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Conserved domains on  [gi|1867850438|ref|WP_178942158|]
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MULTISPECIES: cysteine hydrolase family protein [Furfurilactobacillus]

Protein Classification

cysteine hydrolase family protein( domain architecture ID 10003554)

cysteine hydrolase family protein related to isochorismatase and nicotinamidase; catalyzes the hydrolysis of a chemical bond using an active site cysteinyl residue

CATH:  3.40.50.850
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 10-187 5.36e-55

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: 172.01  E-value: 5.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  10 ALLIIDYTNDFVATkGALTTgKPGQKIETNILTLAEQFLQNGDYVILPTDLHDGVDPYHPETKLFPPHNLKSTWGRELYG 89
Cdd:COG1335     1 ALLVIDVQNDFVPP-GALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  90 ELASwyqshknDDHVYYFDKNRYSAFANTNLDNFLRSRRITNLHLAGVCTDICVLHTAVDAYNLDYQLTIHKDAVASFDP 169
Cdd:COG1335    79 ELAP-------LPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDP 151

                         170
                  ....*....|....*...
gi 1867850438 170 VGHAWALKHFENTLGAII 187
Cdd:COG1335   152 EAHEAALARLRAAGATVV 169
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 10-187 5.36e-55

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: 172.01  E-value: 5.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  10 ALLIIDYTNDFVATkGALTTgKPGQKIETNILTLAEQFLQNGDYVILPTDLHDGVDPYHPETKLFPPHNLKSTWGRELYG 89
Cdd:COG1335     1 ALLVIDVQNDFVPP-GALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  90 ELASwyqshknDDHVYYFDKNRYSAFANTNLDNFLRSRRITNLHLAGVCTDICVLHTAVDAYNLDYQLTIHKDAVASFDP 169
Cdd:COG1335    79 ELAP-------LPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDP 151

                         170
                  ....*....|....*...
gi 1867850438 170 VGHAWALKHFENTLGAII 187
Cdd:COG1335   152 EAHEAALARLRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 10-180 7.53e-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: 166.29  E-value: 7.53e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  10 ALLIIDYTNDFVATKGALTTGkpGQKIETNILTLAEQFLQNGDYVILPTDLHDGVDPYHPETkLFPPHNLKSTWGRELYG 89
Cdd:cd00431     1 ALLVVDMQNDFVPGGGLLLPG--ADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL-LWPPHCVKGTEGAELVP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  90 ELAswyqshkNDDHVYYFDKNRYSAFANTNLDNFLRSRRITNLHLAGVCTDICVLHTAVDAYNLDYQLTIHKDAVASFDP 169
Cdd:cd00431    78 ELA-------PLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDE 150

                         170
                  ....*....|.
gi 1867850438 170 VGHAWALKHFE 180
Cdd:cd00431   151 EDHEAALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 10-187 2.41e-45

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 147.55  E-value: 2.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  10 ALLIIDYTNDFVAtkGALTTGKPGQKIETNILTLAEQFLQNGDYVILPTDLHDGVDPYHPETKLFPPHNLKSTWGRELYG 89
Cdd:pfam00857   2 ALLVIDMQNDFVD--SGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPPGTTGAELVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  90 ELASWYqshknDDHVyyFDKNRYSAFANTNLDNFLRSRRITNLHLAGVCTDICVLHTAVDAYNLDYQLTIHKDAVASFDP 169
Cdd:pfam00857  80 ELAPLP-----GDLV--VDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSP 152

                         170
                  ....*....|....*...
gi 1867850438 170 VGHAWALKHFENTLGAII 187
Cdd:pfam00857 153 EAHDAALERLAQRGAEVT 170
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 8-188 1.32e-18

