(data stored in SCRATCH 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   11-DEC-2019, entry version 34.
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;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73258.1};
RN   [1] {ECO:0000313|EMBL:ADP73258.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73258.1};
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., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   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 3-
CC       phosphoglycerate. {ECO:0000256|SAAS:SAAS00978404}.
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|HAMAP-Rule:MF_01038,
CC         ECO:0000256|SAAS:SAAS01223275};
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|HAMAP-Rule:MF_01038,
CC       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}.
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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   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   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01038,
KW   ECO:0000256|SAAS:SAAS00850939};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01038, ECO:0000256|SAAS:SAAS00850936,
KW   ECO:0000313|EMBL:ADP73258.1};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01038, ECO:0000256|PIRSR:PIRSR001492-
KW   3, ECO:0000256|SAAS:SAAS00241368};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01038,
KW   ECO:0000256|PIRSR:PIRSR001492-3, ECO:0000256|SAAS:SAAS00241382};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01038};
KW   Sporulation {ECO:0000256|HAMAP-Rule:MF_01038}.
FT   DOMAIN          4..498
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
FT   DOMAIN          82..299
FT                   /note="iPGM_N"
FT                   /evidence="ECO:0000259|Pfam:PF06415"
FT   REGION          153..154
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   REGION          261..264
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   ACT_SITE        62
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-1"
FT   METAL           12
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-3"
FT   METAL           62
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-3"
FT   METAL           403
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-3"
FT   METAL           407
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-3"
FT   METAL           444
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-3"
FT   METAL           445
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-3"
FT   METAL           462
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         123
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         185
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         191
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         336
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01038,
FT                   ECO:0000256|PIRSR:PIRSR001492-2"
FT   MOD_RES         36
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000256|HAMAP-Rule: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
//

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