NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1232914429|gb|OZB19991.1|]
View 

phosphoglycerate mutase [Rhodobacterales bacterium 34-62-10]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
5-159 1.48e-51

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


:

Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 161.58  E-value: 1.48e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429   5 LILMRHAKSDWGNPGLADHDRPLHARGAGDAPAMGAWLRAKGYVPDEVLCSTATRTRQTLA----GLGLTAPTQFIPALY 80
Cdd:COG2062     1 LILVRHAKAEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEilaeALGLPPKVEVEDELY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429  81 HADPDSMFDVLRR-ATGRCVLMVGHNPGIAAFAAELLAQAPshtrFHDYPTSATLVARFgieDWADLRPGTGQAQDFIIP 159
Cdd:COG2062    81 DADPEDLLDLLRElDDGETVLLVGHNPGLSELAALLAGGEP----LDGFPTGGLAVLEF---DIDDLGPGKGRLVWFLTP 153
 
Name Accession Description Interval E-value
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
5-159 1.48e-51

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 161.58  E-value: 1.48e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429   5 LILMRHAKSDWGNPGLADHDRPLHARGAGDAPAMGAWLRAKGYVPDEVLCSTATRTRQTLA----GLGLTAPTQFIPALY 80
Cdd:COG2062     1 LILVRHAKAEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEilaeALGLPPKVEVEDELY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429  81 HADPDSMFDVLRR-ATGRCVLMVGHNPGIAAFAAELLAQAPshtrFHDYPTSATLVARFgieDWADLRPGTGQAQDFIIP 159
Cdd:COG2062    81 DADPEDLLDLLRElDDGETVLLVGHNPGLSELAALLAGGEP----LDGFPTGGLAVLEF---DIDDLGPGKGRLVWFLTP 153
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 4-135 1.47e-22

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: 87.38  E-value: 1.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429   4 TLILMRHAKSDW--GNPGLADHDRPLHARGAGDAPAMGAWLRAKGYVPDEVLCSTATRTRQTLAGLG---LTAPTQFIPA 78
Cdd:cd07067     1 RLYLVRHGESEWnaEGRFQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILeelPGLPVEVDPR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1232914429  79 LYHADPDSMF-DVLRRATGRCVLMVGHNPGIAAFAAELLAQAPSHTRFHDYPTSATLV 135
Cdd:cd07067    81 LREARVLPALeELIAPHDGKNVLIVSHGGVLRALLAYLLGLSDEDILRLNLPNGSISV 138
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 5-116 7.62e-09

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 51.76  E-value: 7.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429   5 LILMRHAKSDWGNPglADHDRPLHARGAGDAPAMGAWLRAKGYVPDEVLCSTATRTRQTLAGLG--LTAPTQF--IPALY 80
Cdd:TIGR00249   3 LFIMRHGDAALDAA--SDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGdcLNLPSSAevLEGLT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1232914429  81 -HADPDSMFD---VLRRATGRCVLMVGHNPGIAAFAAELL 116
Cdd:TIGR00249  81 pCGDIGLVSDyleALTNEGVASVLLVSHLPLVGYLVAELC 120
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 4-70 1.84e-08

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: 50.54  E-value: 1.84e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429    4 TLILMRHAKSDW--GNPGLADHDRPLHARGAGDAPAMGAWLRA-KGYVPDEVLCSTATRTRQTLAGLGLT 70
Cdd:smart00855   1 RLYLIRHGETEWnrEGRLYGDTDVPLTELGRAQAEALGRLLASlLLPRFDVVYSSPLKRARQTAEALAIA 70
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 1-64 6.09e-07

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 46.99  E-value: 6.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1232914429   1 MTRTLILMRHAKSDWG--N--PGLADHDrpLHARGAGDAPAMGAWLRAKGYVPDEVLCSTATRTRQTL 64
Cdd:PRK01295    1 MSRTLVLVRHGQSEWNlkNlfTGWRDPD--LTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTC 66
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 5-145 5.30e-03