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 79.73  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438   8 KQALLIIDYTNDFVaTKGALTTGKPGQKIET-NILTLAEQFlqngDYVILPTDLH-------------DGVDPYHPETKL 73
Cdd:PTZ00331   12 NDALIIVDVQNDFC-KGGSLAVPDAEEVIPViNQVRQSHHF----DLVVATQDWHppnhisfasnhgkPKILPDGTTQGL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  74 FPPHNLKSTWGRELYGELASwyqshKNDDHVYYFDKNR----YSAFAN-----TNLDNFLRSRRITNLHLAGVCTDICVL 144
Cdd:PTZ00331   87 WPPHCVQGTKGAQLHKDLVV-----ERIDIIIRKGTNRdvdsYSAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFCVL 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1867850438 145 HTAVDAYNLDYQLTIHKDAVASFDPVGHAWALKHFENtLGAIIV 188
Cdd:PTZ00331  162 FTALDAVKLGFKVVVLEDATRAVDPDAISKQRAELLE-AGVILL 204
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 10-187 5.36e-55

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: 172.01  E-value: 5.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  10 ALLIIDYTNDFVATkGALTTgKPGQKIETNILTLAEQFLQNGDYVILPTDLHDGVDPYHPETKLFPPHNLKSTWGRELYG 89
Cdd:COG1335     1 ALLVIDVQNDFVPP-GALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  90 ELASwyqshknDDHVYYFDKNRYSAFANTNLDNFLRSRRITNLHLAGVCTDICVLHTAVDAYNLDYQLTIHKDAVASFDP 169
Cdd:COG1335    79 ELAP-------LPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDP 151

                         170
                  ....*....|....*...
gi 1867850438 170 VGHAWALKHFENTLGAII 187
Cdd:COG1335   152 EAHEAALARLRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 10-180 7.53e-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: 166.29  E-value: 7.53e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  10 ALLIIDYTNDFVATKGALTTGkpGQKIETNILTLAEQFLQNGDYVILPTDLHDGVDPYHPETkLFPPHNLKSTWGRELYG 89
Cdd:cd00431     1 ALLVVDMQNDFVPGGGLLLPG--ADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL-LWPPHCVKGTEGAELVP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  90 ELAswyqshkNDDHVYYFDKNRYSAFANTNLDNFLRSRRITNLHLAGVCTDICVLHTAVDAYNLDYQLTIHKDAVASFDP 169
Cdd:cd00431    78 ELA-------PLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDE 150

                         170
                  ....*....|.
gi 1867850438 170 VGHAWALKHFE 180
Cdd:cd00431   151 EDHEAALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 10-187 2.41e-45

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 147.55  E-value: 2.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  10 ALLIIDYTNDFVAtkGALTTGKPGQKIETNILTLAEQFLQNGDYVILPTDLHDGVDPYHPETKLFPPHNLKSTWGRELYG 89
Cdd:pfam00857   2 ALLVIDMQNDFVD--SGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPPGTTGAELVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  90 ELASWYqshknDDHVyyFDKNRYSAFANTNLDNFLRSRRITNLHLAGVCTDICVLHTAVDAYNLDYQLTIHKDAVASFDP 169
Cdd:pfam00857  80 ELAPLP-----GDLV--VDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSP 152

                         170
                  ....*....|....*...
gi 1867850438 170 VGHAWALKHFENTLGAII 187
Cdd:pfam00857 153 EAHDAALERLAQRGAEVT 170
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
10-179 1.47e-21

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 87.21  E-value: 1.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  10 ALLIIDYTNDFVATKGAltTGKPGQKIETNILTLAEQFLQNGDYVILPTDLHDGvdpyHPETKLFpphnLKSTWG----- 84
Cdd:COG1535    21 ALLIHDMQNYFLRPYDP--DEPPIRELVANIARLRDACRAAGIPVVYTAQPGDQ----TPEDRGL----LNDFWGpglta 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  85 ----RELYGELAswyqsHKNDDHVyyFDKNRYSAFANTNLDNFLRSRRITNLHLAGVCTDICVLHTAVDAYNLDYQLTIH 160
Cdd:COG1535    91 gpegQEIVDELA-----PAPGDTV--LTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVV 163

                         170
                  ....*....|....*....
gi 1867850438 161 KDAVASFDPVGHAWALKHF 179
Cdd:COG1535   164 ADAVADFSREEHRMALEYV 182
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 8-188 2.74e-19

Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, converts nicotinamide to nicotinic acid (niacin) and ammonia, which in turn can be recycled to make nicotinamide adenine dinucleotide (NAD). The same enzyme is also called pyrazinamidase, because in converts the tuberculosis drug pyrazinamide (PZA) into its active form pyrazinoic acid (POA).


