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Conserved domains on  [gi|521289750|ref|WP_020454018|]
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MULTISPECIES: acid phosphatase PhoC [Enterobacteriaceae]

Protein Classification

acid phosphatase( domain architecture ID 10130290)

acid phosphatase belonging to the phosphatase PAP2 family catalyzes phosphomonoester hydrolysis to yield alcohol and phosphate

CATH:  1.20.144.10
EC:  3.1.3.2
Gene Ontology:  GO:0003993|GO:0016311
PubMed:  12447906|9260289
SCOP:  4001226

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PAP2_acid_phosphatase cd03397
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes ...
10-244 1.07e-94

PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes catalyze phosphomonoester hydrolysis, with optimal activity in low pH conditions. They are secreted into the periplasmic space, and their physiological role remains to be determined.


:

Pssm-ID: 239491  Cd Length: 232  Bit Score: 277.29  E-value: 1.07e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750  10 LASLLSTSAFALVPSGNDATTKPDLYYLKNAQA-IDSLALLPPPPEVGSIAFLNDQAMYEQGRLLRNTERGKQAAEDANL 88
Cdd:cd03397    2 LLLSAGAPASQQPAPSATIRALPASGYLPPVGAtPDSLDLLPPPPAAGSAAFAADLAAYLAARALRGTPRWALATTDADL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750  89 SSGGVANAFSGAFGspitEKDSPQLHKLLTNMIEDAGDlATRGAKQKYMRIRPFAFYGVPTCNTKEQDSLAKNGSYPSGH 168
Cdd:cd03397   82 SFPGAANAFSCALG----EERTPELYRLLRRVLEDAGS-ATYPAKKYYNRPRPFVLNDEPICTPPDESGLAKDGSYPSGH 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521289750 169 TSIGWATALVLAEINPQRQDQILKRGYDLGQSRVICGYHWQSDVDAARIVGSAVVATLHTNPAFQQQLQKAKDEFA 244
Cdd:cd03397  157 TAAGYAWALILAELVPERADEILARGSEYGQSRIVCGVHWPSDVMGGRIMAAALVAALLADPAFAADLAAARAELR 232
 
Name Accession Description Interval E-value
PAP2_acid_phosphatase cd03397
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes ...
10-244 1.07e-94

PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes catalyze phosphomonoester hydrolysis, with optimal activity in low pH conditions. They are secreted into the periplasmic space, and their physiological role remains to be determined.


Pssm-ID: 239491  Cd Length: 232  Bit Score: 277.29  E-value: 1.07e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750  10 LASLLSTSAFALVPSGNDATTKPDLYYLKNAQA-IDSLALLPPPPEVGSIAFLNDQAMYEQGRLLRNTERGKQAAEDANL 88
Cdd:cd03397    2 LLLSAGAPASQQPAPSATIRALPASGYLPPVGAtPDSLDLLPPPPAAGSAAFAADLAAYLAARALRGTPRWALATTDADL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750  89 SSGGVANAFSGAFGspitEKDSPQLHKLLTNMIEDAGDlATRGAKQKYMRIRPFAFYGVPTCNTKEQDSLAKNGSYPSGH 168
Cdd:cd03397   82 SFPGAANAFSCALG----EERTPELYRLLRRVLEDAGS-ATYPAKKYYNRPRPFVLNDEPICTPPDESGLAKDGSYPSGH 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521289750 169 TSIGWATALVLAEINPQRQDQILKRGYDLGQSRVICGYHWQSDVDAARIVGSAVVATLHTNPAFQQQLQKAKDEFA 244
Cdd:cd03397  157 TAAGYAWALILAELVPERADEILARGSEYGQSRIVCGVHWPSDVMGGRIMAAALVAALLADPAFAADLAAARAELR 232
acidPPc smart00014
Acid phosphatase homologues;
119-227 2.66e-31

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 111.67  E-value: 2.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750   119 NMIEDAGDLATRGAKQKYMRIRPFAFY-GVPTCNTKEQDSLAKNGSYPSGHTSIGWATALVLAEINPQRQDQ------IL 191
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFLSiGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGRklliflLL 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 521289750   192 KRGYDLGQSRVICGYHWQSDVDAARIVGSAVVATLH 227
Cdd:smart00014  81 LLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
127-227 1.62e-19

Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; Membrane-associated phospholipid phosphatase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 440435 [Multi-domain]  Cd Length: 189  Bit Score: 83.17  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750 127 LATRGAKQKYMRIRPFAFYGVptcntKEQDSLAKNGSYPSGHTSIGWATALVLAEINPQR--QDQILKRGYDLGQSRVIC 204
Cdd:COG0671   87 LLLLLLKYLFGRPRPFVVPDL-----ELLLGTAGGYSFPSGHAAAAFALALVLALLLPRRwlAALLLALALLVGLSRVYL 161
                         90       100
                 ....*....|....*....|...
gi 521289750 205 GYHWQSDVDAARIVGSAVVATLH 227
Cdd:COG0671  162 GVHYPSDVLAGALLGLAIALLLL 184
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
116-224 1.07e-13

PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), Glucose-6-phosphatase EC:3.1.3.9, Phosphatidylglycerophosphatase B EC:3.1.3.27 and bacterial acid phosphatase EC:3.1.3.2. The family also includes a variety of haloperoxidases that function by oxidising halides in the presence of hydrogen peroxide to form the corresponding hypohalous acids.


Pssm-ID: 426329 [Multi-domain]  Cd Length: 124  Bit Score: 65.90  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750  116 LLTNMIedAGDLATRGAKQKYMRIRPFAFYGVPTCNTKEQDSLAKNGSYPSGHTSIGWATALVLAEINPQRQDQILKRGY 195
Cdd:pfam01569   2 LLLALA--LAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLA 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 521289750  196 DL--------GQSRVICGYHWQSDVDAARIVGSAVVA 224
Cdd:pfam01569  80 LLllvlallvGLSRLYLGVHFPSDVLAGALIGILLAL 116
 
Name Accession Description Interval E-value
PAP2_acid_phosphatase cd03397
PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes ...
10-244 1.07e-94

PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes catalyze phosphomonoester hydrolysis, with optimal activity in low pH conditions. They are secreted into the periplasmic space, and their physiological role remains to be determined.


Pssm-ID: 239491  Cd Length: 232  Bit Score: 277.29  E-value: 1.07e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750  10 LASLLSTSAFALVPSGNDATTKPDLYYLKNAQA-IDSLALLPPPPEVGSIAFLNDQAMYEQGRLLRNTERGKQAAEDANL 88
Cdd:cd03397    2 LLLSAGAPASQQPAPSATIRALPASGYLPPVGAtPDSLDLLPPPPAAGSAAFAADLAAYLAARALRGTPRWALATTDADL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750  89 SSGGVANAFSGAFGspitEKDSPQLHKLLTNMIEDAGDlATRGAKQKYMRIRPFAFYGVPTCNTKEQDSLAKNGSYPSGH 168
Cdd:cd03397   82 SFPGAANAFSCALG----EERTPELYRLLRRVLEDAGS-ATYPAKKYYNRPRPFVLNDEPICTPPDESGLAKDGSYPSGH 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521289750 169 TSIGWATALVLAEINPQRQDQILKRGYDLGQSRVICGYHWQSDVDAARIVGSAVVATLHTNPAFQQQLQKAKDEFA 244
Cdd:cd03397  157 TAAGYAWALILAELVPERADEILARGSEYGQSRIVCGVHWPSDVMGGRIMAAALVAALLADPAFAADLAAARAELR 232
PAP2_like_1 cd03380
PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium ...
49-228 2.88e-58

PAP2_like_1 proteins, a sub-family of PAP2, containing bacterial acid phosphatase, vanadium chloroperoxidases and vanadium bromoperoxidases.