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: 35.65  E-value: 5.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429   5 LILMRHAKSDWGNPGLA--DHDRPLHARGAGDAPAMGAWLRAKGyvPDEVLCSTATRTRQT--LAGLGLTAPTQFIPAL- 79
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFqgRTDSPLTELGREQAEALAERLAGEP--FDAIYSSPLKRARQTaeIIAEALGLPVEIDPRLr 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429  80 -------------------------YHADPD--------SMFDVLRRAT-----------GRCVLMVGHNPGIAAFAAEL 115
Cdd:pfam00300  79 eidfgdwegltfeeiaerypeeydaWLADPAdyrppggeSLADVRARVRaaleelaarhpGKTVLVVSHGGVIRALLAHL 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1232914429 116 LAQAPSH-TRFHDYPTSATLV----ARFGIEDWAD 145
Cdd:pfam00300 159 LGLPLEAlRRFPLDNASLSILefdgGGWVLVLLND 193
 
Name Accession Description Interval E-value
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
5-159 1.48e-51

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 161.58  E-value: 1.48e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429   5 LILMRHAKSDWGNPGLADHDRPLHARGAGDAPAMGAWLRAKGYVPDEVLCSTATRTRQTLA----GLGLTAPTQFIPALY 80
Cdd:COG2062     1 LILVRHAKAEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEilaeALGLPPKVEVEDELY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429  81 HADPDSMFDVLRR-ATGRCVLMVGHNPGIAAFAAELLAQAPshtrFHDYPTSATLVARFgieDWADLRPGTGQAQDFIIP 159
Cdd:COG2062    81 DADPEDLLDLLRElDDGETVLLVGHNPGLSELAALLAGGEP----LDGFPTGGLAVLEF---DIDDLGPGKGRLVWFLTP 153
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 4-135 1.47e-22

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: 87.38  E-value: 1.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429   4 TLILMRHAKSDW--GNPGLADHDRPLHARGAGDAPAMGAWLRAKGYVPDEVLCSTATRTRQTLAGLG---LTAPTQFIPA 78
Cdd:cd07067     1 RLYLVRHGESEWnaEGRFQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILeelPGLPVEVDPR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1232914429  79 LYHADPDSMF-DVLRRATGRCVLMVGHNPGIAAFAAELLAQAPSHTRFHDYPTSATLV 135
Cdd:cd07067    81 LREARVLPALeELIAPHDGKNVLIVSHGGVLRALLAYLLGLSDEDILRLNLPNGSISV 138
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 4-150 7.29e-17

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: 72.83  E-value: 7.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429   4 TLILMRHAKSDW--GNPGLADHDRPLHARGAGDAPAMGAWLRAKGYVPDEVLCSTATRTRQTLAGLgltAPTQFIPALYH 81
Cdd:cd07040     1 VLYLVRHGEREPnaEGRFTGWGDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEII---LEGLFEGLPVE 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1232914429  82 ADPDS-----MFDVLRRA--TGRCVLMVGHNPGIAAFAAELLAQAPSHTRFHDYPTSATLVarfgIEDWADLRPGT 150
Cdd:cd07040    78 VDPRArvlnaLLELLARHllDGKNVLIVSHGGTIRALLAALLGLSDEEILSLNLPNGSILV----LELDECGGKYV 149
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
2-135 6.22e-09

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 52.64  E-value: 6.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429   2 TRTLILMRHAKSDWGNPGLA--DHDRPLHARGAGDAPAMGAWLRakGYVPDEVLCSTATRTRQTLAGLG--LTAPTQFIP 77
Cdd:COG0406     1 MTRLYLVRHGETEWNAEGRLqgRLDVPLTELGRAQARALAERLA--DIPFDAVYSSPLQRARQTAEALAeaLGLPVEVDP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429  78 AL--------------------------YHADPD--------SMFDVLRRAT-----------GRCVLMVGHNPGIAAFA 112
Cdd:COG0406    79 RLreidfgdwegltfaelearypealaaWLADPAefrppggeSLADVQARVRaaleellarhpGGTVLVVTHGGVIRALL 158

                         170       180
                  ....*....|....*....|....
gi 1232914429 113 AELLAQAPSHT-RFHDYPTSATLV 135
Cdd:COG0406   159 AHLLGLPLEAFwRLRIDNASVTVL 182
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 5-116 7.62e-09

