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Conserved domains on  [gi|60593626|pdb|1UJB|A]
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Chain A, Phosphohistidine phosphatase sixA

Protein Classification

phosphohistidine phosphatase SixA( domain architecture ID 10794488)

phosphohistidine phosphatase SixA exhibits phosphohistidine phosphatase activity towards the HPt domain of the ArcB sensor involved in the multistep His-Asp phosphorelay

CATH:  3.40.50.1240
EC:  3.1.3.-
Gene Ontology:  GO:0101006|GO:0035971
PubMed:  18092946
SCOP:  3000781

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 1-152 3.89e-90

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


:

Pssm-ID: 129351  Cd Length: 152  Bit Score: 259.00  E-value: 3.89e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UJB_A          1 MQVFIMRHGDAALDAASDSVRPLTTNGCDESRLMANWLKGQKVEIERVLVSPFLRAEQTLEEVGDCLNLPSSAEVLPELT 80
Cdd:TIGR00249   1 MQLFIMRHGDAALDAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGDCLNLPSSAEVLEGLT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1UJB_A         81 PCGDVGLVSAYLQALTNEGVASVLVISHLPLVGYLVAELCPGETPPMFTTSAIASVTLDESGNGTFNWQMSP 152
Cdd:TIGR00249  81 PCGDIGLVSDYLEALTNEGVASVLLVSHLPLVGYLVAELCPGENPIMFTTGAIASLLWDESKNGTLNWQMSP 152
 
Name Accession Description Interval E-value
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 1-152 3.89e-90

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 259.00  E-value: 3.89e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UJB_A          1 MQVFIMRHGDAALDAASDSVRPLTTNGCDESRLMANWLKGQKVEIERVLVSPFLRAEQTLEEVGDCLNLPSSAEVLPELT 80
Cdd:TIGR00249   1 MQLFIMRHGDAALDAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGDCLNLPSSAEVLEGLT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1UJB_A         81 PCGDVGLVSAYLQALTNEGVASVLVISHLPLVGYLVAELCPGETPPMFTTSAIASVTLDESGNGTFNWQMSP 152
Cdd:TIGR00249  81 PCGDIGLVSDYLEALTNEGVASVLLVSHLPLVGYLVAELCPGENPIMFTTGAIASLLWDESKNGTLNWQMSP 152
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
3-152 9.03e-45

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 144.25  E-value: 9.03e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UJB_A        3 VFIMRHGDAALDAA--SDSVRPLTTNGCDESRLMANWLKGQKVEIERVLVSPFLRAEQTLEEVGDCLNLPSSAEVLPELT 80
Cdd:COG2062   1 LILVRHAKAEWRAPggDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLPPKVEVEDELY 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1UJB_A       81 PcGDVGLVSAYLQALtnEGVASVLVISHLPLVGYLVAELCPGETPPMFTTSAIASVTLD----ESGNGTFNWQMSP 152
Cdd:COG2062  81 D-ADPEDLLDLLREL--DDGETVLLVGHNPGLSELAALLAGGEPLDGFPTGGLAVLEFDiddlGPGKGRLVWFLTP 153
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 2-148 1.16e-20

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: 82.76  E-value: 1.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UJB_A        2 QVFIMRHGDAALDAA----SDSVRPLTTNGCDESRLMANWLKGQKVEIERVLVSPFLRAEQTLEEVGDCLNLPsSAEVLP 77
Cdd:cd07067   1 RLYLVRHGESEWNAEgrfqGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGL-PVEVDP 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1UJB_A       78 ELTPCGdvglVSAYLQALTNE-GVASVLVISHLPLVGYLVAELCPGETPPM----FTTSAIASVTLDESGNGTFNW 148
Cdd:cd07067  80 RLREAR----VLPALEELIAPhDGKNVLIVSHGGVLRALLAYLLGLSDEDIlrlnLPNGSISVLELDENGGGVLLL 151
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 2-70 2.48e-07

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: 47.46  E-value: 2.48e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1UJB_A           2 QVFIMRHG------DAALDAASDSvrPLTTNGCDESRLMANWLKGQK-VEIERVLVSPFLRAEQTLEEVGDCLNLP 70
Cdd:smart00855   1 RLYLIRHGetewnrEGRLYGDTDV--PLTELGRAQAEALGRLLASLLlPRFDVVYSSPLKRARQTAEALAIALGLP 74
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 3-79 3.24e-07

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: 47.59  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UJB_A          3 VFIMRHGDAALDAA------SDSvrPLTTNGCDESRLMANWLKGqkVEIERVLVSPFLRAEQTLEEVGDCLNLPssAEVL 76
Cdd:pfam00300   1 LYLVRHGETEWNLEgrfqgrTDS--PLTELGREQAEALAERLAG--EPFDAIYSSPLKRARQTAEIIAEALGLP--VEID 74


