(data stored in ACNUC1104 zone)

SWISSPROT: D7A242_STAND

ID   D7A242_STAND            Unreviewed;       207 AA.
AC   D7A242;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
DE            Short=BPG-dependent PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=dPGM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            EC=5.4.2.11 {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
GN   Name=gpmA {ECO:0000256|HAMAP-Rule:MF_01039};
GN   OrderedLocusNames=Snov_0324 {ECO:0000313|EMBL:ADH87658.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87658.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87658.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
CC       3-phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01039,
CC       ECO:0000256|RuleBase:RU004512}.
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=5.4.2.11; Evidence={ECO:0000256|HAMAP-Rule:MF_01039,
CC         ECO:0000256|RuleBase:RU004512, ECO:0000256|SAAS:SAAS01121992};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-
CC       Rule:MF_01039, ECO:0000256|RuleBase:RU004512}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01039}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000256|HAMAP-Rule:MF_01039,
CC       ECO:0000256|SAAS:SAAS01086980}.
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DR   EMBL; CP002026; ADH87658.1; -; Genomic_DNA.
DR   RefSeq; WP_013165163.1; NC_014217.1.
DR   STRING; 639283.Snov_0324; -.
DR   EnsemblBacteria; ADH87658; ADH87658; Snov_0324.
DR   KEGG; sno:Snov_0324; -.
DR   eggNOG; ENOG4105DKJ; Bacteria.
DR   eggNOG; COG0588; LUCA.
DR   HOGENOM; HOG000221682; -.
DR   KO; K01834; -.
DR   OMA; RMLPYWY; -.
DR   OrthoDB; 1122642at2; -.
DR   BioCyc; SNOV639283:G1GLM-328-MONOMER; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000006633; Chromosome.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   HAMAP; MF_01039; PGAM_GpmA; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; PTHR11931; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D7A242.
DR   SWISS-2DPAGE; D7A242.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006633};
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_01039};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01039,
KW   ECO:0000256|SAAS:SAAS01087007};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01039,
KW   ECO:0000256|SAAS:SAAS01086924};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633}.
FT   REGION       10     17       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION       23     24       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION       89     92       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION      116    117       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION      160    161       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   ACT_SITE     11     11       Tele-phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
FT   ACT_SITE     89     89       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
FT   BINDING      62     62       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01039}.
FT   BINDING     100    100       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01039}.
FT   SITE        159    159       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
SQ   SEQUENCE   207 AA;  23177 MW;  E6A147785E7D1FAF CRC64;
     MSERLLVLVR HGQSEWNLKN LFTGWRDPDL TELGVEEAKT AGKRLKADGY TFDIAFTSKL
     SRAQKTLDLA LAELGQTGLP TIENLALNER DYGELSGLNK DDARVKWGEE QVHIWRRSYD
     VPPPGGESLK DTIARTLPYY VTEILPKVLQ GNRTLVVAHG NSLRALIMVL EKHTPESIMK
     RELLTGVPVI YRLKPDSTIE SVVDLAG
//

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