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Conserved domains on  [gi|393537031|ref|NP_000142|]
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glucose-6-phosphatase catalytic subunit 1 isoform 1 [Homo sapiens]

Protein Classification

glucose-6-phosphatase( domain architecture ID 10130180)

glucose-6-phosphatase is a type 2 phosphatidic acid phosphatase (PAP2) family protein that catalyzes the hydrolysis of glucose-6-phosphate to glucose and phosphate

CATH:  1.20.144.10
EC:  3.1.3.9
Gene Ontology:  GO:0004346|GO:0016311|GO:0051156
PubMed:  12192101|11879177|9122162|12447906|9260289
SCOP:  3001110|4001226

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAP2_glucose_6_phosphatase cd03381
PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts ...
 42-280 2.32e-139

PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts glucose-6-phosphate into free glucose and is active in the lumen of the endoplasmic reticulum, where it is bound to the membrane. The generation of free glucose is an important control point in metabolism, and stands at the end of gluconeogenesis and the release of glucose from glycogen. Deficiency of glucose-6-phosphatase leads to von Gierke's disease.


:

Pssm-ID: 239476  Cd Length: 235  Bit Score: 395.21  E-value: 2.32e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031  42 AFYVLFPIWFHLQEAVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVLDTDYYSNTSVPLIKQFPVTCETGPGSPSGHAM 121
Cdd:cd03381    1 LFLIVFPLCGHLSQSVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVHETDYYSNSSVPKIEQFPLTCETGPGSPSGHAM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031 122 GTAGVYYVMVTSTLSIFQGKIkptyRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVVAGVLSGIAVAETFSHIHSI 201
Cdd:cd03381   81 GTTAVLLVMVTALLSHLAGRK----RSRFLRVMLWLVFWGVQLAVCLSRIYLAAHFPHQVIAGVISGIAVAETFSHIRYI 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 393537031 202 YNASLKKYFLITFFLFSFAIGFYLLLKGLGVDLLWTLEKAQRWCEQPEWVHIDTTPFASLLKNLGTLFGLGLALNSSMY 280
Cdd:cd03381  157 YSASLKRYVLITFFLFGFALGFYLLLKWLGVDLLWSLEKAFKWCERPEWVHIDTTPFASLLRNLGTLLGLGLALNSSMY 235
 
Name Accession Description Interval E-value
PAP2_glucose_6_phosphatase cd03381
PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts ...
 42-280 2.32e-139

PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts glucose-6-phosphate into free glucose and is active in the lumen of the endoplasmic reticulum, where it is bound to the membrane. The generation of free glucose is an important control point in metabolism, and stands at the end of gluconeogenesis and the release of glucose from glycogen. Deficiency of glucose-6-phosphatase leads to von Gierke's disease.


Pssm-ID: 239476  Cd Length: 235  Bit Score: 395.21  E-value: 2.32e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031  42 AFYVLFPIWFHLQEAVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVLDTDYYSNTSVPLIKQFPVTCETGPGSPSGHAM 121
Cdd:cd03381    1 LFLIVFPLCGHLSQSVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVHETDYYSNSSVPKIEQFPLTCETGPGSPSGHAM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031 122 GTAGVYYVMVTSTLSIFQGKIkptyRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVVAGVLSGIAVAETFSHIHSI 201
Cdd:cd03381   81 GTTAVLLVMVTALLSHLAGRK----RSRFLRVMLWLVFWGVQLAVCLSRIYLAAHFPHQVIAGVISGIAVAETFSHIRYI 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 393537031 202 YNASLKKYFLITFFLFSFAIGFYLLLKGLGVDLLWTLEKAQRWCEQPEWVHIDTTPFASLLKNLGTLFGLGLALNSSMY 280
Cdd:cd03381  157 YSASLKRYVLITFFLFGFALGFYLLLKWLGVDLLWSLEKAFKWCERPEWVHIDTTPFASLLRNLGTLLGLGLALNSSMY 235
acidPPc smart00014
Acid phosphatase homologues;
62-195 5.83e-23

