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Conserved domains on  [gi|881073450|ref|WP_048789815|]
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MULTISPECIES: cysteine hydrolase family protein [Streptococcus]

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 ...
 4-182 6.00e-50

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: 158.91  E-value: 6.00e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450   4 ALISIDYTVDFVaDEGKLTAgAPAQAISESIAQVTQLAFDQGAYVFFAIDAHDVDDPFHPESKLFPPHNIIGTSGRDLYG 83
Cdd:COG1335    1 ALLVIDVQNDFV-PPGALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450  84 PLADFyrehkadPRVFWMDKRHYSAFSGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIEVVAPAVASLTP 163
Cdd:COG1335   79 ELAPL-------PGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDP 151

                        170
                 ....*....|....*....
gi 881073450 164 ENHQFALNHFKHvLGAKVV 182
Cdd:COG1335  152 EAHEAALARLRA-AGATVV 169
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 4-182 6.00e-50

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: 158.91  E-value: 6.00e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450   4 ALISIDYTVDFVaDEGKLTAgAPAQAISESIAQVTQLAFDQGAYVFFAIDAHDVDDPFHPESKLFPPHNIIGTSGRDLYG 83
Cdd:COG1335    1 ALLVIDVQNDFV-PPGALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450  84 PLADFyrehkadPRVFWMDKRHYSAFSGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIEVVAPAVASLTP 163
Cdd:COG1335   79 ELAPL-------PGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDP 151

                        170
                 ....*....|....*....
gi 881073450 164 ENHQFALNHFKHvLGAKVV 182
Cdd:COG1335  152 EAHEAALARLRA-AGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 4-174 6.52e-45

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: 145.87  E-value: 6.52e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450   4 ALISIDYTVDFVADEGKLTAGAPAqaISESIAQVTQLAFDQGAYVFFAIDAHDVDDPFHPESkLFPPHNIIGTsgrdlyg 83
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLLPGADE--LVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL-LWPPHCVKGT------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450  84 PLADFYREHKADPRVFWMDKRHYSAFSGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIEVVAPAVASLTP 163
Cdd:cd00431   71 EGAELVPELAPLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDE 150

                        170
                 ....*....|.
gi 881073450 164 ENHQFALNHFK 174
Cdd:cd00431  151 EDHEAALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 4-182 3.74e-40

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 134.07  E-value: 3.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450    4 ALISIDYTVDFVADEGKLTAGApaQAISESIAQVTQLAFDQGAYVFFAIDAHDVDDPFHPESKLFPPHNIIGTSGRDLYG 83
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGI--AAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPPGTTGAELVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450   84 PLADfyreHKADPRVfwmDKRHYSAFSGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIEVVAPAVASLTP 163
Cdd:pfam00857  80 ELAP----LPGDLVV---DKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSP 152

                         170
                  ....*....|....*....
gi 881073450  164 ENHQFALNHFKHvLGAKVV 182
Cdd:pfam00857 153 EAHDAALERLAQ-RGAEVT 170
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 4-174 5.07e-17

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 75.49  E-value: 5.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450   4 ALISIDYTVDFVADeGKLtAGAPAQAISESIAQVTQ-LAFDqgaYVFFAIDAHDVD-------------DPFHPESKLFP 69
Cdd:PTZ00331  14 ALIIVDVQNDFCKG-GSL-AVPDAEEVIPVINQVRQsHHFD---LVVATQDWHPPNhisfasnhgkpkiLPDGTTQGLWP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450  70 PHNIIGTSGRDLygpladfyreHKaDPRVFWMDKR----------HYSAFSG-----TDLDIRLRERGVDTVILTGVLTD 134
Cdd:PTZ00331  89 PHCVQGTKGAQL----------HK-DLVVERIDIIirkgtnrdvdSYSAFDNdkgskTGLAQILKAHGVRRVFICGLAFD 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 881073450 135 ICVLHTAVDAYNLGYQIEVVAPAVASLTPENHQFALNHFK 174
Cdd:PTZ00331 158 FCVLFTALDAVKLGFKVVVLEDATRAVDPDAISKQRAELL 197
 
Name Accession Description Interval E-value
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 4-182 6.00e-50

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: 158.91  E-value: 6.00e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450   4 ALISIDYTVDFVaDEGKLTAgAPAQAISESIAQVTQLAFDQGAYVFFAIDAHDVDDPFHPESKLFPPHNIIGTSGRDLYG 83
Cdd:COG1335    1 ALLVIDVQNDFV-PPGALAV-PGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAEFDLWPPHCVPGTPGAELVP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450  84 PLADFyrehkadPRVFWMDKRHYSAFSGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIEVVAPAVASLTP 163
Cdd:COG1335   79 ELAPL-------PGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDP 151

