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Conserved domains on  [gi|939207352|gb|ALJ65448|]
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arginase [Vibrio cholerae O1 str. KW3]

Protein Classification

arginase family protein( domain architecture ID 98571)

arginase family protein is a metal-dependent enzyme that catalyzes the hydrolysis of an amide bond, such as arginase-like amidino hydrolases and histone/histone-like deacetylases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Arginase_HDAC super family cl17011
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
52-245 2.33e-07

Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily includes metal-dependent enzymes that belong to Arginase-like amidino hydrolase family and histone/histone-like deacetylase class I, II, IV family, respectively. These enzymes catalyze hydrolysis of amide bond. Arginases are known to be involved in control of cellular levels of arginine and ornithine, in histidine and arginine degradation and in clavulanic acid biosynthesis. Deacetylases play a role in signal transduction through histone and/or other protein modification and can repress/activate transcription of a number of different genes. They participate in different cellular processes including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. Mammalian histone deacetyases are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.


The actual alignment was detected with superfamily member cd09988:

Pssm-ID: 450134 [Multi-domain]  Cd Length: 262  Bit Score: 50.59  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939207352  52 LYQQQSTPKYADASHYVLDG----QTQAKYQQALNQSVALGVIPVAFANCHEILLHSLPALTQ-DGASVGMV-------- 118
Cdd:cd09988   34 LPPGNWGLKIYDLGDIICDGdsleDTQQALAEVVAELLKKGIIPIVIGGGHDLAYGHYRGLDKaLEKKIGIInfdahfdl 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939207352 119 -------HIGHGFelKQTLDLQVGSAFHFalsrfaqaklFCIGIDTEHTHAQTLEYAEDLGCDWVSHEECGFLNRTQLKA 191
Cdd:cd09988  114 rpleegrHSGTPF--RQILEECPNNLFNY----------SVLGIQEYYNTQELFDLAKELGVLYFEAERLLGEKILDILE 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939207352 192 QLsgyIEHCEQLVINIDL----ASLVPG------NGLethkvlDNQVVLRVLRQMILSGKVRYI 245
Cdd:cd09988  182 AE---PALRDAIYLSIDLdvisSSDAPGvsapspNGL------SPEEACAIARYAGKSGKVRSF 236
 
Name Accession Description Interval E-value
Formimidoylglutamase cd09988
Formimidoylglutamase or HutE; Formimidoylglutamase (N-formimidoyl-L-glutamate ...
52-245 2.33e-07

Formimidoylglutamase or HutE; Formimidoylglutamase (N-formimidoyl-L-glutamate formimidoylhydrolase; formiminoglutamase; N-formiminoglutamate hydrolase; N-formimino-L-glutamate formiminohydrolase; HutE; EC 3.5.3.8) is a metalloenzyme that catalyzes hydrolysis of N-formimidoyl-L-glutamate to L-glutamate and formamide. This enzyme is involved in histidine degradation, requiring Mn as a cofactor while glutathione may be required for maximal activity. In Pseudomonas PAO1, mutation studies show that histidine degradation proceeds via a 'four-step' pathway if the 'five-step' route is absent and vice versa; in the four-step pathway, formiminoglutaminase (HutE, EC 3.5.3.8) directly converts formiminoglutamate (FIGLU) to L-glutamate and formamide in a single step. Formiminoglutamase has traditionally also been referred to as HutG; however, formiminoglutamase is structurally and mechanistically unrelated to N-formyl-glutamate deformylase (also called HutG). Phylogenetic analysis has suggested that HutE was acquired by horizontal gene transfer from a Ralstonia-like ancestor.


Pssm-ID: 212514 [Multi-domain]  Cd Length: 262  Bit Score: 50.59  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939207352  52 LYQQQSTPKYADASHYVLDG----QTQAKYQQALNQSVALGVIPVAFANCHEILLHSLPALTQ-DGASVGMV-------- 118
Cdd:cd09988   34 LPPGNWGLKIYDLGDIICDGdsleDTQQALAEVVAELLKKGIIPIVIGGGHDLAYGHYRGLDKaLEKKIGIInfdahfdl 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939207352 119 -------HIGHGFelKQTLDLQVGSAFHFalsrfaqaklFCIGIDTEHTHAQTLEYAEDLGCDWVSHEECGFLNRTQLKA 191
Cdd:cd09988  114 rpleegrHSGTPF--RQILEECPNNLFNY----------SVLGIQEYYNTQELFDLAKELGVLYFEAERLLGEKILDILE 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939207352 192 QLsgyIEHCEQLVINIDL----ASLVPG------NGLethkvlDNQVVLRVLRQMILSGKVRYI 245
Cdd:cd09988  182 AE---PALRDAIYLSIDLdvisSSDAPGvsapspNGL------SPEEACAIARYAGKSGKVRSF 236
SpeB COG0010
Arginase/agmatinase family enzyme [Amino acid transport and metabolism]; Arginase/agmatinase ...
72-243 2.08e-05

