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Conserved domains on  [gi|503757806|ref|WP_013991882|]
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histidine phosphatase family protein [Zobellia galactanivorans]

Protein Classification

SixA phosphatase family protein( domain architecture ID 10788349)

SixA phosphatase family protein belongs to the histidine phosphatase superfamily, members of which contain a conserved His residue that is transiently phosphorylated during the catalytic cycle

CATH:  3.40.50.1240
EC:  3.1.3.-
Gene Ontology:  GO:0016791
PubMed:  18092946
SCOP:  3000781

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
4-141 1.17e-46

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


:

Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 148.87  E-value: 1.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806   4 LVLVRHGKSSWDYS-VGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMRQLGLPlAKVEVTDEL 82
Cdd:COG2062    1 LILVRHAKAEWRAPgGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLP-PKVEVEDEL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806  83 YDFSGESVFDFVEKLDDAlDSVLVFGHNHAFTYVANSL-GNTYIDNVSTSGLVHLDFNVD 141
Cdd:COG2062   80 YDADPEDLLDLLRELDDG-ETVLLVGHNPGLSELAALLaGGEPLDGFPTGGLAVLEFDID 138
 
Name Accession Description Interval E-value
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
4-141 1.17e-46

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 148.87  E-value: 1.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806   4 LVLVRHGKSSWDYS-VGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMRQLGLPlAKVEVTDEL 82
Cdd:COG2062    1 LILVRHAKAEWRAPgGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLP-PKVEVEDEL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806  83 YDFSGESVFDFVEKLDDAlDSVLVFGHNHAFTYVANSL-GNTYIDNVSTSGLVHLDFNVD 141
Cdd:COG2062   80 YDADPEDLLDLLRELDDG-ETVLLVGHNPGLSELAALLaGGEPLDGFPTGGLAVLEFDID 138
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-139 1.46e-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: 90.07  E-value: 1.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806   3 TLVLVRHGKSSWD---YSVGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMRqlGLPLAKVEVT 79
Cdd:cd07067    1 RLYLVRHGESEWNaegRFQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILE--ELPGLPVEVD 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503757806  80 DELYDfsgESVFDFVEKLDDALD--SVLVFGHNHAFTYVANSLGNTYID-----NVSTSGLVHLDFN 139
Cdd:cd07067   79 PRLRE---ARVLPALEELIAPHDgkNVLIVSHGGVLRALLAYLLGLSDEdilrlNLPNGSISVLELD 142
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-112 2.15e-13

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: 64.54  E-value: 2.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806    4 LVLVRHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKpqAVKIDKVFSSPANRALHTCMIFMRQLGLPlakVEVTD 80
Cdd:pfam00300   1 LYLVRHGETEWNLEgrfQGRTDSPLTELGREQAEALAERLA--GEPFDAIYSSPLKRARQTAEIIAEALGLP---VEIDP 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503757806   81 EL--YDF--------------------------------SGESVFDFVEKLDDALD---------SVLVFGHNHA 112
Cdd:pfam00300  76 RLreIDFgdwegltfeeiaerypeeydawladpadyrppGGESLADVRARVRAALEelaarhpgkTVLVVSHGGV 150
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 2-72 1.86e-11

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 59.70  E-value: 1.86e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503757806   2 KTLVLVRHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMRQLGLP 72
Cdd:PRK01295   3 RTLVLVRHGQSEWNLKnlfTGWRDPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCQLILEELGQP 76
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-112 5.43e-11

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: 57.47  E-value: 5.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806     3 TLVLVRHGKSSWD---YSVGDRDRPLQERGIRDALKVSSAFKPQ-AVKIDKVFSSPANRALHTCMIFMRQLGLPL----- 73
Cdd:smart00855   1 RLYLIRHGETEWNregRLYGDTDVPLTELGRAQAEALGRLLASLlLPRFDVVYSSPLKRARQTAEALAIALGLPGlrerd 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503757806    74 ------------------AKVEVTDELYDFS------GESVFDFVEKLDDALDS-----------VLVFGHNHA 112
Cdd:smart00855  81 fgawegltwdeiaakypeEYLAAWRDPYDPAppappgGESLADLVERVEPALDEliatadasgqnVLIVSHGGV 154
pgm_1 TIGR01258
phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are ...
 4-75 1.14e-07

