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Conserved domains on  [gi|736501793|ref|WP_034517935|]
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N-formylglutamate amidohydrolase [Rhizobium rhizogenes]

Protein Classification

N-formylglutamate amidohydrolase( domain architecture ID 10008145)

N-formylglutamate amidohydrolase (FGase) catalyzes the terminal reaction in the five-step pathway for histidine utilization, the hydrolysis of N-formyl-L-glutamate to produce L-glutamate plus formate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HutG2 COG3931
Predicted N-formylglutamate amidohydrolase [Amino acid transport and metabolism];
8-255 4.84e-129

Predicted N-formylglutamate amidohydrolase [Amino acid transport and metabolism];


:

Pssm-ID: 443132  Cd Length: 252  Bit Score: 365.24  E-value: 4.84e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793   8 LTEADGECVAVERPDGKSPFFIICEHASRRLPERFGDLGLSPEALSSHIAWDPGALAVARKISDSLDATLVHQRFSRLIY 87
Cdd:COG3931    3 LAPDDPAPVEVINPDGRSPVLLVCDHASNAVPAALGDLGLPAADLERHIAWDIGAAGVARALAERLDAPLVLSRYSRLVI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793  88 DCNRPPESAGAMPEISEIYTIPGNQHLRAADREARTEALYIPFHNRIQALLKERANSGQKTVIVTVHSFTSVYNGKPRAV 167
Cdd:COG3931   83 DCNRPPDDPTLIPELSDGTVIPGNRGLSAAERAARLAAIYRPYHDAIAALLAARLARGRPPVIVSIHSFTPVYKGVPRPW 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793 168 ELGILHDDDRWLADRMLDAAAEAPLYRTERNEPYGPEDGVTHTLKLHGIANGLHNVMIEVRNDLIVDDVGQEVVADYLTG 247
Cdd:COG3931  163 HIGILHDRDPRLADPLLAALRAEGDLVVGDNEPYSGADGVDYTLDRHAEARGLPNVLIEIRQDLIADEAGQAAWAERLAR 242

                 ....*...
gi 736501793 248 LLQSSLEA 255
Cdd:COG3931  243 LLRAALAA 250
 
Name Accession Description Interval E-value
HutG2 COG3931
Predicted N-formylglutamate amidohydrolase [Amino acid transport and metabolism];
8-255 4.84e-129

Predicted N-formylglutamate amidohydrolase [Amino acid transport and metabolism];


Pssm-ID: 443132  Cd Length: 252  Bit Score: 365.24  E-value: 4.84e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793   8 LTEADGECVAVERPDGKSPFFIICEHASRRLPERFGDLGLSPEALSSHIAWDPGALAVARKISDSLDATLVHQRFSRLIY 87
Cdd:COG3931    3 LAPDDPAPVEVINPDGRSPVLLVCDHASNAVPAALGDLGLPAADLERHIAWDIGAAGVARALAERLDAPLVLSRYSRLVI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793  88 DCNRPPESAGAMPEISEIYTIPGNQHLRAADREARTEALYIPFHNRIQALLKERANSGQKTVIVTVHSFTSVYNGKPRAV 167
Cdd:COG3931   83 DCNRPPDDPTLIPELSDGTVIPGNRGLSAAERAARLAAIYRPYHDAIAALLAARLARGRPPVIVSIHSFTPVYKGVPRPW 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793 168 ELGILHDDDRWLADRMLDAAAEAPLYRTERNEPYGPEDGVTHTLKLHGIANGLHNVMIEVRNDLIVDDVGQEVVADYLTG 247
Cdd:COG3931  163 HIGILHDRDPRLADPLLAALRAEGDLVVGDNEPYSGADGVDYTLDRHAEARGLPNVLIEIRQDLIADEAGQAAWAERLAR 242

                 ....*...
gi 736501793 248 LLQSSLEA 255
Cdd:COG3931  243 LLRAALAA 250
FGase pfam05013
N-formylglutamate amidohydrolase; Formylglutamate amidohydrolase (FGase) catalyzes the ...
25-232 1.62e-50

N-formylglutamate amidohydrolase; Formylglutamate amidohydrolase (FGase) catalyzes the terminal reaction in the five-step pathway for histidine utilization in Pseudomonas putida. By this action, N-formyl-L-glutamate (FG) is hydrolysed to produce L-glutamate plus formate.


Pssm-ID: 461519  Cd Length: 219  Bit Score: 164.67  E-value: 1.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793   25 SPFFIICEHASRRLPERFGDlGLSPEALSSHIAWDPGALAVARKISDsLDATLVHQRFSRLIYDCNRPP-ESAGAMPEIS 103
Cdd:pfam05013   1 SPLLLSSPHAGTAIPPDLGA-GLALDEAELHIAEDWHVDELYAFAPA-LGASLLVARFSRLVIDLNRPPdDLDPYMPVQS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793  104 EIYTIPGN---------QHLRAADREARTEALYIPFHNRIQALLKERANSGQKTVIVTVHSFTSV---YNGKPRA-VELG 170
Cdd:pfam05013  79 GLGLIPRNtfdgepiydRPLDAAERAARIERYYRPYHAALAALLARLRARHGPAVLIDCHSMPSRgprLFGGPRPdIVLG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736501793  171 ILHD--DDRWLADRMLDAAAEAPlYRTERNEPYgpeDGVTHTLKLHGIANGLHNVMIEVRNDLI 232
Cdd:pfam05013 159 TRYGasCDPRLADALLAALEAAG-YSVGRNEPY---AGGYITRHYGRPARGVHAVQIEIRRDLY 218
 