Pssm-ID: 239475  Cd Length: 209  Bit Score: 183.79  E-value: 2.88e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750  49 LPPPPEVGSIAFLNDQAMYEQGRLL----RNTERGKQAAEDANLSS--GGVANAFSGAFGSP-ITEKDSPQLHKLLTNMI 121
Cdd:cd03380   23 LPPPPPALSAAYAADLAEVKALGALqstaRTTAQTALAAFDADGGDppPHYANAFSIALGTPgLSEERTPRLYALLARAL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750 122 EDAGdLATRGAKQKYMRIRPFAFYGV---PTCNTKEQdsLAKNGSYPSGHTSIGWATALVLAEINPQRQDQILKRGYDLG 198
Cdd:cd03380  103 TDAG-IATWDAKYHYNRPRPFVAIRLqwlPICTPEEG--TPKHPSYPSGHATFGGAAALVLAELFPERAAELLARAAEAG 179
                        170       180       190
                 ....*....|....*....|....*....|
gi 521289750 199 QSRVICGYHWQSDVDAARIVGSAVVATLHT 228
Cdd:cd03380  180 NSRVVAGVHWPSDVEAGRILGEAIAAALLA 209
acidPPc smart00014
Acid phosphatase homologues;
119-227 2.66e-31

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 111.67  E-value: 2.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750   119 NMIEDAGDLATRGAKQKYMRIRPFAFY-GVPTCNTKEQDSLAKNGSYPSGHTSIGWATALVLAEINPQRQDQ------IL 191
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFLSiGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPARAGRklliflLL 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 521289750   192 KRGYDLGQSRVICGYHWQSDVDAARIVGSAVVATLH 227
Cdd:smart00014  81 LLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVLF 116
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
127-227 1.62e-19

Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; Membrane-associated phospholipid phosphatase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 440435 [Multi-domain]  Cd Length: 189  Bit Score: 83.17  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750 127 LATRGAKQKYMRIRPFAFYGVptcntKEQDSLAKNGSYPSGHTSIGWATALVLAEINPQR--QDQILKRGYDLGQSRVIC 204
Cdd:COG0671   87 LLLLLLKYLFGRPRPFVVPDL-----ELLLGTAGGYSFPSGHAAAAFALALVLALLLPRRwlAALLLALALLVGLSRVYL 161
                         90       100
                 ....*....|....*....|...
gi 521289750 205 GYHWQSDVDAARIVGSAVVATLH 227
Cdd:COG0671  162 GVHYPSDVLAGALLGLAIALLLL 184
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
111-227 3.90e-19

PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, includes type 2 phosphatidic acid phosphatase or lipid phosphate phosphatase (LPP), Glucose-6-phosphatase, Phosphatidylglycerophosphatase B and bacterial acid phosphatase, vanadium chloroperoxidases, vanadium bromoperoxidases, and several other mostly uncharacterized subfamilies. Several members of this superfamily have been predicted to be transmembrane proteins.


Pssm-ID: 238813 [Multi-domain]  Cd Length: 122  Bit Score: 80.20  E-value: 3.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750 111 PQLHKLLTNMIEDAGDLATRGAKQKYMRIRPFAFYGVPTCNTKEQdSLAKNGSYPSGHTSIGWATALVLAEINPQRQDQ- 189
Cdd:cd01610    1 RRLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDGDPLL-LTEGGYSFPSGHAAFAFALALFLALLLPRRLLRl 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 521289750 190 -----ILKRGYDLGQSRVICGYHWQSDVDAARIVGSAVVATLH 227
Cdd:cd01610   80 llgllLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
116-224 1.07e-13

PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), Glucose-6-phosphatase EC:3.1.3.9, Phosphatidylglycerophosphatase B EC:3.1.3.27 and bacterial acid phosphatase EC:3.1.3.2. The family also includes a variety of haloperoxidases that function by oxidising halides in the presence of hydrogen peroxide to form the corresponding hypohalous acids.


Pssm-ID: 426329 [Multi-domain]  Cd Length: 124  Bit Score: 65.90  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750  116 LLTNMIedAGDLATRGAKQKYMRIRPFAFYGVPTCNTKEQDSLAKNGSYPSGHTSIGWATALVLAEINPQRQDQILKRGY 195
Cdd:pfam01569   2 LLLALA--LAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLPGLGYSFPSGHSATAFALALLLALLLRRLRKIVRVLLA 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 521289750  196 DL--------GQSRVICGYHWQSDVDAARIVGSAVVA 224
Cdd:pfam01569  80 LLllvlallvGLSRLYLGVHFPSDVLAGALIGILLAL 116
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
116-224 8.13e-06

PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.


