(data stored in ACNUC30630 zone)

SWISSPROT: GPMI_THERP

ID   GPMI_THERP              Reviewed;         524 AA.
AC   B9KYT9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   11-DEC-2019, entry version 67.
DE   RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01038};
DE            Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01038};
DE            Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01038};
DE            Short=iPGM {ECO:0000255|HAMAP-Rule:MF_01038};
DE            EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01038};
GN   Name=gpmI {ECO:0000255|HAMAP-Rule:MF_01038}; OrderedLocusNames=trd_0643;
OS   Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC   Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae;
OC   Thermomicrobium.
OX   NCBI_TaxID=309801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27502 / DSM 5159 / P-2;
RX   PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA   Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA   Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA   Eisen J.A.;
RT   "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT   Thermomicrobium roseum.";
RL   PLoS ONE 4:E4207-E4207(2009).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01038};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01038};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01038};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC       Rule:MF_01038}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01038}.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01038}.
DR   EMBL; CP001275; ACM06389.1; -; Genomic_DNA.
DR   RefSeq; WP_012642039.1; NC_011959.1.
DR   SMR; B9KYT9; -.
DR   STRING; 309801.trd_0643; -.
DR   EnsemblBacteria; ACM06389; ACM06389; trd_0643.
DR   KEGG; tro:trd_0643; -.
DR   eggNOG; ENOG4105CJI; Bacteria.
DR   eggNOG; COG0696; LUCA.
DR   HOGENOM; HOG000223664; -.
DR   KO; K15633; -.
DR   OMA; FMDGRDT; -.
DR   OrthoDB; 338375at2; -.
DR   BioCyc; TROS309801:G1GU8-591-MONOMER; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000000447; 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   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; B9KYT9.
DR   SWISS-2DPAGE; B9KYT9.
KW   Glycolysis; Isomerase; Manganese; Metal-binding.
FT   CHAIN           1..524
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_1000149491"
FT   REGION          154..155
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   REGION          262..265
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   ACT_SITE        63
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   METAL           13
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   METAL           63
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   METAL           404
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   METAL           408
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   METAL           445
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   METAL           446
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   METAL           464
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         124
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         186
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         192
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         337
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
SQ   SEQUENCE   524 AA;  57422 MW;  AE6877EE3A334FB2 CRC64;
     MDRPPMVCLV VLDGWAIGPD YPGNAIRAAH TPVMDRLQAT YPMTTLRCWG RDVGLPDDQM
     GNSEVGHLNL GAGRIVYQLI TRIDLAIEDG SFFQNEAFQR ALDRARQPGR TLHLMGLIGD
     GGVHSHQRHL LALLELAARA GISRVAVHAF TDGRDTAPTS GIEHLRELLA ALDRLRTGFV
     ATVSGRYYAM DRDKRWERTK LAYDAIVCGL GQTARSPLEA IERSYAQGIT DEFIVPTVIV
     DAEGKPLATI NDGDAVIFFN FRADRARQLT QALTDAGGFT AFPRCRWPRD LLMVTMAEYE
     PHFPVLVAFA PDIVRVPLAR VLSDVGLRQF HTAETEKYAH VTYFFNGGRE EPFPGEDRLL
     VPSPKVPTYD LKPEMSAPEV TDAAVQAIVS QRYAFVLVNY ANPDMVGHTG VFAAAVAAVE
     CVDRCLGRIE QAVRSVNGYL VVTADHGNAD EMLVPGTNEV WTAHTKNPVP FILVAPNHSP
     FRSVALRTGG RLADVAPTIL EIMGLPQPEE MTGRSLIVAP SVGR
//

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