(data stored in ACNUC7421 zone)

SWISSPROT: Q13E67_RHOPS

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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