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Conserved domains on  [gi|1712326359|ref|WP_143716815|]
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isochorismate family cysteine hydrolase YcaC [Raoultella terrigena]

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 ...
 4-204 1.14e-174

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: 476.43  E-value: 1.14e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359   4 PYVRLDKSDAAVLLVDHQAGLLSLVRDIDPDKFKNNVLALGDMAKYFGLPTILTTSFENGPNGPLIPELKAQFPDAPYIA 83
Cdd:NF041461    1 PYKRLDKDDAAVLLVDHQTGLLSLVRDFSPDEFKNNVLALADIAKYFNLPTILTTSFEDGPNGPLVPELKEMFPDAPYIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  84 RPGNINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFNPITRDAAWDRMSQAGVQLM 163
Cdd:NF041461   81 RPGQINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSALEEGYEVFVVTDASGTFNEVTRDAAWDRMSQAGAQLM 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1712326359 164 SWFGAACELHRDWRNDVEGLGTLFSNHIPDYRNLMTSFNTL 204
Cdd:NF041461  161 NWFAVACELHRDWRNDVEGLGTLFSNHIPDYRNLMTSYAAV 201
 
Name Accession Description Interval E-value
C_hydro_YcaC NF041461
isochorismate family cysteine hydrolase YcaC; YcaC is a well-conserved cysteine hydrolase of ...
 4-204 1.14e-174

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: 476.43  E-value: 1.14e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359   4 PYVRLDKSDAAVLLVDHQAGLLSLVRDIDPDKFKNNVLALGDMAKYFGLPTILTTSFENGPNGPLIPELKAQFPDAPYIA 83
Cdd:NF041461    1 PYKRLDKDDAAVLLVDHQTGLLSLVRDFSPDEFKNNVLALADIAKYFNLPTILTTSFEDGPNGPLVPELKEMFPDAPYIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  84 RPGNINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFNPITRDAAWDRMSQAGVQLM 163
Cdd:NF041461   81 RPGQINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSALEEGYEVFVVTDASGTFNEVTRDAAWDRMSQAGAQLM 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1712326359 164 SWFGAACELHRDWRNDVEGLGTLFSNHIPDYRNLMTSFNTL 204
Cdd:NF041461  161 NWFAVACELHRDWRNDVEGLGTLFSNHIPDYRNLMTSYAAV 201
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 14-174 5.59e-71

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: 212.84  E-value: 5.59e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  14 AVLLVDHQAGLLSLVRDidPDKFKNNVLALGDMAKYFGLPTILTTSFEnGPNGPLIPELKAQFPDAPYIARPGnINAWDN 93
Cdd:cd01012     1 ALLLVDVQEKLAPAIKS--FDELINNTVKLAKAAKLLDVPVILTEQYP-KGLGPTVPELREVFPDAPVIEKTS-FSCWED 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  94 EDFVKAVKATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFNPITRDAAWDRMSQAGVQLMSWFGAACELH 173
Cdd:cd01012    77 EAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQAGAVLTTSESVLFELQ 156


                  .
gi 1712326359 174 R 174
Cdd:cd01012   157 R 157
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 14-163 1.36e-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: 115.39  E-value: 1.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  14 AVLLVDHQAGLLS--LVRDIDPDKFKNNVLALGDMAKYFGLPTILTT--------SF-----------ENGPNGPLIPEL 72
Cdd:COG1335     1 ALLVIDVQNDFVPpgALAVPGADAVVANIARLLAAARAAGVPVIHTRdwhppdgsEFaefdlwpphcvPGTPGAELVPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  73 KAQfPDAPYIARPGNiNAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFNPITRDAAW 152
Cdd:COG1335    81 APL-PGDPVVDKTRY-SAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAAL 158

                         170
                  ....*....|.
gi 1712326359 153 DRMSQAGVQLM 163
Cdd:COG1335   159 ARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 13-165 3.32e-24

