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Conserved domains on  [gi|1258190867|ref|WP_097528983|]
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histidine phosphatase family protein, partial [Listeria monocytogenes]

Protein Classification

histidine phosphatase family protein( domain architecture ID 10001383)

histidine phosphatase family protein is a probable phosphatase that may catalyze the dephosphorylation of a phosphorylated substrate involving a conserved catalytic histidine residue which becomes phosphorylated during the reaction

CATH:  3.40.50.1240
Gene Ontology:  GO:0016791
PubMed:  18092946
SCOP:  3000781

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
8-93 2.63e-29

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


:

Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 103.10  E-value: 2.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   8 VYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLREIPFDAVYTSDRGRTIETAGIVLRESNqahLEINELRDF 87
Cdd:COG0406     4 LYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALG---LPVEVDPRL 80


                  ....*.
gi 1258190867  88 REFGFG 93
Cdd:COG0406    81 REIDFG 86
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
8-93 2.63e-29

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 103.10  E-value: 2.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   8 VYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLREIPFDAVYTSDRGRTIETAGIVLRESNqahLEINELRDF 87
Cdd:COG0406     4 LYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALG---LPVEVDPRL 80


                  ....*.
gi 1258190867  88 REFGFG 93
Cdd:COG0406    81 REIDFG 86
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 8-93 3.05e-28

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 100.36  E-value: 3.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   8 VYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLREIPFDAVYTSDRGRTIETAGIVLRESNqahLEINELRDF 87
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALG---LPVEIDPRL 77


                  ....*.
gi 1258190867  88 REFGFG 93
Cdd:pfam00300  78 REIDFG 83
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 7-89 2.72e-27

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 97.01  E-value: 2.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   7 NVYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE--IPFDAVYTSDRGRTIETAGIVLRESNqaHLEINEL 84
Cdd:cd07067     1 RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKElgIKFDRIYSSPLKRAIQTAEIILEELP--GLPVEVD 78


                  ....*
gi 1258190867  85 RDFRE 89
Cdd:cd07067    79 PRLRE 83
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 8-93 7.21e-23

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 85.98  E-value: 7.21e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867    8 VYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE---IPFDAVYTSDRGRTIETAgivlresnQAHLEINEL 84
Cdd:smart00855   2 LYLIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLASlllPRFDVVYSSPLKRARQTA--------EALAIALGL 73


                   ....*....
gi 1258190867   85 RDFREFGFG 93
Cdd:smart00855  74 PGLRERDFG 82
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 8-93 9.17e-20

alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 78.43  E-value: 9.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   8 VYLVRHGKTMFNTSRRVqGWSDTPLTNEGIEVAEFLGRGLREIPFDAVYTSDRGRTIETAGIVLresNQAHLEINELRDF 87
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCY-GQTDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILA---ERRGLPIIKDDRL 76


                  ....*.
gi 1258190867  88 REFGFG 93
Cdd:TIGR03162  77 REMDFG 82
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
6-80 1.02e-16

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 71.30  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   6 LNVYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLREIPFDAVYTSDRGRTIETAGIV-------------LR 72
Cdd:PRK03482    2 LQVYLVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVAERAKELGITHIISSDLGRTRRTAEIIaqacgcdiifdprLR 81


                  ....*...
gi 1258190867  73 ESNQAHLE 80
Cdd:PRK03482   82 ELNMGVLE 89
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
8-93 2.63e-29

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 103.10  E-value: 2.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   8 VYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLREIPFDAVYTSDRGRTIETAGIVLRESNqahLEINELRDF 87
Cdd:COG0406     4 LYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEALG---LPVEVDPRL 80


                  ....*.
gi 1258190867  88 REFGFG 93
Cdd:COG0406    81 REIDFG 86
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 8-93 3.05e-28

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 100.36  E-value: 3.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   8 VYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLREIPFDAVYTSDRGRTIETAGIVLRESNqahLEINELRDF 87
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEALG---LPVEIDPRL 77


                  ....*.
gi 1258190867  88 REFGFG 93
Cdd:pfam00300  78 REIDFG 83
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 7-89 2.72e-27

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 97.01  E-value: 2.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   7 NVYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE--IPFDAVYTSDRGRTIETAGIVLRESNqaHLEINEL 84
Cdd:cd07067     1 RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKElgIKFDRIYSSPLKRAIQTAEIILEELP--GLPVEVD 78


                  ....*
gi 1258190867  85 RDFRE 89
Cdd:cd07067    79 PRLRE 83
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 8-93 7.21e-23

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 85.98  E-value: 7.21e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867    8 VYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE---IPFDAVYTSDRGRTIETAgivlresnQAHLEINEL 84
Cdd:smart00855   2 LYLIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLASlllPRFDVVYSSPLKRARQTA--------EALAIALGL 73


                   ....*....
gi 1258190867   85 RDFREFGFG 93
Cdd:smart00855  74 PGLRERDFG 82
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 8-88 9.80e-22

