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Conserved domains on  [gi|495001668|ref|WP_007727682|]
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isochorismate family cysteine hydrolase YcaC [Brevibacillus sp. BC25]

Protein Classification

hydrolase( domain architecture ID 10099061)

putative YcaC-like hydrolase with unknown specificity

CATH:  3.40.50.850
Gene Ontology:  GO:0016787
PubMed:  9782055
SCOP:  4000591

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C_hydro_YcaC NF041461
isochorismate family cysteine hydrolase YcaC; YcaC is a well-conserved cysteine hydrolase of ...
 4-205 5.20e-154

isochorismate family cysteine hydrolase YcaC; YcaC is a well-conserved cysteine hydrolase of unknown function, found in both Pseudomonas aeruginosa and Escherichia coli K-12, with an isochorismate family crystal structure.


:

Pssm-ID: 469349  Cd Length: 201  Bit Score: 424.42  E-value: 5.20e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668   4 LYSRISKNDAAVLLIDHQTGLISgLVRDYGVDEFKNNVLALAKTAKFFNLPVILTTSFESGPNGPLIRELVELFPDASKI 83
Cdd:NF041461   1 PYKRLDKDDAAVLLVDHQTGLLS-LVRDFSPDEFKNNVLALADIAKYFNLPTILTTSFEDGPNGPLVPELKEMFPDAPYI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  84 ARPGQINAWDNEDFVKAIQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTFSKQVAEASLMRMAHAGAQL 163
Cdd:NF041461  80 ARPGQINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSALEEGYEVFVVTDASGTFNEVTRDAAWDRMSQAGAQL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 495001668 164 MNWFSVACELQRDWRNDVEGFGALLAAHLPGYQNVIESYQAQ 205
Cdd:NF041461 160 MNWFAVACELHRDWRNDVEGLGTLFSNHIPDYRNLMTSYAAV 201
 
Name Accession Description Interval E-value
C_hydro_YcaC NF041461
isochorismate family cysteine hydrolase YcaC; YcaC is a well-conserved cysteine hydrolase of ...
 4-205 5.20e-154

isochorismate family cysteine hydrolase YcaC; YcaC is a well-conserved cysteine hydrolase of unknown function, found in both Pseudomonas aeruginosa and Escherichia coli K-12, with an isochorismate family crystal structure.


Pssm-ID: 469349  Cd Length: 201  Bit Score: 424.42  E-value: 5.20e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668   4 LYSRISKNDAAVLLIDHQTGLISgLVRDYGVDEFKNNVLALAKTAKFFNLPVILTTSFESGPNGPLIRELVELFPDASKI 83
Cdd:NF041461   1 PYKRLDKDDAAVLLVDHQTGLLS-LVRDFSPDEFKNNVLALADIAKYFNLPTILTTSFEDGPNGPLVPELKEMFPDAPYI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  84 ARPGQINAWDNEDFVKAIQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTFSKQVAEASLMRMAHAGAQL 163
Cdd:NF041461  80 ARPGQINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSALEEGYEVFVVTDASGTFNEVTRDAAWDRMSQAGAQL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 495001668 164 MNWFSVACELQRDWRNDVEGFGALLAAHLPGYQNVIESYQAQ 205
Cdd:NF041461 160 MNWFAVACELHRDWRNDVEGLGTLFSNHIPDYRNLMTSYAAV 201
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 14-175 5.62e-64

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: 195.12  E-value: 5.62e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  14 AVLLIDHQTGLISGLVRdygVDEFKNNVLALAKTAKFFNLPVILTTSFESGpNGPLIRELVELFPDASKIARPGqINAWD 93
Cdd:cd01012    1 ALLLVDVQEKLAPAIKS---FDELINNTVKLAKAAKLLDVPVILTEQYPKG-LGPTVPELREVFPDAPVIEKTS-FSCWE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  94 NEDFVKAIQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTFSKQVAEASLMRMAHAGAQLMNWFSVACEL 173
Cdd:cd01012   76 DEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQAGAVLTTSESVLFEL 155


                 ..
gi 495001668 174 QR 175
Cdd:cd01012  156 QR 157
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 14-164 2.76e-32

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: 114.62  E-value: 2.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  14 AVLLIDHQTGLIS-GLVRDYGVDEFKNNVLALAKTAKFFNLPVILTTsFESGPNGPLIRELvELFPDASKIARPG----- 87
Cdd:COG1335    1 ALLVIDVQNDFVPpGALAVPGADAVVANIARLLAAARAAGVPVIHTR-DWHPPDGSEFAEF-DLWPPHCVPGTPGaelvp 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  88 --------------QINAWDNEDFVKAIQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTFSKQVAEASL 153
Cdd:COG1335   79 elaplpgdpvvdktRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAAL 158

                        170
                 ....*....|.
gi 495001668 154 MRMAHAGAQLM 164
Cdd:COG1335  159 ARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 13-166 5.95e-24

