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Conserved domains on  [gi|489062066|ref|WP_002972094|]
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MULTISPECIES: N-formylglutamate amidohydrolase [Brucella]

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];
1-219 1.36e-117

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


:

Pssm-ID: 443132  Cd Length: 252  Bit Score: 335.20  E-value: 1.36e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489062066   1 MPESFAGLGLDAETRKTHIAWDPGAVEVARELSKALDAPLVEAGLPRLLIDCNRPLDAPDLIPEISETTLVPGNHGLNTA 80
Cdd:COG3931   33 VPAALGDLGLPAADLERHIAWDIGAAGVARALAERLDAPLVLSRYSRLVIDCNRPPDDPTLIPELSDGTVIPGNRGLSAA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489062066  81 ERMARIDLSHRPFHRRIEEVIAMRAARGQPSWIVTVHSFTPVYRGVSRPWQIGIIHDEDDRIARPLIAALRQDMGLHIGV 160
Cdd:COG3931  113 ERAARLAAIYRPYHDAIAALLAARLARGRPPVIVSIHSFTPVYKGVPRPWHIGILHDRDPRLADPLLAALRAEGDLVVGD 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489062066 161 NEPYSPADRVYYTLERHARPRNAPCVMIEIRNDEITDAGTQTAWGRKLTAILKKYQETM 219
Cdd:COG3931  193 NEPYSGADGVDYTLDRHAEARGLPNVLIEIRQDLIADEAGQAAWAERLARLLRAALAAL 251
 
Name Accession Description Interval E-value
HutG2 COG3931
Predicted N-formylglutamate amidohydrolase [Amino acid transport and metabolism];
1-219 1.36e-117

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


Pssm-ID: 443132  Cd Length: 252  Bit Score: 335.20  E-value: 1.36e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489062066   1 MPESFAGLGLDAETRKTHIAWDPGAVEVARELSKALDAPLVEAGLPRLLIDCNRPLDAPDLIPEISETTLVPGNHGLNTA 80
Cdd:COG3931   33 VPAALGDLGLPAADLERHIAWDIGAAGVARALAERLDAPLVLSRYSRLVIDCNRPPDDPTLIPELSDGTVIPGNRGLSAA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489062066  81 ERMARIDLSHRPFHRRIEEVIAMRAARGQPSWIVTVHSFTPVYRGVSRPWQIGIIHDEDDRIARPLIAALRQDMGLHIGV 160
Cdd:COG3931  113 ERAARLAAIYRPYHDAIAALLAARLARGRPPVIVSIHSFTPVYKGVPRPWHIGILHDRDPRLADPLLAALRAEGDLVVGD 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489062066 161 NEPYSPADRVYYTLERHARPRNAPCVMIEIRNDEITDAGTQTAWGRKLTAILKKYQETM 219
Cdd:COG3931  193 NEPYSGADGVDYTLDRHAEARGLPNVLIEIRQDLIADEAGQAAWAERLARLLRAALAAL 251
FGase pfam05013
N-formylglutamate amidohydrolase; Formylglutamate amidohydrolase (FGase) catalyzes the ...
2-193 8.54e-43

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: 143.87  E-value: 8.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489062066    2 PESFAGlGLDAETRKTHIAWDPGAVEVARELsKALDAPLVEAGLPRLLIDCNR-PLDAPDLIPEISETTLVPGN------ 74
Cdd:pfam05013  15 PPDLGA-GLALDEAELHIAEDWHVDELYAFA-PALGASLLVARFSRLVIDLNRpPDDLDPYMPVQSGLGLIPRNtfdgep 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489062066   75 ---HGLNTAERMARIDLSHRPFHRRIEEVIAMRAARGQPSWIVTVHSFT---PVYRGVSRP-WQIGIIHDE--DDRIARP 145
Cdd:pfam05013  93 iydRPLDAAERAARIERYYRPYHAALAALLARLRARHGPAVLIDCHSMPsrgPRLFGGPRPdIVLGTRYGAscDPRLADA 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 489062066  146 LIAALRQdMGLHIGVNEPYSpadrVYYTLERHARP-RNAPCVMIEIRND 193
Cdd:pfam05013 173 LLAALEA-AGYSVGRNEPYA----GGYITRHYGRPaRGVHAVQIEIRRD 216
 