                  ...
1UJB_A         77 PEL 79
Cdd:pfam00300  75 PRL 77
 
Name Accession Description Interval E-value
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 1-152 3.89e-90

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 259.00  E-value: 3.89e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UJB_A          1 MQVFIMRHGDAALDAASDSVRPLTTNGCDESRLMANWLKGQKVEIERVLVSPFLRAEQTLEEVGDCLNLPSSAEVLPELT 80
Cdd:TIGR00249   1 MQLFIMRHGDAALDAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGDCLNLPSSAEVLEGLT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1UJB_A         81 PCGDVGLVSAYLQALTNEGVASVLVISHLPLVGYLVAELCPGETPPMFTTSAIASVTLDESGNGTFNWQMSP 152
Cdd:TIGR00249  81 PCGDIGLVSDYLEALTNEGVASVLLVSHLPLVGYLVAELCPGENPIMFTTGAIASLLWDESKNGTLNWQMSP 152
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
3-152 9.03e-45

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 144.25  E-value: 9.03e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UJB_A        3 VFIMRHGDAALDAA--SDSVRPLTTNGCDESRLMANWLKGQKVEIERVLVSPFLRAEQTLEEVGDCLNLPSSAEVLPELT 80
Cdd:COG2062   1 LILVRHAKAEWRAPggDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLPPKVEVEDELY 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1UJB_A       81 PcGDVGLVSAYLQALtnEGVASVLVISHLPLVGYLVAELCPGETPPMFTTSAIASVTLD----ESGNGTFNWQMSP 152
Cdd:COG2062  81 D-ADPEDLLDLLREL--DDGETVLLVGHNPGLSELAALLAGGEPLDGFPTGGLAVLEFDiddlGPGKGRLVWFLTP 153
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 2-148 1.16e-20

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: 82.76  E-value: 1.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UJB_A        2 QVFIMRHGDAALDAA----SDSVRPLTTNGCDESRLMANWLKGQKVEIERVLVSPFLRAEQTLEEVGDCLNLPsSAEVLP 77
Cdd:cd07067   1 RLYLVRHGESEWNAEgrfqGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGL-PVEVDP 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1UJB_A       78 ELTPCGdvglVSAYLQALTNE-GVASVLVISHLPLVGYLVAELCPGETPPM----FTTSAIASVTLDESGNGTFNW 148
Cdd:cd07067  80 RLREAR----VLPALEELIAPhDGKNVLIVSHGGVLRALLAYLLGLSDEDIlrlnLPNGSISVLELDENGGGVLLL 151
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 2-119 1.28e-14

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: 67.05  E-value: 1.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UJB_A        2 QVFIMRHGDAALDAA----SDSVRPLTTNGCDESRLMANWLKGQKVEIERVLVSPFLRAEQTLEEVGDCLNLPSSAEVLP 77
Cdd:cd07040   1 VLYLVRHGEREPNAEgrftGWGDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFEGLPVEVDP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
1UJB_A       78 EltpcgdVGLVSAYLQALTNE--GVASVLVISHLPLVGYLVAEL 119
Cdd:cd07040  81 R------ARVLNALLELLARHllDGKNVLIVSHGGTIRALLAAL 118
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-79 1.84e-10

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 56.49  E-value: 1.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UJB_A        1 MQVFIMRHGDAALDAA------SDSvrPLTTNGCDESRLMANWLKGqkVEIERVLVSPFLRAEQTLEEVGDCLNLPssAE 74
Cdd:COG0406   2 TRLYLVRHGETEWNAEgrlqgrLDV--PLTELGRAQARALAERLAD--IPFDAVYSSPLQRARQTAEALAEALGLP--VE 75


                ....*
1UJB_A       75 VLPEL 79
Cdd:COG0406  76 VDPRL 80
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 2-70 2.48e-07

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: 47.46  E-value: 2.48e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1UJB_A           2 QVFIMRHG------DAALDAASDSvrPLTTNGCDESRLMANWLKGQK-VEIERVLVSPFLRAEQTLEEVGDCLNLP 70
Cdd:smart00855   1 RLYLIRHGetewnrEGRLYGDTDV--PLTELGRAQAEALGRLLASLLlPRFDVVYSSPLKRARQTAEALAIALGLP 74
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 3-79 3.24e-07

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: 47.59  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1UJB_A          3 VFIMRHGDAALDAA------SDSvrPLTTNGCDESRLMANWLKGqkVEIERVLVSPFLRAEQTLEEVGDCLNLPssAEVL 76
Cdd:pfam00300   1 LYLVRHGETEWNLEgrfqgrTDS--PLTELGREQAEALAERLAG--EPFDAIYSSPLKRARQTAEIIAEALGLP--VEID 74


                  ...
1UJB_A         77 PEL 79
Cdd:pfam00300  75 PRL 77
 
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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