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


Pssm-ID: 132716 [Multi-domain]  Cd Length: 153  Bit Score: 82.85  E-value: 9.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   8 VYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE--IPFDAVYTSDRGRTIETAGIVLRESNQaHLEINELR 85
Cdd:cd07040     2 LYLVRHGEREPNAEGRFTGWGDGPLTEKGRQQARELGKALREryIKFDRIYSSPLKRAIQTAEIILEGLFE-GLPVEVDP 80


                  ...
gi 1258190867  86 DFR 88
Cdd:cd07040    81 RAR 83
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 8-93 9.17e-20

alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 78.43  E-value: 9.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   8 VYLVRHGKTMFNTSRRVqGWSDTPLTNEGIEVAEFLGRGLREIPFDAVYTSDRGRTIETAGIVLresNQAHLEINELRDF 87
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCY-GQTDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILA---ERRGLPIIKDDRL 76


                  ....*.
gi 1258190867  88 REFGFG 93
Cdd:TIGR03162  77 REMDFG 82
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
6-80 1.02e-16

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 71.30  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   6 LNVYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLREIPFDAVYTSDRGRTIETAGIV-------------LR 72
Cdd:PRK03482    2 LQVYLVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVAERAKELGITHIISSDLGRTRRTAEIIaqacgcdiifdprLR 81


                  ....*...
gi 1258190867  73 ESNQAHLE 80
Cdd:PRK03482   82 ELNMGVLE 89
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
9-84 1.69e-15

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 67.77  E-value: 1.69e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1258190867   9 YLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLREIPFDAVYTSDRGRTIETAGIVL---RESNQAHLEINEL 84
Cdd:PRK15004    4 WLVRHGETQANVDGLYSGHAPTPLTARGIEQAQNLHTLLRDVPFDLVLCSELERAQHTARLVLsdrQLPVHIIPELNEM 82
pgm_1 TIGR01258
phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are ...
 10-82 5.13e-14

phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are phosphoglycerate mutase (EC 5.4.2.1). This enzyme interconverts 2-phosphoglycerate and 3-phosphoglycerate. The enzyme is transiently phosphorylated on an active site histidine by 2,3-diphosphoglyerate, which is both substrate and product. Some members of this family have are phosphoglycerate mutase as a minor activity and act primarily as a bisphoglycerate mutase, interconverting 2,3-diphosphoglycerate and 1,3-diphosphoglycerate (EC 5.4.2.4). This model is designated as a subfamily for this reason. The second and third paralogs in S. cerevisiae are somewhat divergent and apparently inactive (see PUBMED:9544241) but are also part of this subfamily phylogenetically.


Pssm-ID: 213596 [Multi-domain]  Cd Length: 245  Bit Score: 64.74  E-value: 5.13e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1258190867  10 LVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE--IPFDAVYTSDRGRTIETAGIVLRESNQAHLEIN 82
Cdd:TIGR01258   5 LVRHGESEWNALNLFTGWVDVKLSEKGQQEAKRAGELLKEegYEFDVAYTSLLKRAIHTLNIALDELDQLWIPVK 79
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 10-79 1.26e-13

Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-dependent) is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440353  Cd Length: 229  Bit Score: 63.18  E-value: 1.26e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1258190867  10 LVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE--IPFDAVYTSDRGRTIETAGIVLRESNQAHL 79
Cdd:COG0588     5 LLRHGESEWNLENRFTGWTDVDLSEKGRAEAKRAGRLLKEagFLFDVAYTSVLKRAIRTLWIVLDEMDRLWI 76
PRK13463 PRK13463
phosphoserine phosphatase 1;
5-93 5.17e-13

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 61.22  E-value: 5.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   5 KLNVYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLREIPFDAVYTSDRGRTIETAGIVLRESNqahLEINEL 84
Cdd:PRK13463    2 KTTVYVTRHGETEWNVAKRMQGRKNSALTENGILQAKQLGERMKDLSIHAIYSSPSERTLHTAELIKGERD---IPIIAD 78


                  ....*....
gi 1258190867  85 RDFREFGFG 93
Cdd:PRK13463   79 EHFYEINMG 87
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
10-88 8.56e-13

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 61.08  E-value: 8.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867  10 LVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE--IPFDAVYTSDRGRTIETAGIVLRESNQahLEINELRDF 87
Cdd:PRK14116    6 LIRHGQSEWNLSNQFTGWVDVDLSEKGVEEAKKAGRLIKEagLEFDQAYTSVLTRAIKTLHYALEESDQ--LWIPETKTW 83


                  .
gi 1258190867  88 R 88
Cdd:PRK14116   84 R 84
PRK01112 PRK01112
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
10-76 3.60e-12

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 234902  Cd Length: 228  Bit Score: 59.35  E-value: 3.60e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1258190867  10 LVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLREIPFDAVYTSDRGRTIETAGIVLRESNQ 76
Cdd:PRK01112    6 LLRHGQSVWNAKNLFTGWVDIPLSQQGIAEAIAAGEKIKDLPIDCIFTSTLVRSLMTALLAMTNHSS 72
gpmA PRK14118
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
6-88 1.43e-11