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: 49.33  E-value: 1.14e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503757806    4 LVLVRHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMR---QLGLPLAK 75
Cdd:TIGR01258   3 LVLVRHGESEWNALnlfTGWVDVKLSEKGQQEAKRAGELLKEEGYEFDVAYTSLLKRAIHTLNIALDeldQLWIPVKK 80
 
Name Accession Description Interval E-value
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
4-141 1.17e-46

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 148.87  E-value: 1.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806   4 LVLVRHGKSSWDYS-VGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMRQLGLPlAKVEVTDEL 82
Cdd:COG2062    1 LILVRHAKAEWRAPgGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLP-PKVEVEDEL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806  83 YDFSGESVFDFVEKLDDAlDSVLVFGHNHAFTYVANSL-GNTYIDNVSTSGLVHLDFNVD 141
Cdd:COG2062   80 YDADPEDLLDLLRELDDG-ETVLLVGHNPGLSELAALLaGGEPLDGFPTGGLAVLEFDID 138
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-139 1.46e-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: 90.07  E-value: 1.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806   3 TLVLVRHGKSSWD---YSVGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMRqlGLPLAKVEVT 79
Cdd:cd07067    1 RLYLVRHGESEWNaegRFQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILE--ELPGLPVEVD 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503757806  80 DELYDfsgESVFDFVEKLDDALD--SVLVFGHNHAFTYVANSLGNTYID-----NVSTSGLVHLDFN 139
Cdd:cd07067   79 PRLRE---ARVLPALEELIAPHDgkNVLIVSHGGVLRALLAYLLGLSDEdilrlNLPNGSISVLELD 142
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 3-148 1.20e-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: 82.46  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806   3 TLVLVRHGKSSWDYSV---GDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMRQLGLPLaKVEVT 79
Cdd:cd07040    1 VLYLVRHGEREPNAEGrftGWGDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFEGL-PVEVD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503757806  80 DElydfsgESVFDFVEKL----DDALDSVLVFGHNHAFTYVANSLGNTYID-----NVSTSGLVHLDFNVDFWKSVQK 148
Cdd:cd07040   80 PR------ARVLNALLELlarhLLDGKNVLIVSHGGTIRALLAALLGLSDEeilslNLPNGSILVLELDECGGKYVRL 151
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-143 2.58e-17

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 74.98  E-value: 2.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806   1 MKTLVLVRHGKSSW---DYSVGDRDRPLQERGIRDALKVSSAFKpqAVKIDKVFSSPANRALHTCMIFMRQLGLPlakVE 77
Cdd:COG0406    1 MTRLYLVRHGETEWnaeGRLQGRLDVPLTELGRAQARALAERLA--DIPFDAVYSSPLQRARQTAEALAEALGLP---VE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806  78 VTDEL--YDF--------------------------------SGESVFDFVEKLDDALDS---------VLVFGHNHAFT 114
Cdd:COG0406   76 VDPRLreIDFgdwegltfaelearypealaawladpaefrppGGESLADVQARVRAALEEllarhpggtVLVVTHGGVIR 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 503757806 115 YVANSLGNTYIDN-----VSTSGLVHLDFNVDFW 143
Cdd:COG0406  156 ALLAHLLGLPLEAfwrlrIDNASVTVLEFDDGRW 189
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-112 2.15e-13

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: 64.54  E-value: 2.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806    4 LVLVRHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKpqAVKIDKVFSSPANRALHTCMIFMRQLGLPlakVEVTD 80
Cdd:pfam00300   1 LYLVRHGETEWNLEgrfQGRTDSPLTELGREQAEALAERLA--GEPFDAIYSSPLKRARQTAEIIAEALGLP---VEIDP 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503757806   81 EL--YDF--------------------------------SGESVFDFVEKLDDALD---------SVLVFGHNHA 112
Cdd:pfam00300  76 RLreIDFgdwegltfeeiaerypeeydawladpadyrppGGESLADVRARVRAALEelaarhpgkTVLVVSHGGV 150
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 2-72 1.86e-11