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 94.01  E-value: 3.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  13 AAVLLVDHQAGLLSLVRDIDPD--KFKNNVLALGDMAKYFGLPTILTTsFENGPNGP--------------------LIP 70
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKVEGiaAILENINRLLKAARKAGIPVIFTR-QVPEPDDAdfalkdrpspafppgttgaeLVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  71 ELKAQFPDAPYIARPgnINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFNPITRDA 150
Cdd:pfam00857  80 ELAPLPGDLVVDKTR--FSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDA 157

                         170
                  ....*....|....*
gi 1712326359 151 AWDRMSQAGVQLMSW 165
Cdd:pfam00857 158 ALERLAQRGAEVTTT 172
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 101-164 1.78e-09

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 55.46  E-value: 1.78e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712326359 101 KATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFNPITRDAAWDRMSQAGVQLMS 164
Cdd:PTZ00331  142 KAHGVRRVFICGLAFDFCVLFTALDAVKLGFKVVVLEDATRAVDPDAISKQRAELLEAGVILLT 205
 
Name Accession Description Interval E-value
C_hydro_YcaC NF041461
isochorismate family cysteine hydrolase YcaC; YcaC is a well-conserved cysteine hydrolase of ...
 4-204 1.14e-174

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: 476.43  E-value: 1.14e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359   4 PYVRLDKSDAAVLLVDHQAGLLSLVRDIDPDKFKNNVLALGDMAKYFGLPTILTTSFENGPNGPLIPELKAQFPDAPYIA 83
Cdd:NF041461    1 PYKRLDKDDAAVLLVDHQTGLLSLVRDFSPDEFKNNVLALADIAKYFNLPTILTTSFEDGPNGPLVPELKEMFPDAPYIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  84 RPGNINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFNPITRDAAWDRMSQAGVQLM 163
Cdd:NF041461   81 RPGQINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSALEEGYEVFVVTDASGTFNEVTRDAAWDRMSQAGAQLM 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1712326359 164 SWFGAACELHRDWRNDVEGLGTLFSNHIPDYRNLMTSFNTL 204
Cdd:NF041461  161 NWFAVACELHRDWRNDVEGLGTLFSNHIPDYRNLMTSYAAV 201
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 14-174 5.59e-71

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: 212.84  E-value: 5.59e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  14 AVLLVDHQAGLLSLVRDidPDKFKNNVLALGDMAKYFGLPTILTTSFEnGPNGPLIPELKAQFPDAPYIARPGnINAWDN 93
Cdd:cd01012     1 ALLLVDVQEKLAPAIKS--FDELINNTVKLAKAAKLLDVPVILTEQYP-KGLGPTVPELREVFPDAPVIEKTS-FSCWED 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  94 EDFVKAVKATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFNPITRDAAWDRMSQAGVQLMSWFGAACELH 173
Cdd:cd01012    77 EAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQAGAVLTTSESVLFELQ 156


                  .
gi 1712326359 174 R 174
Cdd:cd01012   157 R 157
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 14-163 1.36e-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: 115.39  E-value: 1.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  14 AVLLVDHQAGLLS--LVRDIDPDKFKNNVLALGDMAKYFGLPTILTT--------SF-----------ENGPNGPLIPEL 72
Cdd:COG1335     1 ALLVIDVQNDFVPpgALAVPGADAVVANIARLLAAARAAGVPVIHTRdwhppdgsEFaefdlwpphcvPGTPGAELVPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  73 KAQfPDAPYIARPGNiNAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFNPITRDAAW 152
Cdd:COG1335    81 APL-PGDPVVDKTRY-SAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAAL 158

                         170
                  ....*....|.
gi 1712326359 153 DRMSQAGVQLM 163
Cdd:COG1335   159 ARLRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 14-155 5.32e-30

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: 108.51  E-value: 5.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  14 AVLLVDHQAGLLSLVRDIDP--DKFKNNVLALGDMAKYFGLPTILTTSF------------------ENGPNGPLIPELK 73
Cdd:cd00431     1 ALLVVDMQNDFVPGGGLLLPgaDELVPNINRLLAAARAAGIPVIFTRDWhppddpefaellwpphcvKGTEGAELVPELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  74 AQfPDAPYIARpGNINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFNPITRDAAWD 153
Cdd:cd00431    81 PL-PDDLVIEK-TRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAALE 158