Pssm-ID: 238493  Cd Length: 196  Bit Score: 81.16  E-value: 2.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438   8 KQALLIIDYTNDFVATkGALTTGKpGQKIETNILTLAEQFLqnGDYVILPTDLHD---------------GVDPYHPETK 72
Cdd:cd01011     1 TDALLVVDVQNDFCPG-GALAVPG-GDAIVPLINALLSLFQ--YDLVVATQDWHPanhasfasnhpgqmpFITLPPGPQV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  73 LFPPHNLKSTWGRELYGELASwyqsHKNDDHVY---YFDKNRYSAF------ANTNLDNFLRSRRITNLHLAGVCTDICV 143
Cdd:cd01011    77 LWPDHCVQGTPGAELHPGLPV----PDIDLIVRkgtNPDIDSYSAFfdndrrSSTGLAEYLRERGIDRVDVVGLATDYCV 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1867850438 144 LHTAVDAYNLDYQLTIHKDAVASFDPVGHAWALKHFeNTLGAIIV 188
Cdd:cd01011   153 KATALDALKAGFEVRVLEDACRAVDPETIERAIEEM-KEAGVVLV 196
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 8-188 1.32e-18

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 79.73  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438   8 KQALLIIDYTNDFVaTKGALTTGKPGQKIET-NILTLAEQFlqngDYVILPTDLH-------------DGVDPYHPETKL 73
Cdd:PTZ00331   12 NDALIIVDVQNDFC-KGGSLAVPDAEEVIPViNQVRQSHHF----DLVVATQDWHppnhisfasnhgkPKILPDGTTQGL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  74 FPPHNLKSTWGRELYGELASwyqshKNDDHVYYFDKNR----YSAFAN-----TNLDNFLRSRRITNLHLAGVCTDICVL 144
Cdd:PTZ00331   87 WPPHCVQGTKGAQLHKDLVV-----ERIDIIIRKGTNRdvdsYSAFDNdkgskTGLAQILKAHGVRRVFICGLAFDFCVL 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1867850438 145 HTAVDAYNLDYQLTIHKDAVASFDPVGHAWALKHFENtLGAIIV 188
Cdd:PTZ00331  162 FTALDAVKLGFKVVVLEDATRAVDPDAISKQRAELLE-AGVILL 204
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 10-176 5.47e-17

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: 73.78  E-value: 5.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  10 ALLIIDYTNDFVatkgalTTGKPGQ---KIETNILTLAEQFLQNGDYVILPTDLHDGVDPYHPETKLFpphnlkstwgrE 86
Cdd:cd01014     1 ALLVIDVQNGYF------DGGLPPLnneAALENIAALIAAARAAGIPVIHVRHIDDEGGSFAPGSEGW-----------E 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  87 LYGELASwyqshKNDDHVyyFDKNRYSAFANTNLDNFLRSRRITNLHLAGVCTDICVLHTAVDAYNLDYQLTIHKDAVAS 166
Cdd:cd01014    64 IHPELAP-----LEGETV--IEKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACAT 136

                         170
                  ....*....|
gi 1867850438 167 FDPVGHAWAL 176
Cdd:cd01014   137 FDLPDHGGVL 146
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
8-162 1.52e-11

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 60.39  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438   8 KQALLIIDYTNDFVAtKGALTTGKPGQKIETnILTLAEQFLQNGDYVILPTDLH----------DGVDPYH-------PE 70
Cdd:PRK11609    2 KRALLLVDLQNDFCA-GGALAVPEGDSTIDV-ANRLIDWCQSRGIPVIASQDWHpanhgsfasnHGAEPGTqgeldglPQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  71 TkLFPPHNLKSTWGRELYGELaswyqSHKNDDHVYYFDKNR----YSAF------ANTNLDNFLRSRRITNLHLAGVCTD 140
Cdd:PRK11609   80 T-WWPDHCVQNSEGAALHPLL-----NQKAIDAVFHKGENPlidsYSAFfdnghrQKTALDDWLREHGITELIVMGLATD 153