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 59.70  E-value: 1.86e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503757806   2 KTLVLVRHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMRQLGLP 72
Cdd:PRK01295   3 RTLVLVRHGQSEWNLKnlfTGWRDPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCQLILEELGQP 76
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-112 5.43e-11

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: 57.47  E-value: 5.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806     3 TLVLVRHGKSSWD---YSVGDRDRPLQERGIRDALKVSSAFKPQ-AVKIDKVFSSPANRALHTCMIFMRQLGLPL----- 73
Cdd:smart00855   1 RLYLIRHGETEWNregRLYGDTDVPLTELGRAQAEALGRLLASLlLPRFDVVYSSPLKRARQTAEALAIALGLPGlrerd 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503757806    74 ------------------AKVEVTDELYDFS------GESVFDFVEKLDDALDS-----------VLVFGHNHA 112
Cdd:smart00855  81 fgawegltwdeiaakypeEYLAAWRDPYDPAppappgGESLADLVERVEPALDEliatadasgqnVLIVSHGGV 154
PRK01112 PRK01112
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
1-68 1.48e-08

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 234902  Cd Length: 228  Bit Score: 51.64  E-value: 1.48e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503757806   1 MKTLVLVRHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKPqaVKIDKVFSSPANRALHTCMIFMRQ 68
Cdd:PRK01112   1 MALLILLRHGQSVWNAKnlfTGWVDIPLSQQGIAEAIAAGEKIKD--LPIDCIFTSTLVRSLMTALLAMTN 69
pgm_1 TIGR01258
phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are ...
 4-75 1.14e-07

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: 49.33  E-value: 1.14e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503757806    4 LVLVRHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMR---QLGLPLAK 75
Cdd:TIGR01258   3 LVLVRHGESEWNALnlfTGWVDVKLSEKGQQEAKRAGELLKEEGYEFDVAYTSLLKRAIHTLNIALDeldQLWIPVKK 80
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 4-109 2.34e-07

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: 48.00  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806    4 LVLVRHGKSSWDYSV--GDRDRPLQERGIRDALKVssAFKPQAVKIDKVFSSPANRALHTCMIFMRQLGLPLAKV----- 76
Cdd:TIGR03162   1 LYLIRHGETDVNAGLcyGQTDVPLAESGEEQAAAL--REKLADVPFDAVYSSPLSRCRELAEILAERRGLPIIKDdrlre 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503757806   77 ------------EVTDELYDFS-------------GESVFDFVEKLDDAL---------DSVLVFGH 109
Cdd:TIGR03162  79 mdfgdwegrswdEIPEAYPELDawaadwqharppgGESFADFYQRVSEFLeellkahegDNVLIVTH 145
gpmA PRK14118
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
4-75 2.88e-07

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172608  Cd Length: 227  Bit Score: 48.43  E-value: 2.88e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503757806   4 LVLVRHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMR---QLGLPLAK 75
Cdd:PRK14118   3 LVFIRHGFSEWNAKnlfTGWRDVNLTERGVEEAKAAGKKLKEAGYEFDIAFTSVLTRAIKTCNIVLEesnQLWIPQVK 80
gpmA PRK14119
phosphoglyceromutase; Provisional
 1-75 4.45e-07

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 47.58  E-value: 4.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806   1 MKTLVLVRHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMR---QLGLPLA 74
Cdd:PRK14119   1 MPKLILCRHGQSEWNAKnlfTGWEDVNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTTHYILTeskQQWIPVY 80


                 .
gi 503757806  75 K 75
Cdd:PRK14119  81 K 81
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
1-61 6.53e-07

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 47.22  E-value: 6.53e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503757806   1 MKTLVLVRHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHT 61
Cdd:PRK14116   1 MAKLVLIRHGQSEWNLSnqfTGWVDVDLSEKGVEEAKKAGRLIKEAGLEFDQAYTSVLTRAIKT 64
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
1-83 8.39e-06

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 43.89  E-value: 8.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806   1 MKtLVLVRHGKSSWD----YSvGDRDRPLQERGIRDALKVSSAFkpQAVKIDKVFSSPANRALHTCMIFMRQLGLPLAKV 76
Cdd:PRK15004   1 MR-LWLVRHGETQANvdglYS-GHAPTPLTARGIEQAQNLHTLL--RDVPFDLVLCSELERAQHTARLVLSDRQLPVHII 76


                 ....*..
gi 503757806  77 EVTDELY 83
Cdd:PRK15004  77 PELNEMF 83
PRK13463 PRK13463
phosphoserine phosphatase 1;
1-113 8.95e-06

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 43.88  E-value: 8.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806   1 MKTLVLV-RHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKPqaVKIDKVFSSPANRALHTCMIFMRQLGLPLakv 76
Cdd:PRK13463   1 MKTTVYVtRHGETEWNVAkrmQGRKNSALTENGILQAKQLGERMKD--LSIHAIYSSPSERTLHTAELIKGERDIPI--- 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 503757806  77 eVTDE-LYDFS-----GESVFDFVEKLDDalDSVLVFGHNHAF 113
Cdd:PRK13463  76 -IADEhFYEINmgiweGQTIDDIERQYPD--DIQLFWNEPHLF 115
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 2-72 9.00e-06

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: 43.92  E-value: 9.00e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503757806   2 KTLVLVRHGKSSWDYSvgDR-----DRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMRQLGLP 72
Cdd:COG0588    1 YKLVLLRHGESEWNLE--NRftgwtDVDLSEKGRAEAKRAGRLLKEAGFLFDVAYTSVLKRAIRTLWIVLDEMDRL 74
gpmA PRK14117
phosphoglyceromutase; Provisional
 1-75 1.85e-05

phosphoglyceromutase; Provisional


Pssm-ID: 184517  Cd Length: 230  Bit Score: 43.09  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806   1 MKTLVLVRHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMR---QLGLPLA 74
Cdd:PRK14117   1 MVKLVFARHGESEWNKAnlfTGWADVDLSEKGTQQAIDAGKLIKEAGIEFDLAFTSVLKRAIKTTNLALEasdQLWVPVE 80


                 .
gi 503757806  75 K 75
Cdd:PRK14117  81 K 81
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 3-85 3.54e-05

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 42.66  E-value: 3.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503757806   3 TLVLVRHGKS--SWD--YSvGDRDRPLQERGIRDALKVSSAFKPQAvKIDKVFSSPANRALHTCMIFMRQLGLPlakVEV 78
Cdd:PRK07238 173 RLLLLRHGQTelSVQrrYS-GRGNPELTEVGRRQAAAAARYLAARG-GIDAVVSSPLQRARDTAAAAAKALGLD---VTV 247


                 ....*....
gi 503757806  79 TDEL--YDF 85
Cdd:PRK07238 248 DDDLieTDF 256
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
2-71 1.29e-04

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 40.61  E-value: 1.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503757806   2 KTLVLVRHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHTCMIFMRQLGL 71
Cdd:PRK14115   1 TKLVLIRHGESQWNKEnrfTGWTDVDLSEKGVSEAKAAGKLLKEEGYTFDVAYTSVLKRAIRTLWIVLDELDQ 73
PRK06193 PRK06193
hypothetical protein; Provisional
 8-61 1.69e-04

hypothetical protein; Provisional


Pssm-ID: 235734  Cd Length: 206  Bit Score: 40.06  E-value: 1.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503757806   8 RHGKSSWDYSvgDRD----------RPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHT 61
Cdd:PRK06193  49 RHAATDRSQA--DQDtsdmddcstqRNLSEEGREQARAIGEAFRALAIPVGKVISSPYCRAWET 110
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
1-73 6.52e-04

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 38.56  E-value: 6.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503757806   1 MKTLVLVRHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKPQAvkIDKVFSSPANRALHTCMIFMRQLGLPL 73
Cdd:PRK03482   1 MLQVYLVRHGETQWNAErriQGQSDSPLTAKGEQQAMQVAERAKELG--ITHIISSDLGRTRRTAEIIAQACGCDI 74
gpmA PRK14120
phosphoglyceromutase; Provisional
 1-61 1.17e-03

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 38.10  E-value: 1.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503757806   1 MKTLVLVRHGKSSWDYS---VGDRDRPLQERGIRDALKVSSAFKPQAVKIDKVFSSPANRALHT 61
Cdd:PRK14120   4 TYTLVLLRHGESEWNAKnlfTGWVDVDLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRT 67
 
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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