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172608  Cd Length: 227  Bit Score: 57.67  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   6 LNVYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE--IPFDAVYTSDRGRTIETAGIVLRESNQahLEINE 83
Cdd:PRK14118    1 MELVFIRHGFSEWNAKNLFTGWRDVNLTERGVEEAKAAGKKLKEagYEFDIAFTSVLTRAIKTCNIVLEESNQ--LWIPQ 78


                  ....*
gi 1258190867  84 LRDFR 88
Cdd:PRK14118   79 VKNWR 83
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 10-87 3.70e-11

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 56.24  E-value: 3.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867  10 LVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE--IPFDAVYTSDRGRTIETAGIVLRESNQAHLEI------ 81
Cdd:PRK01295    7 LVRHGQSEWNLKNLFTGWRDPDLTEQGVAEAKAAGRKLKAagLKFDIAFTSALSRAQHTCQLILEELGQPGLETirdqal 86


                  ....*.
gi 1258190867  82 NElRDF 87
Cdd:PRK01295   87 NE-RDY 91
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
10-79 2.16e-10

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 54.87  E-value: 2.16e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1258190867  10 LVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE--IPFDAVYTSDRGRTIETAGIVLRESNQAHL 79
Cdd:PRK14115    5 LIRHGESQWNKENRFTGWTDVDLSEKGVSEAKAAGKLLKEegYTFDVAYTSVLKRAIRTLWIVLDELDQMWL 76
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
 19-81 2.52e-10

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 54.66  E-value: 2.52e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1258190867  19 NTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE--IPFDAVYTSDRGRTIETAGIVLRESNQAHLEI 81
Cdd:PTZ00123    2 NKENRFTGWTDVPLSEKGVQEAREAGKLLKEkgFRFDVVYTSVLKRAIKTAWIVLEELGQLHVPV 66
gpmA PRK14119
phosphoglyceromutase; Provisional
 10-76 3.60e-10

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 54.13  E-value: 3.60e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1258190867  10 LVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE--IPFDAVYTSDRGRTIETAGIVLRESNQ 76
Cdd:PRK14119    6 LCRHGQSEWNAKNLFTGWEDVNLSEQGINEATRAGEKVREnnIAIDVAFTSLLTRALDTTHYILTESKQ 74
gpmA PRK14120
phosphoglyceromutase; Provisional
 1-88 3.87e-09

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 51.19  E-value: 3.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   1 MATGKLnvYLVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE---IPfDAVYTSDRGRTIETAGIVLRESNQa 77
Cdd:PRK14120    2 MMTYTL--VLLRHGESEWNAKNLFTGWVDVDLTEKGEAEAKRGGELLAEagvLP-DVVYTSLLRRAIRTANLALDAADR- 77

                          90
                  ....*....|.
gi 1258190867  78 hLEINELRDFR 88
Cdd:PRK14120   78 -LWIPVRRSWR 87
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 10-93 4.50e-09

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 51.52  E-value: 4.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867  10 LVRHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE-IPFDAVYTSDRGRTIETAGIVLResnQAHLEINELRDFR 88
Cdd:PRK07238  176 LLRHGQTELSVQRRYSGRGNPELTEVGRRQAAAAARYLAArGGIDAVVSSPLQRARDTAAAAAK---ALGLDVTVDDDLI 252


                  ....*
gi 1258190867  89 EFGFG 93
Cdd:PRK07238  253 ETDFG 257
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
8-73 4.62e-09

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 49.87  E-value: 4.62e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258190867   8 VYLVRHGKTmfntSRRVQGWSDT--PLTNEGIEVAEFLGRGLRE--IPFDAVYTSDRGRTIETAGIVLRE 73
Cdd:COG2062     1 LILVRHAKA----EWRAPGGDDFdrPLTERGRRQARAMARWLAAlgLKPDRILSSPALRARQTAEILAEA 66
gpmA PRK14117
phosphoglyceromutase; Provisional
 12-76 1.56e-07

phosphoglyceromutase; Provisional


Pssm-ID: 184517  Cd Length: 230  Bit Score: 46.94  E-value: 1.56e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1258190867  12 RHGKTMFNTSRRVQGWSDTPLTNEGIEVAEFLGRGLRE--IPFDAVYTSDRGRTIETAGIVLRESNQ 76
Cdd:PRK14117    8 RHGESEWNKANLFTGWADVDLSEKGTQQAIDAGKLIKEagIEFDLAFTSVLKRAIKTTNLALEASDQ 74
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 6-70 1.30e-03

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 35.58  E-value: 1.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1258190867   6 LNVYLVRHGKTmfntsrRVQGWSDT--PLTNEGIEVAEFLGRGLRE--IPFDAVYTSDRGRTIETAGIV 70
Cdd:TIGR00249   1 MQLFIMRHGDA------ALDAASDSvrPLTTNGCDESRLVAQWLKGqgVEIERILVSPFVRAEQTAEIV 63
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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