(data stored in ACNUC7421 zone)

SWISSPROT: Q2IMH9_ANADE

ID   Q2IMH9_ANADE            Unreviewed;       516 AA.
AC   Q2IMH9;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 102.
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=Adeh_0235 {ECO:0000313|EMBL:ABC80012.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC80012.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-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; CP000251; ABC80012.1; -; Genomic_DNA.
DR   RefSeq; WP_011419295.1; NC_007760.1.
DR   STRING; 290397.Adeh_0235; -.
DR   EnsemblBacteria; ABC80012; ABC80012; Adeh_0235.
DR   KEGG; ade:Adeh_0235; -.
DR   eggNOG; ENOG4105CJI; Bacteria.
DR   eggNOG; COG0696; LUCA.
DR   HOGENOM; HOG000223664; -.
DR   KO; K15633; -.
DR   OMA; FMDGRDT; -.
DR   BioCyc; ADEH290397:G1G5W-242-MONOMER; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001935; 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; Q2IMH9.
DR   SWISS-2DPAGE; Q2IMH9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
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:ABC80012.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935}.
FT   DOMAIN        5    502       Metalloenzyme. {ECO:0000259|Pfam:
FT                                PF01676}.
FT   DOMAIN       83    300       iPGM_N. {ECO:0000259|Pfam:PF06415}.
FT   REGION      154    155       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01038}.
FT   REGION      262    265       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       404    404       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       408    408       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       445    445       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       446    446       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   METAL       464    464       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     124    124       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     186    186       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     192    192       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
FT   BINDING     336    336       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01038}.
SQ   SEQUENCE   516 AA;  56222 MW;  422E8CBA30B08480 CRC64;
     MPKTKPVLLV VLDGWGIRAA REANAIAIAG TPNMDALQRE FPHAALETSG LSVGLPEGQM
     GNSEVGHTNL GAGRIVYQDL VRINRAVEDG SFYKNDALLL ACRRAREAGG ALHLLGLVSD
     GGVHSHVEHL HACLELARRE GVARTYVHAF MDGRDTPPKS GLDYLAAVER RIAAAGYGKV
     ATVTGRYWAM DRDKRWDRVA QAYAAMVSGE GFKAASGAAA MEAAYARGET DEFVKPTVVV
     NGDGKPVGSI RDGDAILFFN FRADRAREIT RAFTQDGFHD FERKAVPRLS AYVCMTQYDE
     TFTLPVAYAP QDLTEIFPEI VARAGLRQLR TAETEKYAHV TFFFNGGRET VFQNEDRILV
     PSPRDVKTYD EKPEMSAREV TDKLVQALGT GQYGFALVNY ANPDMVGHTG LLDAAVKAVR
     VVDECVGRLW QAARKQGMAM LVTADHGNCE MMTDPVTGQP HTAHTLNPVP FILADPDFRG
     AKLREKGVLA DVAPTALQVM GLPQPKEMKG LGLVIR
//

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