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 92.41  E-value: 5.83e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031    62 LWVAVIGDWLNLVFKWILFGQRPYWWvldtdyySNTSVPLIKQFPVTCETGPGSPSGHAMGTAGVYYVMVTSTlsifqgk 141
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFL-------SIGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYL------- 66

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 393537031   142 ikptyRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVVAGVLSGIAVAETF 195
Cdd:smart00014  67 -----PARAGRKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVL 115
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 61-192 2.67e-11

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: 60.13  E-value: 2.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031   61 LLWVAVIGDWLNLVFKWILFGQRPYWWVLDTDYYSNTSVPLikqfpvtcETGPGSPSGHAMGTAGVYYVmvtstLSIFQG 140
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLP--------GLGYSFPSGHSATAFALALL-----LALLLR 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 393537031  141 KIKPTYRFRCLNVILWLGFWavqlnVCLSRIYLAAHFPHQVVAGVLSGIAVA 192
Cdd:pfam01569  69 RLRKIVRVLLALLLLVLALL-----VGLSRLYLGVHFPSDVLAGALIGILLA 115
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 5-192 3.36e-06

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: 46.96  E-value: 3.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031   5 MNVLHDFGIQSTHYLQVNYQDSQDWFILVSVIADLRNAFYVLFPIWFHLQEAVGIKLLWVAVIGDWLNLV--FKWILFGQ 82
Cdd:COG0671   20 LALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLllLKYLFGRP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031  83 RPYWWvldtdyysntsvPLIKQFpVTCETGPGSPSGHAMGTAGVYYVMVtstlsifqgkikptYRFRCLNVILWLGFWAV 162
Cdd:COG0671  100 RPFVV------------PDLELL-LGTAGGYSFPSGHAAAAFALALVLA--------------LLLPRRWLAALLLALAL 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 393537031 163 QlnVCLSRIYLAAHFPHQVVAGVLSGIAVA 192
Cdd:COG0671  153 L--VGLSRVYLGVHYPSDVLAGALLGLAIA 180
 
Name Accession Description Interval E-value
PAP2_glucose_6_phosphatase cd03381
PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts ...
 42-280 2.32e-139

PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts glucose-6-phosphate into free glucose and is active in the lumen of the endoplasmic reticulum, where it is bound to the membrane. The generation of free glucose is an important control point in metabolism, and stands at the end of gluconeogenesis and the release of glucose from glycogen. Deficiency of glucose-6-phosphatase leads to von Gierke's disease.


Pssm-ID: 239476  Cd Length: 235  Bit Score: 395.21  E-value: 2.32e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031  42 AFYVLFPIWFHLQEAVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVLDTDYYSNTSVPLIKQFPVTCETGPGSPSGHAM 121
Cdd:cd03381    1 LFLIVFPLCGHLSQSVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVHETDYYSNSSVPKIEQFPLTCETGPGSPSGHAM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031 122 GTAGVYYVMVTSTLSIFQGKIkptyRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVVAGVLSGIAVAETFSHIHSI 201
Cdd:cd03381   81 GTTAVLLVMVTALLSHLAGRK----RSRFLRVMLWLVFWGVQLAVCLSRIYLAAHFPHQVIAGVISGIAVAETFSHIRYI 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 393537031 202 YNASLKKYFLITFFLFSFAIGFYLLLKGLGVDLLWTLEKAQRWCEQPEWVHIDTTPFASLLKNLGTLFGLGLALNSSMY 280
Cdd:cd03381  157 YSASLKRYVLITFFLFGFALGFYLLLKWLGVDLLWSLEKAFKWCERPEWVHIDTTPFASLLRNLGTLLGLGLALNSSMY 235
acidPPc smart00014
Acid phosphatase homologues;
62-195 5.83e-23