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 93.24  E-value: 5.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668   13 AAVLLIDHQTGLISGLVRD-YGVDEFKNNVLALAKTAKFFNLPVILTT------------------SFESGPNGPLIREL 73
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKvEGIAAILENINRLLKAARKAGIPVIFTRqvpepddadfalkdrpspAFPPGTTGAELVPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668   74 VELFPDASKIARPGqINAWDNEDFVKAIQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTFSKQVAEASL 153
Cdd:pfam00857  81 LAPLPGDLVVDKTR-FSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAAL 159

                         170
                  ....*....|...
gi 495001668  154 MRMAHAGAQLMNW 166
Cdd:pfam00857 160 ERLAQRGAEVTTT 172
PLN02621 PLN02621
nicotinamidase
 13-165 6.72e-12

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 61.72  E-value: 6.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  13 AAVLLIDHQtGLISGLVRdygvdEFKNNVLALAKTAKFFNLPVILTTSFESGP----------NGPLIRE---LVELFPD 79
Cdd:PLN02621  21 AALLVIDMQ-NYFSSMAE-----PILPALLTTIDLCRRASIPVFFTRHSHKSPsdygmlgewwDGDLILDgttEAELMPE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  80 ASKIARPGQI------NAWDNEDFVKAIQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTFSKQVAEASL 153
Cdd:PLN02621  95 IGRVTGPDEVvekstySAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATANEELHEATL 174

                        170
                 ....*....|..
gi 495001668 154 MRMAHAGAQLMN 165
Cdd:PLN02621 175 KNLAYGFAYLVD 186
 
Name Accession Description Interval E-value
C_hydro_YcaC NF041461
isochorismate family cysteine hydrolase YcaC; YcaC is a well-conserved cysteine hydrolase of ...
 4-205 5.20e-154

isochorismate family cysteine hydrolase YcaC; YcaC is a well-conserved cysteine hydrolase of unknown function, found in both Pseudomonas aeruginosa and Escherichia coli K-12, with an isochorismate family crystal structure.


Pssm-ID: 469349  Cd Length: 201  Bit Score: 424.42  E-value: 5.20e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668   4 LYSRISKNDAAVLLIDHQTGLISgLVRDYGVDEFKNNVLALAKTAKFFNLPVILTTSFESGPNGPLIRELVELFPDASKI 83
Cdd:NF041461   1 PYKRLDKDDAAVLLVDHQTGLLS-LVRDFSPDEFKNNVLALADIAKYFNLPTILTTSFEDGPNGPLVPELKEMFPDAPYI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  84 ARPGQINAWDNEDFVKAIQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTFSKQVAEASLMRMAHAGAQL 163
Cdd:NF041461  80 ARPGQINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSALEEGYEVFVVTDASGTFNEVTRDAAWDRMSQAGAQL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 495001668 164 MNWFSVACELQRDWRNDVEGFGALLAAHLPGYQNVIESYQAQ 205
Cdd:NF041461 160 MNWFAVACELHRDWRNDVEGLGTLFSNHIPDYRNLMTSYAAV 201
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 14-175 5.62e-64

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: 195.12  E-value: 5.62e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  14 AVLLIDHQTGLISGLVRdygVDEFKNNVLALAKTAKFFNLPVILTTSFESGpNGPLIRELVELFPDASKIARPGqINAWD 93
Cdd:cd01012    1 ALLLVDVQEKLAPAIKS---FDELINNTVKLAKAAKLLDVPVILTEQYPKG-LGPTVPELREVFPDAPVIEKTS-FSCWE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  94 NEDFVKAIQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTFSKQVAEASLMRMAHAGAQLMNWFSVACEL 173
Cdd:cd01012   76 DEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQAGAVLTTSESVLFEL 155


                 ..
gi 495001668 174 QR 175
Cdd:cd01012  156 QR 157
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 14-164 2.76e-32

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: 114.62  E-value: 2.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  14 AVLLIDHQTGLIS-GLVRDYGVDEFKNNVLALAKTAKFFNLPVILTTsFESGPNGPLIRELvELFPDASKIARPG----- 87
Cdd:COG1335    1 ALLVIDVQNDFVPpGALAVPGADAVVANIARLLAAARAAGVPVIHTR-DWHPPDGSEFAEF-DLWPPHCVPGTPGaelvp 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  88 --------------QINAWDNEDFVKAIQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTFSKQVAEASL 153
Cdd:COG1335   79 elaplpgdpvvdktRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAAL 158

                        170
                 ....*....|.
gi 495001668 154 MRMAHAGAQLM 164
Cdd:COG1335  159 ARLRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 14-157 3.32e-31

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: 111.59  E-value: 3.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  14 AVLLIDHQTGLIS-GLVRDYGVDEFKNNVLALAKTAKFFNLPVILTTSF------------------ESGPNGPLIRELv 74
Cdd:cd00431    1 ALLVVDMQNDFVPgGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWhppddpefaellwpphcvKGTEGAELVPEL- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  75 ELFPDASKIARpGQINAWDNEDFVKAIQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTFSKQVAEASLM 154
Cdd:cd00431   80 APLPDDLVIEK-TRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAALE 158