Pssm-ID: 239486  Cd Length: 182  Bit Score: 44.91  E-value: 8.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750 116 LLTNMIedAGDLATRGAKQKYMRIRPFAFYGVPtcntkeqdslAKNGSYPSGHTSIGWATALVLAE-INPQRQDQILKRG 194
Cdd:cd03392   67 LLLALL--GGGALNTLLKLLVQRPRPPLHLLVP----------EGGYSFPSGHAMGATVLYGFLAYlLARRLPRRRVRIL 134
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 521289750 195 YDL---------GQSRVICGYHWQSDVDAARIVGSAVVA 224
Cdd:cd03392  135 LLIlaailillvGLSRLYLGVHYPSDVLAGWLLGLAWLA 173
PAP2_haloperoxidase cd03398
PAP2, haloperoxidase_like subfamily. Haloperoxidases catalyze the oxidation of halides such as ...
50-222 3.75e-05

PAP2, haloperoxidase_like subfamily. Haloperoxidases catalyze the oxidation of halides such as bromide or chloride by hydrogen peroxide, which results in subsequent halogenation of organic substrates, or halide-assisted disproportionation of hydrogen peroxide forming dioxygen. They are likely to participate in the biosynthesis of halogenated natural products, such as volatile halogenated hydrocarbons, chiral halogenated terpenes, acetogenins and indoles.


Pssm-ID: 239492  Cd Length: 232  Bit Score: 43.56  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750  50 PPPPEVGSIAFLNDQA-MYEQGrLLRNTERGKQAAEDANLSSGG---------VANAFSGAFGSPITEkdSPQLHKLLTN 119
Cdd:cd03398   17 PPPPALGSAEYAAQLAeVKTLG-GARSTSRTARQTAIAAFWADGptppghwnqIARILAARPGLSLFR--TARLFAAVNA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750 120 MIEDAGdLATRGAKQKYMRIRPFAFYGVPTCNTKEQDSLAKN----------GSYPSGHTSIGWATALVLAEINPQRQ-- 187
Cdd:cd03398   94 AMTDAG-IAAWDAKYHYRRWRPVTAIRLADTDGNPATEADPYwlplagtpphPSYPSGHATFAGAAATVLKALFGSDKvp 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 521289750 188 -------------------DQILKRGYDLGQSRVICGYHWQSDVDAARIVGSAV 222
Cdd:cd03398  173 dtvsepdeggpstgvtrvwAELNELADEVAISRVYAGVHFRSDDAAGAALGEQI 226
PAP2_like_5 cd03394
PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
127-219 5.95e-05

PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.


Pssm-ID: 239488 [Multi-domain]  Cd Length: 106  Bit Score: 41.16  E-value: 5.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289750 127 LATRGAKQKYMRIRPFafygvptcntkeqDSLAKNGSYPSGHTSIGWATALVLAEINPQRQDQILkrGYDL----GQSRV 202
Cdd:cd03394   17 AVTEGLKFAVGRARPD-------------GSNNGYRSFPSGHTASAFAAATFLQYRYGWRWYGIP--AYALaslvGASRV 81
                         90
                 ....*....|....*..
gi 521289750 203 ICGYHWQSDVDAARIVG 219
Cdd:cd03394   82 VANRHWLSDVLAGAAIG 98
PAP2_lipid_A_1_phosphatase cd03389
PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from ...
163-226 2.25e-04

PAP2_like proteins, Lipid A 1-phosphatase subfamily. Lipid A 1-phosphatase, or LpxE from Francisella novicida selectively dephosphorylates lipid A at the 1-position. Lipid A is the membrane-anchor component of lipopolysaccharides (LPS), the major constituents of the outer membrane in many gram-negative bacteria.


Pssm-ID: 239483  Cd Length: 186  Bit Score: 40.77  E-value: 2.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521289750 163 SYPSGHTSIGWATALVLAEINPQRQDQILKRGYDLGQSRVICGYHWQSDVDAARIVGSAVVATL 226
Cdd:cd03389  119 SFPSGHSATAGAAAAALALLFPRYRWAFILLALLIAFSRVIVGAHYPSDVIAGSLLGAVTALAL 182
 
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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