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ID Q13E67_RHOPS Unreviewed; 504 AA.
AC Q13E67;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 08-MAY-2019, entry version 97.
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=RPD_0384 {ECO:0000313|EMBL:ABE37622.1};
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37622.1, ECO:0000313|Proteomes:UP000001818};
RN [1] {ECO:0000313|EMBL:ABE37622.1, ECO:0000313|Proteomes:UP000001818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5 {ECO:0000313|EMBL:ABE37622.1,
RC ECO:0000313|Proteomes:UP000001818};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
CC 3-phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01038,
CC ECO:0000256|SAAS:SAAS00978404}.
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}.
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DR EMBL; CP000283; ABE37622.1; -; Genomic_DNA.
DR RefSeq; WP_011500810.1; NC_007958.1.
DR STRING; 316057.RPD_0384; -.
DR EnsemblBacteria; ABE37622; ABE37622; RPD_0384.
DR KEGG; rpd:RPD_0384; -.
DR eggNOG; ENOG4105CJI; Bacteria.
DR eggNOG; COG0696; LUCA.
DR HOGENOM; HOG000223664; -.
DR KO; K15633; -.
DR OMA; FMDGRDT; -.
DR OrthoDB; 338375at2; -.
DR BioCyc; RPAL316057:RPD_RS01980-MONOMER; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001818; 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; Q13E67.
DR SWISS-2DPAGE; Q13E67.
KW Complete proteome {ECO:0000313|Proteomes:UP000001818};
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:ABE37622.1};
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}.
FT DOMAIN 6 491 Metalloenzyme. {ECO:0000259|Pfam:
FT PF01676}.
FT DOMAIN 83 291 iPGM_N. {ECO:0000259|Pfam:PF06415}.
FT REGION 153 154 Substrate binding. {ECO:0000256|HAMAP-
FT Rule:MF_01038}.
FT REGION 254 257 Substrate binding. {ECO:0000256|HAMAP-
FT Rule:MF_01038}.
FT ACT_SITE 63 63 Phosphoserine intermediate.
FT {ECO:0000256|HAMAP-Rule:MF_01038}.
FT METAL 13 13 Manganese 2. {ECO:0000256|HAMAP-Rule:
FT MF_01038}.
FT METAL 63 63 Manganese 2. {ECO:0000256|HAMAP-Rule:
FT MF_01038}.
FT METAL 397 397 Manganese 1. {ECO:0000256|HAMAP-Rule:
FT MF_01038}.
FT METAL 401 401 Manganese 1. {ECO:0000256|HAMAP-Rule:
FT MF_01038}.
FT METAL 438 438 Manganese 2. {ECO:0000256|HAMAP-Rule:
FT MF_01038}.
FT METAL 439 439 Manganese 2. {ECO:0000256|HAMAP-Rule:
FT MF_01038}.
FT METAL 457 457 Manganese 1. {ECO:0000256|HAMAP-Rule:
FT MF_01038}.
FT BINDING 124 124 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01038}.
FT BINDING 183 183 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01038}.
FT BINDING 189 189 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01038}.
FT BINDING 330 330 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01038}.
SQ SEQUENCE 504 AA; 53506 MW; E5BD74B799EEA04B CRC64;
MQSRRPVMLV ILDGWGWRED PADNAVLQAD TPTFDALWAN GPHAFLRTSG KSVGLPNGQM
GNSEVGHLNI GAGRVVMQDL PRISDAIASG EIGQAPELLA FIEKLRASGG TCHLMGLVSP
GGVHSLQDHA CALAKILAKA GVPTVLHAFT DGRDTPPKSA VDDIARVRAE LPPNVPIATV
SGRYYAMDRD NRWERVSKAY GVIADADGPR FADADAVVAA GYASGVNDEF IVPAVVGDYQ
GMRDGDGVLC FNFRADRVRE ILATLLDPTF TGFPRKRVLK IAAAAGMTQY STALDALMRT
IFPPQSLVNG LGQVVAATGR HQLRMAETEK YPHVTYFLNG GEEVPYPGED RIMVPSPKVA
TYDLQPEMSA PELGDKAVQA IESGKYDMII LNFANPDMVG HTGSLPAAIK AVETVDTQLG
RIVAAIRQAG GALLVTADHG NCEMLRDPVT GGPHTAHTTN PVPVLLVGHE GPLADGQLSD
LAPTLLKLMD LPQPAEMTGQ SLIG
//
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