                         170       180
                  ....*....|....*....|..
gi 1867850438 141 ICVLHTAVDAYNLDYQLTIHKD 162
Cdd:PRK11609  154 YCVKFTVLDALALGYQVNVITD 175
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 109-187 3.32e-10

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: 56.26  E-value: 3.32e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867850438 109 KNRYSAFANTNLDNFLRSRRITNLHLAGVCTDICVLHTAVDAYNLDYQLTIHKDAVASFDPVGHAWALKHFENTLGAII 187
Cdd:cd01015    94 KKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDRAPAPHEANLFDIDNKYGDVV 172
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 3-178 2.90e-09

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: 54.27  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438   3 QMDFGKQALLIIDYTNDFVATKGAltTGKPGQKIETNILTLAEQFLQNGDYVIlptdlhdgvdpYHPETKLFPPHN---L 79
Cdd:cd01013    24 QIDPKRAVLLVHDMQRYFLDFYDE--SAEPVPQLIANIARLRDWCRQAGIPVV-----------YTAQPGNQTPEQralL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  80 KSTWG---------RELYGELASwyqshKNDDHVYyfDKNRYSAFANTNLDNFLRSRRITNLHLAGVCTDICVLHTAVDA 150
Cdd:cd01013    91 NDFWGpgltaspeeTKIVTELAP-----QPDDTVL--TKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDA 163

                         170       180
                  ....*....|....*....|....*...
gi 1867850438 151 YNLDYQLTIHKDAVASFDPVGHAWALKH 178
Cdd:cd01013   164 FMRDIQPFVVADAIADFSLEEHRMALKY 191
PRK11440 PRK11440
putative hydrolase; Provisional
 109-178 6.12e-08

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 50.11  E-value: 6.12e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438 109 KNRYSAFANTNLDNFLRSRRITNLHLAGVCTDICVLHTAVDAYNLDYQLTIHKDAVASFDPVGHAWALKH 178
Cdd:PRK11440  101 KRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQHQNSMNH 170
PLN02743 PLN02743
nicotinamidase
 11-152 4.42e-07

nicotinamidase


Pssm-ID: 215396  Cd Length: 239  Bit Score: 48.20  E-value: 4.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438  11 LLIIDYTNDFvATKGA--LTTGKPGQKIETNI---LTLAEQFLQNGDYVILPTDLHDGVDPYHPetklFPPHNLKSTWGR 85
Cdd:PLN02743   30 LVLVDEVNGF-CTVGAgnLAPREPDKQISKMVdesARLAREFCERKWPVLAFLDSHHPDKPEHP----YPPHCIVGTGEE 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1867850438  86 ELYGELAsWYQshkNDDHVYYFDKNRYSAF--------ANTNLDnFLRSRRITNLHLAGVCTDICVLH---TAVDAYN 152
Cdd:PLN02743  105 NLVPALQ-WLE---NDPNVTLRRKDCIDGFvgaiekdgSNVFVD-WVNNNKIKVILVVGICTDICVLDfvaSALSARN 177
PLN02621 PLN02621
nicotinamidase
 108-177 1.31e-06

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 46.70  E-value: 1.31e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438 108 DKNRYSAFANTNLDNFLRSRRITNLHLAGVCTDICVLHTAVDAYNLDYQLTIHKDAVASFDPVGHAWALK 177
Cdd:PLN02621  106 EKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATANEELHEATLK 175
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 106-188 2.10e-06

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: 45.66  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867850438 106 YFDKNRYSAFANTNLDNFLRSRRITNLHLAGVCTDICVLHTAVDAYNLDYQLTIHKDAVASFDPVGHAWALKHFENTlGA 185
Cdd:cd01012    65 VIEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQA-GA 143


                  ...
gi 1867850438 186 IIV 188
Cdd:cd01012   144 VLT 146
 
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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