Name Accession Description Interval E-value
HutG2 COG3931
Predicted N-formylglutamate amidohydrolase [Amino acid transport and metabolism];
1-219 1.36e-117

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


Pssm-ID: 443132  Cd Length: 252  Bit Score: 335.20  E-value: 1.36e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489062066   1 MPESFAGLGLDAETRKTHIAWDPGAVEVARELSKALDAPLVEAGLPRLLIDCNRPLDAPDLIPEISETTLVPGNHGLNTA 80
Cdd:COG3931   33 VPAALGDLGLPAADLERHIAWDIGAAGVARALAERLDAPLVLSRYSRLVIDCNRPPDDPTLIPELSDGTVIPGNRGLSAA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489062066  81 ERMARIDLSHRPFHRRIEEVIAMRAARGQPSWIVTVHSFTPVYRGVSRPWQIGIIHDEDDRIARPLIAALRQDMGLHIGV 160
Cdd:COG3931  113 ERAARLAAIYRPYHDAIAALLAARLARGRPPVIVSIHSFTPVYKGVPRPWHIGILHDRDPRLADPLLAALRAEGDLVVGD 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489062066 161 NEPYSPADRVYYTLERHARPRNAPCVMIEIRNDEITDAGTQTAWGRKLTAILKKYQETM 219
Cdd:COG3931  193 NEPYSGADGVDYTLDRHAEARGLPNVLIEIRQDLIADEAGQAAWAERLARLLRAALAAL 251
FGase pfam05013
N-formylglutamate amidohydrolase; Formylglutamate amidohydrolase (FGase) catalyzes the ...
2-193 8.54e-43

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: 143.87  E-value: 8.54e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489062066    2 PESFAGlGLDAETRKTHIAWDPGAVEVARELsKALDAPLVEAGLPRLLIDCNR-PLDAPDLIPEISETTLVPGN------ 74
Cdd:pfam05013  15 PPDLGA-GLALDEAELHIAEDWHVDELYAFA-PALGASLLVARFSRLVIDLNRpPDDLDPYMPVQSGLGLIPRNtfdgep 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489062066   75 ---HGLNTAERMARIDLSHRPFHRRIEEVIAMRAARGQPSWIVTVHSFT---PVYRGVSRP-WQIGIIHDE--DDRIARP 145
Cdd:pfam05013  93 iydRPLDAAERAARIERYYRPYHAALAALLARLRARHGPAVLIDCHSMPsrgPRLFGGPRPdIVLGTRYGAscDPRLADA 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 489062066  146 LIAALRQdMGLHIGVNEPYSpadrVYYTLERHARP-RNAPCVMIEIRND 193
Cdd:pfam05013 173 LLAALEA-AGYSVGRNEPYA----GGYITRHYGRPaRGVHAVQIEIRRD 216
HutG COG3741
N-formylglutamate amidohydrolase [Amino acid transport and metabolism];
35-191 1.00e-09

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


Pssm-ID: 442955  Cd Length: 273  Bit Score: 57.09  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489062066  35 ALDAPLVEAGLPRLLIDCNRPLDAPDL-----IPEISETTLVP-----G----NHGLNTAERMARIDLSHRPFHRRIEEV 100
Cdd:COG3741   60 ALGATLLRANFSRAVIDLNRDPDELDPymfegPRGQAGLGLIPrttfdGepiyRRRPDVAEAERRIERYWRPYHAALAAL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489062066 101 IA-MRAARGQpSWIVTVHSF---TPVYRGVSRPwQIgIIHDE-----DDRIARPLIAALRQdMGLHIGVNEPYSPAdrvy 171
Cdd:COG3741  140 LArLRARFGY-AVLIDCHSMpsvIPRLFGGRLP-DF-VLGDRdgascAPALTAAVEAALAA-LGYSVVRNGPFKGG---- 211
                        170       180
                 ....*....|....*....|.
gi 489062066 172 YTLERHARP-RNAPCVMIEIR 191
Cdd:COG3741  212 YITRHYGRPaRGVHALQIEIA 232
 
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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