                 ...
gi 495001668 155 RMA 157
Cdd:cd00431  159 RLA 161
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 13-166 5.95e-24

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 93.24  E-value: 5.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668   13 AAVLLIDHQTGLISGLVRD-YGVDEFKNNVLALAKTAKFFNLPVILTT------------------SFESGPNGPLIREL 73
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKvEGIAAILENINRLLKAARKAGIPVIFTRqvpepddadfalkdrpspAFPPGTTGAELVPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668   74 VELFPDASKIARPGqINAWDNEDFVKAIQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTFSKQVAEASL 153
Cdd:pfam00857  81 LAPLPGDLVVDKTR-FSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAAL 159

                         170
                  ....*....|...
gi 495001668  154 MRMAHAGAQLMNW 166
Cdd:pfam00857 160 ERLAQRGAEVTTT 172
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 14-144 6.26e-14

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: 66.46  E-value: 6.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  14 AVLLIDHQTGLISGLVRDYGVDEFKNNVLALAKTAKFFNLPVIL-------TTSFESGpngpliRELVELFPDASkiARP 86
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHvrhiddeGGSFAPG------SEGWEIHPELA--PLE 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495001668  87 GQI-------NAWDNEDFVKAIQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTF 144
Cdd:cd01014   73 GETviektvpNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATF 137
PLN02621 PLN02621
nicotinamidase
 13-165 6.72e-12

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 61.72  E-value: 6.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  13 AAVLLIDHQtGLISGLVRdygvdEFKNNVLALAKTAKFFNLPVILTTSFESGP----------NGPLIRE---LVELFPD 79
Cdd:PLN02621  21 AALLVIDMQ-NYFSSMAE-----PILPALLTTIDLCRRASIPVFFTRHSHKSPsdygmlgewwDGDLILDgttEAELMPE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  80 ASKIARPGQI------NAWDNEDFVKAIQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTFSKQVAEASL 153
Cdd:PLN02621  95 IGRVTGPDEVvekstySAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATANEELHEATL 174

                        170
                 ....*....|..
gi 495001668 154 MRMAHAGAQLMN 165
Cdd:PLN02621 175 KNLAYGFAYLVD 186
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 105-164 2.05e-10

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: 57.66  E-value: 2.05e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668 105 GKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTFSKQVAEASLMRMAHAGAQLM 164
Cdd:cd01011  137 GIDRVDVVGLATDYCVKATALDALKAGFEVRVLEDACRAVDPETIERAIEEMKEAGVVLV 196
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 96-165 3.89e-08

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 51.61  E-value: 3.89e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  96 DFVKAIQATgkkQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGTFSKQVAEASLMRMAHAGAQLMN 165
Cdd:PTZ00331 139 QILKAHGVR---RVFICGLAFDFCVLFTALDAVKLGFKVVVLEDATRAVDPDAISKQRAELLEAGVILLT 205
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
13-158 1.50e-07

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 49.85  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  13 AAVLLIDHQTGLisglVRDYGVD-----EFKNNVLALAKTAKFFNLPVILT------TSFESG----------PNGPLIR 71
Cdd:COG1535   20 AALLIHDMQNYF----LRPYDPDeppirELVANIARLRDACRAAGIPVVYTaqpgdqTPEDRGllndfwgpglTAGPEGQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  72 ELV-ELFPdaskiaRPGQI-------NAWDNEDFVKAIQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDASGT 143
Cdd:COG1535   96 EIVdELAP------APGDTvltkwrySAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVAD 169

                        170
                 ....*....|....*
gi 495001668 144 FSKQVAEASLMRMAH 158
Cdd:COG1535  170 FSREEHRMALEYVAG 184
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
101-164 3.54e-07

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 48.83  E-value: 3.54e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495001668 101 IQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTDA-SGT-FSKQVAEASLMRMAHAGAQLM 164
Cdd:PRK11609 137 LREHGITELIVMGLATDYCVKFTVLDALALGYQVNVITDGcRGVnLQPQDSAHAFMEMSAAGATLY 202
isochorismatase cd01013
Isochorismatase, also known as 2,3 dihydro-2,3 dihydroxybenzoate synthase, catalyses the ...
 14-146 7.76e-04

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: 38.86  E-value: 7.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  14 AVLLI-----------DHQTGLISGLVRdygvdefknNVLALAKTAKFFNLPVILT--------------TSFeSGP--- 65
Cdd:cd01013   30 AVLLVhdmqryfldfyDESAEPVPQLIA---------NIARLRDWCRQAGIPVVYTaqpgnqtpeqrallNDF-WGPglt 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495001668  66 NGPLIRELV-ELFPDASKIarpgQINAWDNEDFVKA-----IQATGKKQLIIAGVVTDVCVSFPALSALHAGYEAFVVTD 139
Cdd:cd01013  100 ASPEETKIVtELAPQPDDT----VLTKWRYSAFKRSpllerLKESGRDQLIITGVYAHIGCLSTAVDAFMRDIQPFVVAD 175


                 ....*..
gi 495001668 140 ASGTFSK 146
Cdd:cd01013  176 AIADFSL 182
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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