                  ..
gi 1712326359 154 RM 155
Cdd:cd00431   159 RL 160
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 13-165 3.32e-24

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 94.01  E-value: 3.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  13 AAVLLVDHQAGLLSLVRDIDPD--KFKNNVLALGDMAKYFGLPTILTTsFENGPNGP--------------------LIP 70
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKVEGiaAILENINRLLKAARKAGIPVIFTR-QVPEPDDAdfalkdrpspafppgttgaeLVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  71 ELKAQFPDAPYIARPgnINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFNPITRDA 150
Cdd:pfam00857  80 ELAPLPGDLVVDKTR--FSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDA 157

                         170
                  ....*....|....*
gi 1712326359 151 AWDRMSQAGVQLMSW 165
Cdd:pfam00857 158 ALERLAQRGAEVTTT 172
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 14-143 1.64e-12

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: 62.61  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  14 AVLLVDHQAGLLSLVRDI-DPDKFKNNVLALGDMAKYFGLPTIL-------TTSFENG-PNGPLIPELKAQfPDAPYI-- 82
Cdd:cd01014     1 ALLVIDVQNGYFDGGLPPlNNEAALENIAALIAAARAAGIPVIHvrhiddeGGSFAPGsEGWEIHPELAPL-EGETVIek 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712326359  83 ARPgniNAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTF 143
Cdd:cd01014    80 TVP---NAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATF 137
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 73-163 9.42e-11

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: 58.43  E-value: 9.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359  73 KAQFPD-APYIARPGNINAwDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFNPITRDAA 151
Cdd:cd01011   106 KGTNPDiDSYSAFFDNDRR-SSTGLAEYLRERGIDRVDVVGLATDYCVKATALDALKAGFEVRVLEDACRAVDPETIERA 184

                          90
                  ....*....|..
gi 1712326359 152 WDRMSQAGVQLM 163
Cdd:cd01011   185 IEEMKEAGVVLV 196
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 101-164 1.78e-09

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 55.46  E-value: 1.78e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712326359 101 KATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFNPITRDAAWDRMSQAGVQLMS 164
Cdd:PTZ00331  142 KAHGVRRVFICGLAFDFCVLFTALDAVKLGFKVVVLEDATRAVDPDAISKQRAELLEAGVILLT 205
PLN02621 PLN02621
nicotinamidase
 9-144 3.44e-09

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 54.40  E-value: 3.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712326359   9 DKSDAAVLLVDHQAGLLSLVRDIDPdkfknNVLALGDMAKYFGLPTILTTSFENGP----------NGPLI------PEL 72
Cdd:PLN02621   17 DPKQAALLVIDMQNYFSSMAEPILP-----ALLTTIDLCRRASIPVFFTRHSHKSPsdygmlgewwDGDLIldgtteAEL 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712326359  73 kaqFPDAPYIARPGNI------NAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFN 144
Cdd:PLN02621   92 ---MPEIGRVTGPDEVvekstySAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATAN 166
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
101-164 2.35e-05

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 43.44  E-value: 2.35e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712326359 101 KATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFN--PITRDAAWDRMSQAGVQLMS 164
Cdd:PRK11609  138 REHGITELIVMGLATDYCVKFTVLDALALGYQVNVITDGCRGVNlqPQDSAHAFMEMSAAGATLYT 203
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
101-151 6.85e-04

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 39.06  E-value: 6.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1712326359 101 KATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASGTFNPITRDAA 151
Cdd:COG1535   128 RELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVADFSREEHRMA 178
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 101-141 7.24e-03

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: 35.84  E-value: 7.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1712326359 101 KATGKKQLIIAGVVTEVCVAFPALSAIEEGFDVFVITDASG 141
Cdd:cd01015   110 TARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVG 150
 
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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