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GPMI_SYNP2
ID   GPMI_SYNP2              Reviewed;         525 AA.
AC   B1XJ47;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 99.
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};
GN   OrderedLocusNames=SYNPCC7002_A2233;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000951; ACB00213.1; -; Genomic_DNA.
DR   RefSeq; WP_012307831.1; NC_010475.1.
DR   AlphaFoldDB; B1XJ47; -.
DR   SMR; B1XJ47; -.
DR   STRING; 32049.SYNPCC7002_A2233; -.
DR   EnsemblBacteria; ACB00213; ACB00213; SYNPCC7002_A2233.
DR   KEGG; syp:SYNPCC7002_A2233; -.
DR   eggNOG; COG0696; Bacteria.
DR   HOGENOM; CLU_026099_2_0_3; -.
DR   OMA; FMDGRDT; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001688; 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;
KW   Glycolysis; Isomerase; Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..525
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_1000135909"
FT   ACT_SITE        65
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         15
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         65
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         156..157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         258..261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         398
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         402
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         439
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         440
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT   BINDING         457
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
SQ   SEQUENCE   525 AA;  57361 MW;  320EAC2B6D238259 CRC64;
     MANAPVSPVV LVILDGWGYR QEANANAIAA ANTPNVDAFF ATYPSTLIHT SGKRVGLPDG
     QMGNSEVGHL NLGAGRVVPQ ELVRISDAIE DGSFLRNDVL VKVCRETRQA GKKLHLIGLC
     SDGGVHSHLN HLLGLLDLAK VNGIADVHIH AITDGRDTNT TEGINYLQQI QAHIDKFGVG
     SISTISGRYF AMDRDRRWDR VKQAYDVMTQ NGNLDQRSFA EILQSHYDNG VTDEFIPPVR
     LKEGAIEPGD GVIFYNFRPD RARQLSYALV DKNFQGFERE LIPDLNFVTF TQYDANLPVQ
     VAFAPQNLTK ILGEVIADNG LKQFRTAETE KYPHVTYFFN GGLEVAFEGE DRELISSPQV
     ATYDQKPEMS AKAVTDAACQ AIEKGIYSLV VINYANPDMV GHTGKLEAAV QAIETVDHCL
     GRLVATIGKM GGTTLITADH GNAEYMADQN GKSWTAHTTN PVPFILIEGE RRKVVGHGAD
     VVLRENGCLA DVAPTILDIL GIDKPQEMTG QSLIAPAPYA VTRRR
 
 
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