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Conserved domains on  [gi|380807051|gb|AFE75401|]
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6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4, partial [Macaca mulatta]

Protein Classification

phosphoglycerate mutase family protein( domain architecture ID 10162637)

phosphoglycerate mutase family protein belonging to the histidine phosphatase superfamily, contains a conserved His residue that is transiently phosphorylated during the catalytic cycle; similar to Saccharomyces cerevisiae phosphoglycerate mutase PMU1 that may have a function related to the manipulation of phosphate groups on carbohydrates

CATH:  3.40.50.1240
PubMed:  18092946|2543188
SCOP:  3000781

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 26-88 5.15e-23

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: 85.84  E-value: 5.15e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380807051  26 IYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTAEAL 88
Cdd:cd07067    2 LYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEII 66
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 1-23 2.87e-09

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


The actual alignment was detected with superfamily member pfam01591:

Pssm-ID: 450170  Cd Length: 223  Bit Score: 51.57  E-value: 2.87e-09
                          10        20
                  ....*....|....*....|...
gi 380807051    1 VNRVADHIQSRIVYYLMNIHVTP 23
Cdd:pfam01591 201 VNNVQGYLQSRIVYYLMNIHVTP 223
 
Name Accession Description Interval E-value
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 26-88 5.15e-23

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: 85.84  E-value: 5.15e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380807051  26 IYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTAEAL 88
Cdd:cd07067    2 LYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEII 66
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 26-89 5.62e-20

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: 79.18  E-value: 5.62e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380807051   26 IYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKdlKVWTSQMKRTIQTAEALG 89
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEIIA 64
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 26-89 1.36e-18

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: 74.80  E-value: 1.36e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380807051    26 IYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQ-NIKDLKVWTSQMKRTIQTAEALG 89
Cdd:smart00855   2 LYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLLASLlLPRFDVVYSSPLKRARQTAEALA 68
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
26-89 5.13e-17

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 71.51  E-value: 5.13e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380807051  26 IYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKdlKVWTSQMKRTIQTAEALG 89
Cdd:COG0406    4 LYLVRHGETEWNAEGRLQGrlDVPLTELGRAQARALAERLADIPFD--AVYSSPLQRARQTAEALA 67
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1-84 1.49e-10

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380807051   1 VNRVADHIQSRIVYYLMNIHVTPRSIYLCRHGESELNLKGRIGGDPGLSPRGREFAKSLAQ-FISDQNIKDLKVWTSQMK 79
Cdd:PTZ00322 397 LNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEYVDLLSGRIGGNSRLTERGRAYSRALFEyFQKEISTTSFTVMSSCAK 476


                 ....*
gi 380807051  80 RTIQT 84
Cdd:PTZ00322 477 RCTET 481
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
 1-23 2.87e-09

6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. This enzyme contains a P-loop motif.


Pssm-ID: 396253  Cd Length: 223  Bit Score: 51.57  E-value: 2.87e-09
                          10        20
                  ....*....|....*....|...
gi 380807051    1 VNRVADHIQSRIVYYLMNIHVTP 23
Cdd:pfam01591 201 VNNVQGYLQSRIVYYLMNIHVTP 223
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 26-89 2.12e-08

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: 48.77  E-value: 2.12e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380807051   26 IYLCRHGESELNLKGRIG-GDPGLSPRGREFAKSLAQFISDQNIKdlKVWTSQMKRTIQTAEALG 89
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGqTDVPLAESGEEQAAALREKLADVPFD--AVYSSPLSRCRELAEILA 63
 
Name Accession Description Interval E-value
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 26-88 5.15e-23

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: 85.84  E-value: 5.15e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380807051  26 IYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTAEAL 88
Cdd:cd07067    2 LYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEII 66
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 26-89 5.62e-20

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: 79.18  E-value: 5.62e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380807051   26 IYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKdlKVWTSQMKRTIQTAEALG 89
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEIIA 64
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 26-88 8.80e-20

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: 77.84  E-value: 8.80e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380807051  26 IYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTAEAL 88
Cdd:cd07040    2 LYLVRHGEREPNAEGRFTGwgDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEII 66
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 26-89 1.36e-18

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: 74.80  E-value: 1.36e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380807051    26 IYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQ-NIKDLKVWTSQMKRTIQTAEALG 89
Cdd:smart00855   2 LYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLLASLlLPRFDVVYSSPLKRARQTAEALA 68
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
26-89 5.13e-17

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 71.51  E-value: 5.13e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380807051  26 IYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKdlKVWTSQMKRTIQTAEALG 89
Cdd:COG0406    4 LYLVRHGETEWNAEGRLQGrlDVPLTELGRAQARALAERLADIPFD--AVYSSPLQRARQTAEALA 67
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
26-89 6.50e-12

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 57.58  E-value: 6.50e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380807051  26 IYLCRHGESELNLKGRIGGDPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTAEALG 89
Cdd:COG2062    1 LILVRHAKAEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILA 64
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1-84 1.49e-10

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380807051   1 VNRVADHIQSRIVYYLMNIHVTPRSIYLCRHGESELNLKGRIGGDPGLSPRGREFAKSLAQ-FISDQNIKDLKVWTSQMK 79
Cdd:PTZ00322 397 LNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEYVDLLSGRIGGNSRLTERGRAYSRALFEyFQKEISTTSFTVMSSCAK 476


                 ....*
gi 380807051  80 RTIQT 84
Cdd:PTZ00322 477 RCTET 481
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 28-85 1.07e-09

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: 52.78  E-value: 1.07e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380807051  28 LCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIK-DLkVWTSQMKRTIQTA 85
Cdd:COG0588    5 LLRHGESEWNLENRFTGwtDVDLSEKGRAEAKRAGRLLKEAGFLfDV-AYTSVLKRAIRTL 64
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
 1-23 2.87e-09

6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. This enzyme contains a P-loop motif.


