Unreviewed; 509 AA. AC A0A855KWQ2; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 19-JAN-2022, entry version 2. DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01038}; DE Short=BPG-independent PGAM {ECO:0000256|HAMAP-Rule:MF_01038}; DE Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01038}; DE Short=iPGM {ECO:0000256|HAMAP-Rule:MF_01038}; DE EC=5.4.2.12 {ECO:0000256|HAMAP-Rule:MF_01038}; GN Name=gpmI {ECO:0000256|HAMAP-Rule:MF_01038}; GN ORFNames=C1640_24190 {ECO:0000313|EMBL:PNS30050.1}; OS Bacillus sp. AKBS9. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=2072506 {ECO:0000313|EMBL:PNS30050.1, ECO:0000313|Proteomes:UP000236481}; RN [1] {ECO:0000313|EMBL:PNS30050.1, ECO:0000313|Proteomes:UP000236481} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AKBS9 {ECO:0000313|EMBL:PNS30050.1, RC ECO:0000313|Proteomes:UP000236481}; RA Kapley A., Jadeja N.B.; RT "Genome-wide analysis of Bacillus sp. AKBS9 for biosurfactant production RT and bioremediation."; RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Essential for rapid growth and for sporulation. Catalyzes the CC interconversion of 2-phosphoglycerate and 3-phosphoglycerate. CC {ECO:0000256|HAMAP-Rule:MF_01038}. 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 ECO:0000256|HAMAP-Rule:MF_01038}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01038}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01038}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798, CC ECO:0000256|HAMAP-Rule:MF_01038}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01038}. CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase CC family. {ECO:0000256|ARBA:ARBA00008819, ECO:0000256|HAMAP- CC Rule:MF_01038}. 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:PNS30050.1}. 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; POYG01000037; PNS30050.1; -; Genomic_DNA. DR RefSeq; WP_073540503.1; NZ_POYG01000037.1. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000236481; Unassembled WGS sequence. DR CDD; cd16010; iPGM; 1. DR Gene3D; 3.40.1450.10; -; 1. DR Gene3D; 3.40.720.10; -; 1. DR HAMAP; MF_01038; GpmI; 1. DR InterPro; IPR017850; Alkaline_phosphatase_core_sf. DR InterPro; IPR011258; BPG-indep_PGM_N. DR InterPro; IPR006124; Metalloenzyme. DR InterPro; IPR036646; PGAM_B_sf. DR InterPro; IPR005995; Pgm_bpd_ind. DR PANTHER; PTHR31637; PTHR31637; 1. DR Pfam; PF06415; iPGM_N; 1. DR Pfam; PF01676; Metalloenzyme; 1. DR PIRSF; PIRSF001492; IPGAM; 1. DR SUPFAM; SSF53649; SSF53649; 1. DR SUPFAM; SSF64158; SSF64158; 1. DR TIGRFAMs; TIGR01307; pgm_bpd_ind; 1. PE 3: Inferred from homology; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_01038}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01038}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01038}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01038}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01038}; KW Sporulation {ECO:0000256|HAMAP-Rule:MF_01038}. FT DOMAIN 3..497 FT /note="Metalloenzyme" FT /evidence="ECO:0000259|Pfam:PF01676" FT DOMAIN 81..298 FT /note="iPGM_N" FT /evidence="ECO:0000259|Pfam:PF06415" FT REGION 152..153 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" FT REGION 260..263 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" FT ACT_SITE 61 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" FT METAL 11 FT /note="Manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" FT METAL 61 FT /note="Manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" FT METAL 402 FT /note="Manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" FT METAL 406 FT /note="Manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" FT METAL 443 FT /note="Manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" FT METAL 444 FT /note="Manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" FT METAL 461 FT /note="Manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" FT BINDING 122 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" FT BINDING 184 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" FT BINDING 190 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" FT BINDING 335 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" FT MOD_RES 35 FT /note="Phosphotyrosine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01038" SQ SEQUENCE 509 AA; 56268 MW; 2BF34A4DA83C372B CRC64; MRKPTALIIL DGFGLREETY GNAVAQAKKP NFDGYWNKFP HTTLTACGEA VGLPEGQMGN SEVGHLNIGA GRIVYQSLTR VNVAIREGEF DKNETFQSAI KSVKEKGTAL HLFGLLSDGG VHSHMNHMFA LLRLAAKEGV EKVYIHAFLD GRDVGPKTAQ SYIDATNEVI KETGVGQFAT ISGRYYSMDR DKRWDRVEKC YRAMVNGEGP TYKSAEECVE DSYANGIYDE FVLPSVIVTE DNTPVATIND DDAVIFYNFR PDRAIQIARV FTNEDFREFD RGEKVPHIPE FVCMTHFSET VDGYVAFKPM NLDNTLGEVV AQAGLKQLRI AETEKYPHVT FFFSGGREAE FPGEERILIN SPKVATYDLK PEMSIYEVTD ALVNEIENDK HDVIILNFAN CDMVGHSGMM EPTIKAVEAT DECLGKVVEA ILAKDGVALI TADHGNADEE LTSDGEPMTA HTTNPVPFIV TKNDVELREG GILGDIAPTM LTLLGVEQPK EMTGKTIIK //