(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BIK7_GEOS0

ID   A0A0F6BIK7_GEOS0        Unreviewed;       512 AA.
AC   A0A0F6BIK7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 28.
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   OrderedLocusNames=GY4MC1_0417 {ECO:0000313|EMBL:ADP73258.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73258.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73258.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73258.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
CC       3-phosphoglycerate. {ECO:0000256|SAAS:SAAS00978404}.
CC   -!- FUNCTION: Essential for rapid growth and for sporulation.
CC       Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = 3-phospho-D-glycerate;
CC         Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC         EC=5.4.2.12; Evidence={ECO:0000256|HAMAP-Rule:MF_01038,
CC         ECO:0000256|SAAS:SAAS01115646};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         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|HAMAP-
CC       Rule:MF_01038, ECO:0000256|SAAS:SAAS00850947}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01038}.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. {ECO:0000256|HAMAP-Rule:MF_01038,
CC       ECO:0000256|SAAS:SAAS00850933}.
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; CP002293; ADP73258.1; -; Genomic_DNA.
DR   RefSeq; WP_003248112.1; NC_014650.1.
DR   EnsemblBacteria; ADP73258; ADP73258; GY4MC1_0417.
DR   KEGG; gmc:GY4MC1_0417; -.
DR   KO; K15633; -.
DR   OMA; FMDGRDT; -.
DR   OrthoDB; 338375at2; -.
DR   BioCyc; GSP581103:G1GOQ-464-MONOMER; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000002034; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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;
DR   PRODOM; A0A0F6BIK7.
DR   SWISS-2DPAGE; A0A0F6BIK7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01038,
KW   ECO:0000256|SAAS:SAAS00850939};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01038,
KW   ECO:0000256|SAAS:SAAS00850936, ECO:0000313|EMBL:ADP73258.1};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01038,
KW   ECO:0000256|SAAS:SAAS00241368};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01038,
KW   ECO:0000256|SAAS:SAAS00241382};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01038};
KW   Sporulation {ECO:0000256|HAMAP-Rule:MF_01038}.
FT   DOMAIN        4    498       Metalloenzyme. {ECO:0000259|Pfam:
FT                                PF01676}.
FT   DOMAIN       82    299       iPGM_N. {ECO:0000259|Pfam:PF06415}.
FT   REGION      153    154       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01038}.
FT   REGION      261    264       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01038}.
FT   ACT_SITE     62     62       Phosphoserine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01038}.
FT   METAL        12     12       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL        62     62       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       403    403       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       407    407       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       444    444       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       445    445       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       462    462       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     123    123       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     185    185       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     191    191       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     336    336       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   MOD_RES      36     36       Phosphotyrosine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
SQ   SEQUENCE   512 AA;  57040 MW;  57E4F81C64C8B013 CRC64;
     MSKKPVALII LDGFALRDET YGNAIAQAKK PNFDRYWNEY PHSTLTACGE AVGLPEGQMG
     NSEVGHLNIG AGRIVYQSLT RVNIAIREGE FDRNETFLAA MNHVKEKGTN LHIFGLLSDG
     GVHSHINHLY ALLKLAAKEG VKNVYIHGFL DGRDVGPQTA PKYIKELQEK IKEYGVGEIA
     TLSGRYYSMD RDKRWERVEK AYRAMVYGEG PTYRDPLECI EDSYQHGIYD EFVLPSVIVR
     EDGSPVATIK DEDAIIFYNF RPDRAIQISN TFTNEDFREF DRGPKHPKNL FFVCLTHFSE
     TVKGYVAFKP TNLDNTIGEV LSQHGLRQLR IAETEKYPHV TYFMNGGREE KFPGEDRILI
     NSPKVATYDL KPEMSAYEVT DALLKEIEAD KYDAIILNYA NPDMVGHSGK LEPTIKAIEA
     VDECLGKVVD AILAKGGIAI ITADHGNADE VLTPDGKPQT AHTTNPVPVI VTKKGIELRK
     GGILGDLAPT MLDLLGLPQP KEMTGKTLII KK
//

If you have problems or comments...

PBIL Back to PBIL home page