                        170
                 ....*....|....*....
gi 881073450 164 ENHQFALNHFKHvLGAKVV 182
Cdd:COG1335  152 EAHEAALARLRA-AGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 4-174 6.52e-45

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: 145.87  E-value: 6.52e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450   4 ALISIDYTVDFVADEGKLTAGAPAqaISESIAQVTQLAFDQGAYVFFAIDAHDVDDPFHPESkLFPPHNIIGTsgrdlyg 83
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLLPGADE--LVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFAEL-LWPPHCVKGT------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450  84 PLADFYREHKADPRVFWMDKRHYSAFSGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIEVVAPAVASLTP 163
Cdd:cd00431   71 EGAELVPELAPLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDE 150

                        170
                 ....*....|.
gi 881073450 164 ENHQFALNHFK 174
Cdd:cd00431  151 EDHEAALERLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 4-182 3.74e-40

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 134.07  E-value: 3.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450    4 ALISIDYTVDFVADEGKLTAGApaQAISESIAQVTQLAFDQGAYVFFAIDAHDVDDPFHPESKLFPPHNIIGTSGRDLYG 83
Cdd:pfam00857   2 ALLVIDMQNDFVDSGGPKVEGI--AAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKDRPSPAFPPGTTGAELVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450   84 PLADfyreHKADPRVfwmDKRHYSAFSGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIEVVAPAVASLTP 163
Cdd:pfam00857  80 ELAP----LPGDLVV---DKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSP 152

                         170
                  ....*....|....*....
gi 881073450  164 ENHQFALNHFKHvLGAKVV 182
Cdd:pfam00857 153 EAHDAALERLAQ-RGAEVT 170
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
103-188 8.81e-24

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 92.99  E-value: 8.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450 103 KRHYSAFSGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIEVVAPAVASLTPENHQFALNHFKHVLGAKVV 182
Cdd:COG1535  112 KWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVADFSREEHRMALEYVAGRCGVVVT 191


                 ....*.
gi 881073450 183 NEQLEE 188
Cdd:COG1535  192 TDEVLE 197
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 4-174 5.07e-17

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 75.49  E-value: 5.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450   4 ALISIDYTVDFVADeGKLtAGAPAQAISESIAQVTQ-LAFDqgaYVFFAIDAHDVD-------------DPFHPESKLFP 69
Cdd:PTZ00331  14 ALIIVDVQNDFCKG-GSL-AVPDAEEVIPVINQVRQsHHFD---LVVATQDWHPPNhisfasnhgkpkiLPDGTTQGLWP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450  70 PHNIIGTSGRDLygpladfyreHKaDPRVFWMDKR----------HYSAFSG-----TDLDIRLRERGVDTVILTGVLTD 134
Cdd:PTZ00331  89 PHCVQGTKGAQL----------HK-DLVVERIDIIirkgtnrdvdSYSAFDNdkgskTGLAQILKAHGVRRVFICGLAFD 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 881073450 135 ICVLHTAVDAYNLGYQIEVVAPAVASLTPENHQFALNHFK 174
Cdd:PTZ00331 158 FCVLFTALDAVKLGFKVVVLEDATRAVDPDAISKQRAELL 197
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 4-170 1.32e-16

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: 73.01  E-value: 1.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450   4 ALISIDYTVDFVadEGKLTAGAPAQAIsESIAQVTQLAFDQGAYVFFaIDAHDVDDPFhpesklFPPhniiGTSGRDLYG 83
Cdd:cd01014    1 ALLVIDVQNGYF--DGGLPPLNNEAAL-ENIAALIAAARAAGIPVIH-VRHIDDEGGS------FAP----GSEGWEIHP 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450  84 PLAdfyrEHKADPRVfwmDKRHYSAFSGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIEVVAPAVASLTP 163
Cdd:cd01014   67 ELA----PLEGETVI---EKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDL 139


                 ....*..
gi 881073450 164 ENHQFAL 170
Cdd:cd01014  140 PDHGGVL 146
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 2-164 1.97e-16