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 92.41  E-value: 5.83e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031    62 LWVAVIGDWLNLVFKWILFGQRPYWWvldtdyySNTSVPLIKQFPVTCETGPGSPSGHAMGTAGVYYVMVTSTlsifqgk 141
Cdd:smart00014   1 ALLAVVSQLFNGVIKNYFGRPRPFFL-------SIGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYL------- 66

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 393537031   142 ikptyRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVVAGVLSGIAVAETF 195
Cdd:smart00014  67 -----PARAGRKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVL 115
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
 55-195 1.40e-16

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: 75.19  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031  55 EAVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVLDTDYYsntsvplikQFPVTCETGPGSPSGHAMGTAGVYYVMVTSt 134
Cdd:cd01610    2 RLLALLLLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDG---------DPLLLTEGGYSFPSGHAAFAFALALFLALL- 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 393537031 135 lsifqgkikptYRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVVAGVLSGIAVAETF 195
Cdd:cd01610   72 -----------LPRRLLRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLV 121
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
 61-192 2.67e-11

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: 60.13  E-value: 2.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031   61 LLWVAVIGDWLNLVFKWILFGQRPYWWVLDTDYYSNTSVPLikqfpvtcETGPGSPSGHAMGTAGVYYVmvtstLSIFQG 140
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPSTLP--------GLGYSFPSGHSATAFALALL-----LALLLR 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 393537031  141 KIKPTYRFRCLNVILWLGFWavqlnVCLSRIYLAAHFPHQVVAGVLSGIAVA 192
Cdd:pfam01569  69 RLRKIVRVLLALLLLVLALL-----VGLSRLYLGVHFPSDVLAGALIGILLA 115
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
 5-192 3.36e-06

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: 46.96  E-value: 3.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031   5 MNVLHDFGIQSTHYLQVNYQDSQDWFILVSVIADLRNAFYVLFPIWFHLQEAVGIKLLWVAVIGDWLNLV--FKWILFGQ 82
Cdd:COG0671   20 LALALLALLLLLALLLLLLLLLALLLILLLLLLLLLLLLLLLLLLLRLLALLLLLLLLAALLLLLLLLLLllLKYLFGRP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031  83 RPYWWvldtdyysntsvPLIKQFpVTCETGPGSPSGHAMGTAGVYYVMVtstlsifqgkikptYRFRCLNVILWLGFWAV 162
Cdd:COG0671  100 RPFVV------------PDLELL-LGTAGGYSFPSGHAAAAFALALVLA--------------LLLPRRWLAALLLALAL 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 393537031 163 QlnVCLSRIYLAAHFPHQVVAGVLSGIAVA 192
Cdd:COG0671  153 L--VGLSRVYLGVHYPSDVLAGALLGLAIA 180
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 71-192 1.58e-05

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: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031  71 LNLVFKWILFGQRPYWWVLDTdyysntsvplikqfpvtcETGPGSPSGHAMGTAgvyyVMVTSTLSIFQGKIKPTyRFRC 150
Cdd:cd03392   77 LNTLLKLLVQRPRPPLHLLVP------------------EGGYSFPSGHAMGAT----VLYGFLAYLLARRLPRR-RVRI 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 393537031 151 LNVILWLGFWavqLNVCLSRIYLAAHFPHQVVAGVLSGIAVA 192
Cdd:cd03392  134 LLLILAAILI---LLVGLSRLYLGVHYPSDVLAGWLLGLAWL 172
PAP2_SPPase1 cd03388
PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an ...
 43-190 7.90e-05

PAP2_like proteins, sphingosine-1-phosphatase subfamily. Sphingosine-1-phosphatase is an intracellular enzyme located in the endoplasmic reticulum, which regulates the level of sphingosine-1-phosphate (S1P), a bioactive lipid. S1P acts as a second messenger in the cell, and extracellularly by binding to G-protein coupled receptors of the endothelial differentiation gene family.