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 51.76  E-value: 7.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429   5 LILMRHAKSDWGNPglADHDRPLHARGAGDAPAMGAWLRAKGYVPDEVLCSTATRTRQTLAGLG--LTAPTQF--IPALY 80
Cdd:TIGR00249   3 LFIMRHGDAALDAA--SDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGdcLNLPSSAevLEGLT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1232914429  81 -HADPDSMFD---VLRRATGRCVLMVGHNPGIAAFAAELL 116
Cdd:TIGR00249  81 pCGDIGLVSDyleALTNEGVASVLLVSHLPLVGYLVAELC 120
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 4-70 1.84e-08

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: 50.54  E-value: 1.84e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429    4 TLILMRHAKSDW--GNPGLADHDRPLHARGAGDAPAMGAWLRA-KGYVPDEVLCSTATRTRQTLAGLGLT 70
Cdd:smart00855   1 RLYLIRHGETEWnrEGRLYGDTDVPLTELGRAQAEALGRLLASlLLPRFDVVYSSPLKRARQTAEALAIA 70
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 1-64 6.09e-07

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 46.99  E-value: 6.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1232914429   1 MTRTLILMRHAKSDWG--N--PGLADHDrpLHARGAGDAPAMGAWLRAKGYVPDEVLCSTATRTRQTL 64
Cdd:PRK01295    1 MSRTLVLVRHGQSEWNlkNlfTGWRDPD--LTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTC 66
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 4-64 7.58e-05

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: 41.22  E-value: 7.58e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1232914429   4 TLILMRHAKSDWgNpgLAD-----HDRPLHARGAGDAPAMGAWLRAKGYVPDEVLCSTATRTRQTL 64
Cdd:COG0588     2 KLVLLRHGESEW-N--LENrftgwTDVDLSEKGRAEAKRAGRLLKEAGFLFDVAYTSVLKRAIRTL 64
gpmA PRK14120
phosphoglyceromutase; Provisional
 1-71 1.51e-04

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 40.41  E-value: 1.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232914429   1 MTRTLILMRHAKSDWGNPGLADH--DRPLHARGAGDAPAMGAWLRAKGYVPDEVLCSTATRTRQTlAGLGLTA 71
Cdd:PRK14120    3 MTYTLVLLRHGESEWNAKNLFTGwvDVDLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRT-ANLALDA 74
pgm_1 TIGR01258
phosphoglycerate mutase, BPG-dependent, family 1; Most members of this family are ...
 5-64 2.02e-03

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: 37.39  E-value: 2.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1232914429   5 LILMRHAKSDWGNPGLAD--HDRPLHARGAGDAPAMGAWLRAKGYVPDEVLCSTATRTRQTL 64
Cdd:TIGR01258   3 LVLVRHGESEWNALNLFTgwVDVKLSEKGQQEAKRAGELLKEEGYEFDVAYTSLLKRAIHTL 64
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 5-145 5.30e-03

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: 35.65  E-value: 5.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429   5 LILMRHAKSDWGNPGLA--DHDRPLHARGAGDAPAMGAWLRAKGyvPDEVLCSTATRTRQT--LAGLGLTAPTQFIPAL- 79
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFqgRTDSPLTELGREQAEALAERLAGEP--FDAIYSSPLKRARQTaeIIAEALGLPVEIDPRLr 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429  80 -------------------------YHADPD--------SMFDVLRRAT-----------GRCVLMVGHNPGIAAFAAEL 115
Cdd:pfam00300  79 eidfgdwegltfeeiaerypeeydaWLADPAdyrppggeSLADVRARVRaaleelaarhpGKTVLVVSHGGVIRALLAHL 158

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1232914429 116 LAQAPSH-TRFHDYPTSATLV----ARFGIEDWAD 145
Cdd:pfam00300 159 LGLPLEAlRRFPLDNASLSILefdgGGWVLVLLND 193
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
5-79 6.20e-03

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 35.80  E-value: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232914429   5 LILMRHAKSDWGNPGL--ADHDRPLHARGAGDAPAMGAWLRAkgyVP-DEVLCSTATRTRQT----LAGLGLTAPTqfIP 77
Cdd:PRK15004    3 LWLVRHGETQANVDGLysGHAPTPLTARGIEQAQNLHTLLRD---VPfDLVLCSELERAQHTarlvLSDRQLPVHI--IP 77


                  ..
gi 1232914429  78 AL 79
Cdd:PRK15004   78 EL 79
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH