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Conserved domains on  [gi|1748320669|gb|KAA6442551|]
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isochorismatase [Bacillus subtilis]

Protein Classification

isochorismatase( domain architecture ID 10099065)

isochorismatase catalyzes the conversion of isochorismate to 2,3-dihydro-2,3-dihydroxybenzoate in siderophore synthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
2-204 2.32e-142

Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the conversion of isochorismate, in the presence of water, to 2,3-dihydroxybenzoate and pyruvate, via the hydrolysis of a vinyl ether, an uncommon reaction in biological systems. Isochorismatase is part of the phenazine biosynthesis pathway. Phenazines are antimicrobial compounds that provide the competitive advantage for certain bacteria.


:

Pssm-ID: 238495  Cd Length: 203  Bit Score: 399.41  E-value: 2.32e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669   2 AIPAIQPYQMPTASDMPQNKVSWVPDPNRAVLLIHDMQNYFVDAFTAGASPVTELSANIRKLKNQCVQLGIPVVYTAQPG 81
Cdd:cd01013     1 AIPKIASYPLPTAESFPANKVDWQIDPKRAVLLVHDMQRYFLDFYDESAEPVPQLIANIARLRDWCRQAGIPVVYTAQPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  82 SQNPDDRALLTDFWGPGLNSGPYEEKIITELAPEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTA 161
Cdd:cd01013    81 NQTPEQRALLNDFWGPGLTASPEETKIVTELAPQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1748320669 162 CEAFMEDIKAFFVGDAVADFSLEKHQMALEYAAGRCAFTVMTD 204
Cdd:cd01013   161 VDAFMRDIQPFVVADAIADFSLEEHRMALKYAATRCAMVVSTD 203
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
235-293 5.06e-08

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


:

Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 49.10  E-value: 5.06e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669 235 IRKQIAELLQETPEDITDQEDLLDRGLDSVRIMTLVEQWRRE-GAEVTFVELAERPTIEE 293
Cdd:pfam00550   3 LRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
 
Name Accession Description Interval E-value
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
2-204 2.32e-142

Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the conversion of isochorismate, in the presence of water, to 2,3-dihydroxybenzoate and pyruvate, via the hydrolysis of a vinyl ether, an uncommon reaction in biological systems. Isochorismatase is part of the phenazine biosynthesis pathway. Phenazines are antimicrobial compounds that provide the competitive advantage for certain bacteria.


Pssm-ID: 238495  Cd Length: 203  Bit Score: 399.41  E-value: 2.32e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669   2 AIPAIQPYQMPTASDMPQNKVSWVPDPNRAVLLIHDMQNYFVDAFTAGASPVTELSANIRKLKNQCVQLGIPVVYTAQPG 81
Cdd:cd01013     1 AIPKIASYPLPTAESFPANKVDWQIDPKRAVLLVHDMQRYFLDFYDESAEPVPQLIANIARLRDWCRQAGIPVVYTAQPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  82 SQNPDDRALLTDFWGPGLNSGPYEEKIITELAPEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTA 161
Cdd:cd01013    81 NQTPEQRALLNDFWGPGLTASPEETKIVTELAPQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1748320669 162 CEAFMEDIKAFFVGDAVADFSLEKHQMALEYAAGRCAFTVMTD 204
Cdd:cd01013   161 VDAFMRDIQPFVVADAIADFSLEEHRMALKYAATRCAMVVSTD 203
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
12-215 1.35e-128

Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 364.56  E-value: 1.35e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  12 PTASDMPQNKVSWVPDPNRAVLLIHDMQNYFVDAFTAGASPVTELSANIRKLKNQCVQLGIPVVYTAQPGSQNPDDRALL 91
Cdd:COG1535     1 PTAADLPANKVSWTLDPARAALLIHDMQNYFLRPYDPDEPPIRELVANIARLRDACRAAGIPVVYTAQPGDQTPEDRGLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  92 TDFWGPGLNSGPYEEKIITELAPEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTACEAFMEDIKA 171
Cdd:COG1535    81 NDFWGPGLTAGPEGQEIVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQP 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1748320669 172 FFVGDAVADFSLEKHQMALEYAAGRCAFTVMTDSLLDQLQNAPA 215
Cdd:COG1535   161 FVVADAVADFSREEHRMALEYVAGRCGVVVTTDEVLEALRAAGP 204
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
31-203 9.27e-45

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 150.25  E-value: 9.27e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  31 AVLLIHDMQNYFVDAFTAGASPVTELSANIRKLKNQCVQLGIPVVYTAQPGSQNPDDRALlTDFWGPGLNSGPYEEKIIT 110
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFAL-KDRPSPAFPPGTTGAELVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669 111 ELAPEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTACEAFMEDIKAFFVGDAVADFSLEKHQMAL 190
Cdd:pfam00857  80 ELAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAAL 159
                         170
                  ....*....|...
gi 1748320669 191 EYAAGRCAfTVMT 203
Cdd:pfam00857 160 ERLAQRGA-EVTT 171
PLN02621 PLN02621
nicotinamidase
25-210 3.32e-26

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 102.55  E-value: 3.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  25 VPDPNRAVLLIHDMQNYFvdaftagASPVTELSANIRKLKNQCVQLGIPVVYTaQPGSQNPDDRALLTDFW-GPGLNSGP 103
Cdd:PLN02621   15 DPDPKQAALLVIDMQNYF-------SSMAEPILPALLTTIDLCRRASIPVFFT-RHSHKSPSDYGMLGEWWdGDLILDGT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669 104 YEEKIITELA-PEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTACEAFMEDIKAFFVGDAVADFS 182
Cdd:PLN02621   87 TEAELMPEIGrVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATAN 166
                         170       180
                  ....*....|....*....|....*...
gi 1748320669 183 LEKHQMALEYAAGRCAFTVMTDSLLDQL 210
Cdd:PLN02621  167 EELHEATLKNLAYGFAYLVDCDRLEAGL 194
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
235-293 5.06e-08

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 49.10  E-value: 5.06e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669 235 IRKQIAELLQETPEDITDQEDLLDRGLDSVRIMTLVEQWRRE-GAEVTFVELAERPTIEE 293
Cdd:pfam00550   3 LRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
235-293 1.44e-04

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 39.84  E-value: 1.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1748320669 235 IRKQIAELLQETPEDITDQEDLL-DRGLDSVRIMTLVEQWRRE-GAEVTFVELAERPTIEE 293
Cdd:COG0236    10 LAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVAD 70
 
Name Accession Description Interval E-value
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
2-204 2.32e-142

Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the conversion of isochorismate, in the presence of water, to 2,3-dihydroxybenzoate and pyruvate, via the hydrolysis of a vinyl ether, an uncommon reaction in biological systems. Isochorismatase is part of the phenazine biosynthesis pathway. Phenazines are antimicrobial compounds that provide the competitive advantage for certain bacteria.


Pssm-ID: 238495  Cd Length: 203  Bit Score: 399.41  E-value: 2.32e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669   2 AIPAIQPYQMPTASDMPQNKVSWVPDPNRAVLLIHDMQNYFVDAFTAGASPVTELSANIRKLKNQCVQLGIPVVYTAQPG 81
Cdd:cd01013     1 AIPKIASYPLPTAESFPANKVDWQIDPKRAVLLVHDMQRYFLDFYDESAEPVPQLIANIARLRDWCRQAGIPVVYTAQPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  82 SQNPDDRALLTDFWGPGLNSGPYEEKIITELAPEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTA 161
Cdd:cd01013    81 NQTPEQRALLNDFWGPGLTASPEETKIVTELAPQPDDTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1748320669 162 CEAFMEDIKAFFVGDAVADFSLEKHQMALEYAAGRCAFTVMTD 204
Cdd:cd01013   161 VDAFMRDIQPFVVADAIADFSLEEHRMALKYAATRCAMVVSTD 203
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
12-215 1.35e-128

Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 364.56  E-value: 1.35e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  12 PTASDMPQNKVSWVPDPNRAVLLIHDMQNYFVDAFTAGASPVTELSANIRKLKNQCVQLGIPVVYTAQPGSQNPDDRALL 91
Cdd:COG1535     1 PTAADLPANKVSWTLDPARAALLIHDMQNYFLRPYDPDEPPIRELVANIARLRDACRAAGIPVVYTAQPGDQTPEDRGLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  92 TDFWGPGLNSGPYEEKIITELAPEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTACEAFMEDIKA 171
Cdd:COG1535    81 NDFWGPGLTAGPEGQEIVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQP 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1748320669 172 FFVGDAVADFSLEKHQMALEYAAGRCAFTVMTDSLLDQLQNAPA 215
Cdd:COG1535   161 FVVADAVADFSREEHRMALEYVAGRCGVVVTTDEVLEALRAAGP 204
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
3-305 8.64e-63

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 200.75  E-value: 8.64e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669   3 IPAIQPYQMPTASDMPQNKVSWVPDPNRAVLLIHDMQNYFVDAFTAGASPVTELSANIRKLKNQCVQLGIPVVYTAQPGS 82
Cdd:COG3433     1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  83 QNPDDRALLTDFWGPGLNSGPYEEKIITELAPEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTAC 162
Cdd:COG3433    81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669 163 EAFMEDIKAFFVGDAVADFSLEKHQMALEYAAGRCAFTVMTDSLLDQLQNAPADVQKTsantgkknvFTCENIRKQIAEL 242
Cdd:COG3433   161 ALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETA---------LTEEELRADVAEL 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1748320669 243 LQETPEDITDQEDLLDRGLDSVRIMTLVEQWRREGAEVTFVELAERPTIEEWQKLLTTRSQQV 305
Cdd:COG3433   232 LGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAA 294
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
32-194 1.09e-53

Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine amidohydrolase), involved in creatine metabolism and nicotinamidase, converting nicotinamide to nicotinic acid and ammonia in the pyridine nucleotide cycle. It also contains isochorismatase, an enzyme that catalyzes the conversion of isochorismate to 2,3-dihydroxybenzoate and pyruvate, via the hydrolysis of the vinyl ether bond, and other related enzymes with unknown function.


Pssm-ID: 238245 [Multi-domain]  Cd Length: 161  Bit Score: 172.84  E-value: 1.09e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  32 VLLIHDMQNYFVDAFTAGASPVTELSANIRKLKNQCVQLGIPVVYTAQPGSQNPDDRALLtdFWGPGLNSGPYEEKIITE 111
Cdd:cd00431     1 ALLVVDMQNDFVPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL--LWPPHCVKGTEGAELVPE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669 112 LAPEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTACEAFMEDIKAFFVGDAVADFSLEKHQMALE 191
Cdd:cd00431    79 LAPLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAALE 158

                  ...
gi 1748320669 192 YAA 194
Cdd:cd00431   159 RLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
31-203 9.27e-45

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 150.25  E-value: 9.27e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  31 AVLLIHDMQNYFVDAFTAGASPVTELSANIRKLKNQCVQLGIPVVYTAQPGSQNPDDRALlTDFWGPGLNSGPYEEKIIT 110
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFAL-KDRPSPAFPPGTTGAELVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669 111 ELAPEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTACEAFMEDIKAFFVGDAVADFSLEKHQMAL 190
Cdd:pfam00857  80 ELAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAAL 159
                         170
                  ....*....|...
gi 1748320669 191 EYAAGRCAfTVMT 203
Cdd:pfam00857 160 ERLAQRGA-EVTT 171
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
31-198 1.96e-36

Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction only]; Nicotinamidase-related amidase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440946 [Multi-domain]  Cd Length: 169  Bit Score: 128.48  E-value: 1.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  31 AVLLIhDMQNYFVDAFTAGASPVTELSANIRKLKNQCVQLGIPVVYTAQpGSQNPDDRALLTDFWGPGLNSGPYEEKIIT 110
Cdd:COG1335     1 ALLVI-DVQNDFVPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRD-WHPPDGSEFAEFDLWPPHCVPGTPGAELVP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669 111 ELAPEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTACEAFMEDIKAFFVGDAVADFSLEKHQMAL 190
Cdd:COG1335    79 ELAPLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAAL 158

                  ....*...
gi 1748320669 191 EYAAGRCA 198
Cdd:COG1335   159 ARLRAAGA 166
PLN02621 PLN02621
nicotinamidase
25-210 3.32e-26

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 102.55  E-value: 3.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  25 VPDPNRAVLLIHDMQNYFvdaftagASPVTELSANIRKLKNQCVQLGIPVVYTaQPGSQNPDDRALLTDFW-GPGLNSGP 103
Cdd:PLN02621   15 DPDPKQAALLVIDMQNYF-------SSMAEPILPALLTTIDLCRRASIPVFFT-RHSHKSPSDYGMLGEWWdGDLILDGT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669 104 YEEKIITELA-PEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTACEAFMEDIKAFFVGDAVADFS 182
Cdd:PLN02621   87 TEAELMPEIGrVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATAN 166
                         170       180
                  ....*....|....*....|....*...
gi 1748320669 183 LEKHQMALEYAAGRCAFTVMTDSLLDQL 210
Cdd:PLN02621  167 EELHEATLKNLAYGFAYLVDCDRLEAGL 194
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
32-211 1.11e-11

YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown specificity. Despite its weak sequence similarity, it is structurally related to other amidohydrolases and shares conserved active site residues with them. Multimerisation interface seems not to be conserved in all members.


Pssm-ID: 238494 [Multi-domain]  Cd Length: 157  Bit Score: 61.84  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  32 VLLIHDMQnyfvDAFTAGASPVTELSANIRKLKNQCVQLGIPVVYTAQpgsqnpddralltdfwGPGLNSGPYEEkiITE 111
Cdd:cd01012     1 ALLLVDVQ----EKLAPAIKSFDELINNTVKLAKAAKLLDVPVILTEQ----------------YPKGLGPTVPE--LRE 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669 112 LAPedDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTACEAFMEDIKAFFVGDAVADFSLEKHQMALE 191
Cdd:cd01012    59 VFP--DAPVIEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALA 136
                         170       180
                  ....*....|....*....|
gi 1748320669 192 YAAGRCAFTVMTDSLLDQLQ 211
Cdd:cd01012   137 RMRQAGAVLTTSESVLFELQ 156
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
32-190 5.32e-11

Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share the catalytic triad with other amidohydrolases, like nicotinamidase, which converts nicotinamide to nicotinic acid and ammonia.


Pssm-ID: 238496 [Multi-domain]  Cd Length: 155  Bit Score: 59.91  E-value: 5.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  32 VLLIHDMQN-YFVDAFTAGASPvtELSANIRKLKNQCVQLGIPVVY----TAQPGSQNPddralltdfwgpglNSGPYEe 106
Cdd:cd01014     1 ALLVIDVQNgYFDGGLPPLNNE--AALENIAALIAAARAAGIPVIHvrhiDDEGGSFAP--------------GSEGWE- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669 107 kIITELAPEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTACEAFMEDIKAFFVGDAVADFSLEKH 186
Cdd:cd01014    64 -IHPELAPLEGETVIEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDH 142

                  ....
gi 1748320669 187 QMAL 190
Cdd:cd01014   143 GGVL 146
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
33-208 7.71e-09

N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, carbon dioxide and ammonia. CSHase is involved in one of the two alternative pathways for creatinine degradation to glycine in microorganisms.This CSHase-containing pathway degrades creatinine via N-methylhydantoin N-carbamoylsarcosine and sarcosine to glycine. Enzymes of this pathway are used in the diagnosis for renal disfunction, for determining creatinine levels in urine and serum.


Pssm-ID: 238497 [Multi-domain]  Cd Length: 179  Bit Score: 54.33  E-value: 7.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669  33 LLIHDMQNYFVDAFTAGASPVTELSANIRKLKNQCVQLGIPVVYTA---QPGSQNP----DDRALLTDfwgpgLNSGPYE 105
Cdd:cd01015     2 LLVIDLVEGYTQPGSYLAPGIAAALENVQRLLAAARAAGVPVIHTTvvyDPDGADGglwaRKVPAMSD-----LVEGSPL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669 106 EKIITELAPEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHiGCL-VTACEAFMEDIKAFFVGDAVADFSLE 184
Cdd:cd01015    77 AAICDELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTS-GCIrATAVDAMQHGFRPIVVRECVGDRAPA 155
                         170       180
                  ....*....|....*....|....
gi 1748320669 185 KHQMALEYAAGRCAFTVMTDSLLD 208
Cdd:cd01015   156 PHEANLFDIDNKYGDVVSTDDALA 179
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
235-293 5.06e-08

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 49.10  E-value: 5.06e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669 235 IRKQIAELLQETPEDITDQEDLLDRGLDSVRIMTLVEQWRRE-GAEVTFVELAERPTIEE 293
Cdd:pfam00550   3 LRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
PRK11440 PRK11440
putative hydrolase; Provisional
110-210 9.03e-06

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 45.49  E-value: 9.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748320669 110 TELAPEDDDLVLTKWRYSAFKRTNLLEMMRKEGRDQLIITGIYAHIGCLVTACEAFMEDIKAFFVGDAVADFSLEKHQMA 189
Cdd:PRK11440   88 AALGKTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQHQNS 167
                          90       100
                  ....*....|....*....|.
gi 1748320669 190 LEYAAGRCAFTVMTDSLLDQL 210
Cdd:PRK11440  168 MNHIFPRIARVRSVEEILNAL 188
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
235-293 1.44e-04

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 39.84  E-value: 1.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1748320669 235 IRKQIAELLQETPEDITDQEDLL-DRGLDSVRIMTLVEQWRRE-GAEVTFVELAERPTIEE 293
Cdd:COG0236    10 LAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVAD 70
 
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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