Name Accession Description Interval E-value
HutG2 COG3931
Predicted N-formylglutamate amidohydrolase [Amino acid transport and metabolism];
8-255 4.84e-129

Predicted N-formylglutamate amidohydrolase [Amino acid transport and metabolism];


Pssm-ID: 443132  Cd Length: 252  Bit Score: 365.24  E-value: 4.84e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793   8 LTEADGECVAVERPDGKSPFFIICEHASRRLPERFGDLGLSPEALSSHIAWDPGALAVARKISDSLDATLVHQRFSRLIY 87
Cdd:COG3931    3 LAPDDPAPVEVINPDGRSPVLLVCDHASNAVPAALGDLGLPAADLERHIAWDIGAAGVARALAERLDAPLVLSRYSRLVI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793  88 DCNRPPESAGAMPEISEIYTIPGNQHLRAADREARTEALYIPFHNRIQALLKERANSGQKTVIVTVHSFTSVYNGKPRAV 167
Cdd:COG3931   83 DCNRPPDDPTLIPELSDGTVIPGNRGLSAAERAARLAAIYRPYHDAIAALLAARLARGRPPVIVSIHSFTPVYKGVPRPW 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793 168 ELGILHDDDRWLADRMLDAAAEAPLYRTERNEPYGPEDGVTHTLKLHGIANGLHNVMIEVRNDLIVDDVGQEVVADYLTG 247
Cdd:COG3931  163 HIGILHDRDPRLADPLLAALRAEGDLVVGDNEPYSGADGVDYTLDRHAEARGLPNVLIEIRQDLIADEAGQAAWAERLAR 242

                 ....*...
gi 736501793 248 LLQSSLEA 255
Cdd:COG3931  243 LLRAALAA 250
FGase pfam05013
N-formylglutamate amidohydrolase; Formylglutamate amidohydrolase (FGase) catalyzes the ...
25-232 1.62e-50

N-formylglutamate amidohydrolase; Formylglutamate amidohydrolase (FGase) catalyzes the terminal reaction in the five-step pathway for histidine utilization in Pseudomonas putida. By this action, N-formyl-L-glutamate (FG) is hydrolysed to produce L-glutamate plus formate.


Pssm-ID: 461519  Cd Length: 219  Bit Score: 164.67  E-value: 1.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793   25 SPFFIICEHASRRLPERFGDlGLSPEALSSHIAWDPGALAVARKISDsLDATLVHQRFSRLIYDCNRPP-ESAGAMPEIS 103
Cdd:pfam05013   1 SPLLLSSPHAGTAIPPDLGA-GLALDEAELHIAEDWHVDELYAFAPA-LGASLLVARFSRLVIDLNRPPdDLDPYMPVQS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793  104 EIYTIPGN---------QHLRAADREARTEALYIPFHNRIQALLKERANSGQKTVIVTVHSFTSV---YNGKPRA-VELG 170
Cdd:pfam05013  79 GLGLIPRNtfdgepiydRPLDAAERAARIERYYRPYHAALAALLARLRARHGPAVLIDCHSMPSRgprLFGGPRPdIVLG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736501793  171 ILHD--DDRWLADRMLDAAAEAPlYRTERNEPYgpeDGVTHTLKLHGIANGLHNVMIEVRNDLI 232
Cdd:pfam05013 159 TRYGasCDPRLADALLAALEAAG-YSVGRNEPY---AGGYITRHYGRPARGVHAVQIEIRRDLY 218
HutG COG3741
N-formylglutamate amidohydrolase [Amino acid transport and metabolism];
16-231 1.37e-09

N-formylglutamate amidohydrolase [Amino acid transport and metabolism];


Pssm-ID: 442955  Cd Length: 273  Bit Score: 57.09  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793  16 VAVERPDG-KSPFFIICEHASRRLPERFGDlGLSPEALSSHIAWDpgaLAVARKISD--SLDATLVHQRFSRLIYDCNRP 92
Cdd:COG3741    5 FEVHRPTAqTSPLVLSSPHSGTDYPPDFLA-RLRLDARALRRDED---WHVDRLYDFapALGATLLRANFSRAVIDLNRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793  93 PESA--------------GAMPEIS----EIYTIPgnqhLRAADREARTEALYIPFHNRIQALLKE-RANSGQkTVIVTV 153
Cdd:COG3741   81 PDELdpymfegprgqaglGLIPRTTfdgePIYRRR----PDVAEAERRIERYWRPYHAALAALLARlRARFGY-AVLIDC 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736501793 154 HSFTSV---YNGKPRA-VELGilhDD-----DRWLADRMLDAAAEAPlYRTERNEPYGpedGVtHTLKLHG-IANGLHNV 223
Cdd:COG3741  156 HSMPSViprLFGGRLPdFVLG---DRdgascAPALTAAVEAALAALG-YSVVRNGPFK---GG-YITRHYGrPARGVHAL 227

                 ....*...
gi 736501793 224 MIEVRNDL 231
Cdd:COG3741  228 QIEIARRL 235
 
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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