Pssm-ID: 239482  Cd Length: 151  Bit Score: 42.22  E-value: 7.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031  43 FYVLF-PIWFHL-QEAVGIKLLWVAVIGDWLNLVFKWILFGQRPYwwvldtdyysntSVPLIKQFPVTCETGPGSPSGHA 120
Cdd:cd03388   18 FYILFlPFLFWNgDPYVGRDLVVVLALGMYIGQFIKDLFCLPRPS------------SPPVVRLTMSSAALEYGFPSTHA 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031 121 MGTAGVYYVMVTSTLSIFQgkikpTYRFRCLNVILwlgFWAVqlNVCLSRIYLAAHFPHQVVAGVLSGIA 190
Cdd:cd03388   86 MNATAISFYLLIYLYDRYQ-----YPFVLGLILAL---FYST--LVCLSRIYMGMHSVLDVIAGSLIGVL 145
PAP2_dolichyldiphosphatase cd03382
PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a ...
 111-192 1.98e-04

PAP2_like proteins, dolichyldiphosphatase subfamily. Dolichyldiphosphatase is a membrane-associated protein located in the endoplasmic reticulum and hydrolyzes dolichyl pyrophosphate, as well as dolichylmonophosphate at a low rate. The enzyme is necessary for maintaining proper levels of dolichol-linked oligosaccharides and protein N-glycosylation, and might play a role in re-utilization of the glycosyl carrier lipid for additional rounds of lipid intermediate biosynthesis after its release during protein N-glycosylation reactions.


Pssm-ID: 239477  Cd Length: 159  Bit Score: 41.49  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031 111 TGPGSPSGHA--MGTAGVYyvmvtSTLSIFQgKIKPTYRFRcLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVVAGVLSG 188
Cdd:cd03382   79 SGYGMPSSHSqfMGFFAVY-----LLLFIYL-RLGRLNSLV-SRFLLSLGLLLLALLVSYSRVYLGYHTVSQVVVGAIVG 151


                 ....
gi 393537031 189 IAVA 192
Cdd:cd03382  152 ILLG 155
PAP2_like_3 cd03393
PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
 58-192 2.55e-03

PAP2_like_3 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria and archaea, lacks functional characterization and may act as a membrane-associated lipid phosphatase.


Pssm-ID: 239487 [Multi-domain]  Cd Length: 125  Bit Score: 37.35  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031  58 GIKLLWVAVIGDWLNLVFKWILFGQRPYwwvldtdyysnTSVPLIKQFPVTcETGPGSPSGHAMGTAgvyyvmvtstlsI 137
Cdd:cd03393   15 GRYLGLALCASGYLNAALKEVFKIPRPF-----------TYDGIQAIYEES-AGGYGFPSGHAQTSA------------T 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 393537031 138 FQGKIKPTYRFRClnvILWLGFWAVQLnVCLSRIYLAAHFPHQVVAGVLSGIAVA 192
Cdd:cd03393   71 FWGSLMLHVRKKW---FTLIGVVLVVL-ISFSRLYLGVHWPSDVIGGVLIGLLVL 121
PAP2_haloperoxidase cd03398
PAP2, haloperoxidase_like subfamily. Haloperoxidases catalyze the oxidation of halides such as ...
 113-193 6.28e-03

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: 37.79  E-value: 6.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393537031 113 PGSPSGHAMgTAGVY-----------YVMVTSTLSIFQGKIKPTYRFrclnvilWLGFWAVQLNVCLSRIYLAAHFPHQV 181
Cdd:cd03398  145 PSYPSGHAT-FAGAAatvlkalfgsdKVPDTVSEPDEGGPSTGVTRV-------WAELNELADEVAISRVYAGVHFRSDD 216

                         90
                 ....*....|..
gi 393537031 182 VAGVLSGIAVAE 193
Cdd:cd03398  217 AAGAALGEQIGA 228
 
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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