Arginase/agmatinase family enzyme [Amino acid transport and metabolism]; Arginase/agmatinase family enzyme is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 439781 [Multi-domain]  Cd Length: 283  Bit Score: 44.82  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939207352  72 QTQAKYQQALNQSVALGVIPVAFANCHEILLHSLPALTQDGASVGMVHI-GHgfelkqtLDLQV--------GSAFHFAL 142
Cdd:COG0010   74 ETLAALAEAVAELLAAGKFPIVLGGDHSITLGTIRALARAYGPLGVIHFdAH-------ADLRDpyegnlshGTPLRRAL 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939207352 143 --SRFAQAKLFCIGIDTehTHAQTLEYAEDLGCDWVSHEECGFLNRTQLKAQLSGYIEHCEQLVINIDL----ASLVPG- 215
Cdd:COG0010  147 eeGLLDPENVVQIGIRS--NDPEEFELARELGVTVFTAREIRERGLAAVLEEALERLRAGDPVYVSFDIdvldPAFAPGv 224
                        170       180       190
                 ....*....|....*....|....*....|...
gi 939207352 216 -----NGLETHkvldnqVVLRVLRQMILSGKVR 243
Cdd:COG0010  225 gtpepGGLTPR------EALELLRALAASGKVV 251
 
Name Accession Description Interval E-value
Formimidoylglutamase cd09988
Formimidoylglutamase or HutE; Formimidoylglutamase (N-formimidoyl-L-glutamate ...
52-245 2.33e-07

Formimidoylglutamase or HutE; Formimidoylglutamase (N-formimidoyl-L-glutamate formimidoylhydrolase; formiminoglutamase; N-formiminoglutamate hydrolase; N-formimino-L-glutamate formiminohydrolase; HutE; EC 3.5.3.8) is a metalloenzyme that catalyzes hydrolysis of N-formimidoyl-L-glutamate to L-glutamate and formamide. This enzyme is involved in histidine degradation, requiring Mn as a cofactor while glutathione may be required for maximal activity. In Pseudomonas PAO1, mutation studies show that histidine degradation proceeds via a 'four-step' pathway if the 'five-step' route is absent and vice versa; in the four-step pathway, formiminoglutaminase (HutE, EC 3.5.3.8) directly converts formiminoglutamate (FIGLU) to L-glutamate and formamide in a single step. Formiminoglutamase has traditionally also been referred to as HutG; however, formiminoglutamase is structurally and mechanistically unrelated to N-formyl-glutamate deformylase (also called HutG). Phylogenetic analysis has suggested that HutE was acquired by horizontal gene transfer from a Ralstonia-like ancestor.


Pssm-ID: 212514 [Multi-domain]  Cd Length: 262  Bit Score: 50.59  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939207352  52 LYQQQSTPKYADASHYVLDG----QTQAKYQQALNQSVALGVIPVAFANCHEILLHSLPALTQ-DGASVGMV-------- 118
Cdd:cd09988   34 LPPGNWGLKIYDLGDIICDGdsleDTQQALAEVVAELLKKGIIPIVIGGGHDLAYGHYRGLDKaLEKKIGIInfdahfdl 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939207352 119 -------HIGHGFelKQTLDLQVGSAFHFalsrfaqaklFCIGIDTEHTHAQTLEYAEDLGCDWVSHEECGFLNRTQLKA 191
Cdd:cd09988  114 rpleegrHSGTPF--RQILEECPNNLFNY----------SVLGIQEYYNTQELFDLAKELGVLYFEAERLLGEKILDILE 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939207352 192 QLsgyIEHCEQLVINIDL----ASLVPG------NGLethkvlDNQVVLRVLRQMILSGKVRYI 245
Cdd:cd09988  182 AE---PALRDAIYLSIDLdvisSSDAPGvsapspNGL------SPEEACAIARYAGKSGKVRSF 236
SpeB COG0010
Arginase/agmatinase family enzyme [Amino acid transport and metabolism]; Arginase/agmatinase ...
72-243 2.08e-05

Arginase/agmatinase family enzyme [Amino acid transport and metabolism]; Arginase/agmatinase family enzyme is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 439781 [Multi-domain]  Cd Length: 283  Bit Score: 44.82  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939207352  72 QTQAKYQQALNQSVALGVIPVAFANCHEILLHSLPALTQDGASVGMVHI-GHgfelkqtLDLQV--------GSAFHFAL 142
Cdd:COG0010   74 ETLAALAEAVAELLAAGKFPIVLGGDHSITLGTIRALARAYGPLGVIHFdAH-------ADLRDpyegnlshGTPLRRAL 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939207352 143 --SRFAQAKLFCIGIDTehTHAQTLEYAEDLGCDWVSHEECGFLNRTQLKAQLSGYIEHCEQLVINIDL----ASLVPG- 215
Cdd:COG0010  147 eeGLLDPENVVQIGIRS--NDPEEFELARELGVTVFTAREIRERGLAAVLEEALERLRAGDPVYVSFDIdvldPAFAPGv 224
                        170       180       190
                 ....*....|....*....|....*....|...
gi 939207352 216 -----NGLETHkvldnqVVLRVLRQMILSGKVR 243
Cdd:COG0010  225 gtpepGGLTPR------EALELLRALAASGKVV 251
 
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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