Pssm-ID: 396253  Cd Length: 223  Bit Score: 51.57  E-value: 2.87e-09
                          10        20
                  ....*....|....*....|...
gi 380807051    1 VNRVADHIQSRIVYYLMNIHVTP 23
Cdd:pfam01591 201 VNNVQGYLQSRIVYYLMNIHVTP 223
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 22-92 1.64e-08

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 49.59  E-value: 1.64e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380807051  22 TPRSIYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKDLkVWTSQMKRTIQTA----EALGVPY 92
Cdd:PRK07238 170 TPTRLLLLRHGQTELSVQRRYSGrgNPELTEVGRRQAAAAARYLAARGGIDA-VVSSPLQRARDTAaaaaKALGLDV 245
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 26-89 2.12e-08

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: 48.77  E-value: 2.12e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380807051   26 IYLCRHGESELNLKGRIG-GDPGLSPRGREFAKSLAQFISDQNIKdlKVWTSQMKRTIQTAEALG 89
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGqTDVPLAESGEEQAAALREKLADVPFD--AVYSSPLSRCRELAEILA 63
gpmA PRK14120
phosphoglyceromutase; Provisional
 22-85 3.32e-08

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 48.88  E-value: 3.32e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380807051  22 TPRSIYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTA 85
Cdd:PRK14120   3 MTYTLVLLRHGESEWNAKNLFTGwvDVDLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRTA 68
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
26-86 6.17e-08

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 47.80  E-value: 6.17e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380807051  26 IYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKdlKVWTSQMKRTIQTAE 86
Cdd:PRK03482   4 VYLVRHGETQWNAERRIQGqsDSPLTAKGEQQAMQVAERAKELGIT--HIISSDLGRTRRTAE 64
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 23-91 1.45e-06

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 43.91  E-value: 1.45e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380807051  23 PRSIYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTA----EALGVP 91
Cdd:PRK01295   2 SRTLVLVRHGQSEWNLKNLFTGwrDPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCqlilEELGQP 76
PRK13463 PRK13463
phosphoserine phosphatase 1;
25-86 4.51e-06

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 42.73  E-value: 4.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380807051  25 SIYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKdlKVWTSQMKRTIQTAE 86
Cdd:PRK13463   4 TVYVTRHGETEWNVAKRMQGrkNSALTENGILQAKQLGERMKDLSIH--AIYSSPSERTLHTAE 65
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
28-84 7.32e-06

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 42.21  E-value: 7.32e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 380807051  28 LCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQT 84
Cdd:PRK14116   6 LIRHGQSEWNLSNQFTGwvDVDLSEKGVEEAKKAGRLIKEAGLEFDQAYTSVLTRAIKT 64
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
26-86 9.72e-06

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 41.58  E-value: 9.72e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380807051  26 IYLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFIsdQNIKDLKVWTSQMKRTIQTAE 86
Cdd:PRK15004   3 LWLVRHGETQANVDGLYSGhaPTPLTARGIEQAQNLHTLL--RDVPFDLVLCSELERAQHTAR 63
gpmA PRK14119
phosphoglyceromutase; Provisional
 23-88 1.12e-05

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 41.80  E-value: 1.12e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380807051  23 PRSIyLCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTAEAL 88
Cdd:PRK14119   2 PKLI-LCRHGQSEWNAKNLFTGweDVNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTTHYI 68
PRK13462 PRK13462
acid phosphatase; Provisional
 28-90 1.82e-05

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 40.97  E-value: 1.82e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380807051  28 LCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTAEALGV 90
Cdd:PRK13462  10 LLRHGETEWSKSGRHTGrtELELTETGRTQAELAGQALGELELDDPLVISSPRRRALDTAKLAGL 74
PRK01112 PRK01112
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
28-85 1.19e-04

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 234902  Cd Length: 228  Bit Score: 38.55  E-value: 1.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380807051  28 LCRHGESELNLKGRIGG--DPGLSPRGREFAkslaqFISDQNIKDLKV---WTSQMKRTIQTA 85
Cdd:PRK01112   6 LLRHGQSVWNAKNLFTGwvDIPLSQQGIAEA-----IAAGEKIKDLPIdciFTSTLVRSLMTA 63
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
28-84 1.40e-04

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 38.69  E-value: 1.40e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 380807051  28 LCRHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQT 84
Cdd:PRK14115   5 LIRHGESQWNKENRFTGwtDVDLSEKGVSEAKAAGKLLKEEGYTFDVAYTSVLKRAIRT 63
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
 36-92 7.10e-04

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 36.56  E-value: 7.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380807051  36 LNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTA----EALGVPY 92
Cdd:PTZ00123   1 WNKENRFTGwtDVPLSEKGVQEAREAGKLLKEKGFRFDVVYTSVLKRAIKTAwivlEELGQLH 63
gpmA PRK14117
phosphoglyceromutase; Provisional
 30-91 2.16e-03

phosphoglyceromutase; Provisional


Pssm-ID: 184517  Cd Length: 230  Bit Score: 35.39  E-value: 2.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380807051  30 RHGESELNLKGRIGG--DPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQT-------AEALGVP 91
Cdd:PRK14117   8 RHGESEWNKANLFTGwaDVDLSEKGTQQAIDAGKLIKEAGIEFDLAFTSVLKRAIKTtnlaleaSDQLWVP 78
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 26-89 2.21e-03

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 34.81  E-value: 2.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380807051   26 IYLCRHGESELnlKGRIGGDPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTAEALG 89
Cdd:TIGR00249   3 LFIMRHGDAAL--DAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVG 64
 
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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