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: 73.45  E-value: 1.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450   2 TKALISIDYTVDFVadEGKLTAGAPAQAISESIAQVTQLAfdQGAYVFFAIDAH-----------DVDDPFHPESK---- 66
Cdd:cd01011    1 TDALLVVDVQNDFC--PGGALAVPGGDAIVPLINALLSLF--QYDLVVATQDWHpanhasfasnhPGQMPFITLPPgpqv 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450  67 LFPPHNIIGTSG----RDLYGPLADFYREHKADPrvfwmDKRHYSAF------SGTDLDIRLRERGVDTVILTGVLTDIC 136
Cdd:cd01011   77 LWPDHCVQGTPGaelhPGLPVPDIDLIVRKGTNP-----DIDSYSAFfdndrrSSTGLAEYLRERGIDRVDVVGLATDYC 151

                        170       180
                 ....*....|....*....|....*...
gi 881073450 137 VLHTAVDAYNLGYQIEVVAPAVASLTPE 164
Cdd:cd01011  152 VKATALDALKAGFEVRVLEDACRAVDPE 179
PRK11440 PRK11440
putative hydrolase; Provisional
 103-172 4.80e-16

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 72.45  E-value: 4.80e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450 103 KRHYSAFSGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIEVVAPAVASLTPENHQFALNH 172
Cdd:PRK11440 101 KRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQHQNSMNH 170
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 101-183 7.64e-15

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: 68.39  E-value: 7.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450 101 MDKRHYSAFSGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIEVVAPAVASLTPENHQFALNHFKHvLGAK 180
Cdd:cd01012   66 IEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQ-AGAV 144


                 ...
gi 881073450 181 VVN 183
Cdd:cd01012  145 LTT 147
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 4-170 1.50e-14

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: 68.20  E-value: 1.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450   4 ALISIDYTVDFvADEGKLTAGAPAQAIsESIAQVTQLAFDQGAYVFFAIDAHDVDDPFHPESKLFPPHNIIGTSGrdlyG 83
Cdd:cd01015    1 ALLVIDLVEGY-TQPGSYLAPGIAAAL-ENVQRLLAAARAAGVPVIHTTVVYDPDGADGGLWARKVPAMSDLVEG----S 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450  84 PLADFYREHKADPRVFWMDKRHYSAFSGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIEVVAPAVASLTP 163
Cdd:cd01015   75 PLAAICDELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDRAP 154


                 ....*..
gi 881073450 164 ENHQFAL 170
Cdd:cd01015  155 APHEANL 161
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 80-172 5.23e-14

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: 66.98  E-value: 5.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450  80 DLYGP-LADFYREHKADPRV------FWMDKRHYSAFSGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIE 152
Cdd:cd01013   92 DFWGPgLTASPEETKIVTELapqpddTVLTKWRYSAFKRSPLLERLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPF 171

                         90       100
                 ....*....|....*....|
gi 881073450 153 VVAPAVASLTPENHQFALNH 172
Cdd:cd01013  172 VVADAIADFSLEEHRMALKY 191
PLN02621 PLN02621
nicotinamidase
 102-170 6.35e-12

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 61.33  E-value: 6.35e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 881073450 102 DKRHYSAFSGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIEVVAPAVASLTPENHQFAL 170
Cdd:PLN02621 106 EKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATANEELHEATL 174
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
106-171 1.54e-08

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 52.30  E-value: 1.54e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 881073450 106 YSAF------SGTDLDIRLRERGVDTVILTGVLTDICVLHTAVDAYNLGYQIEVVAPAV--ASLTPENHQFALN 171
Cdd:PRK11609 119 YSAFfdnghrQKTALDDWLREHGITELIVMGLATDYCVKFTVLDALALGYQVNVITDGCrgVNLQPQDSAHAFM 192
PLN02743 PLN02743
nicotinamidase
 19-149 5.45e-07

nicotinamidase


Pssm-ID: 215396  Cd Length: 239  Bit Score: 48.20  E-value: 5.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 881073450  19 GKLTAGAPAQAISESIAQVTQLA---FDQGAYVFFAIDAHDVDDPFHPesklFPPHNIIGTSGRDLYGPLAdfYREHkaD 95
Cdd:PLN02743  45 GNLAPREPDKQISKMVDESARLArefCERKWPVLAFLDSHHPDKPEHP----YPPHCIVGTGEENLVPALQ--WLEN--D 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 881073450  96 PRVFWMDKRHYSAFSGTdldIR----------LRERGVDTVILTGVLTDICVLH---TAVDAYNLGY 149
Cdd:PLN02743 117 PNVTLRRKDCIDGFVGA---IEkdgsnvfvdwVNNNKIKVILVVGICTDICVLDfvaSALSARNHGI 180
 
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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