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Conserved domains on  [gi|489186526|ref|WP_003095940|]
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MULTISPECIES: N-formylglutamate deformylase [Pseudomonas]

Protein Classification

N-formylglutamate amidohydrolase( domain architecture ID 2882)

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; may be partial

CATH:  3.40.630.40
EC:  3.5.1.68
Gene Ontology:  GO:0006548|GO:0050129
SCOP:  4002298

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FGase super family cl01522
N-formylglutamate amidohydrolase; Formylglutamate amidohydrolase (FGase) catalyzes the ...
3-263 1.50e-147

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.


The actual alignment was detected with superfamily member TIGR02017:

Pssm-ID: 470234  Cd Length: 263  Bit Score: 413.01  E-value: 1.50e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526    3 EVLSFKRGRVPLLISMPHPGTRLTPAVDAGLVEEARALTDTDWHIPRLYDFAEELGASTLAAHYSRYVVDLNRPSDDKPL 82
Cdd:TIGR02017   1 DWLEVQRGNAPLLISIPHTGTDLPDAVESGLVSPWLALRDTDWHIHQLYDFARDLGATVVRTTYSRTVIDVNRDPDGVSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526   83 YST-ATTGLYPDTLFDGRPLYREGMAPSAEERMRYLAEVWTPYHRTIAEELARLKAEFGYALLWDAHSIRSHVPHLFDGR 161
Cdd:TIGR02017  81 YPGqATTGLCPETTFDGEPLYRDGEAPSPAEIDDRRTQIFRPYHAALQAEIERLRAQHGYAVLYDAHSIRSVIPRLFEGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526  162 LPDFNLGTNAGASCDPALAARLEAVCAAAEGYSHVLNGRFKGGHITRHYGQPEQHVHAVQLELAQCTYMDEQA-PFAYRA 240
Cdd:TIGR02017 161 LPDFNIGTNDGASCDPALTDAVEAVCAKATGYSHVLNGRFKGGWITRHYGQPQNGVHAVQMELAQRGYMAEEAePFAYRP 240
                         250       260
                  ....*....|....*....|...
gi 489186526  241 DLAEATRAVIRELLESLLAWGRE 263
Cdd:TIGR02017 241 DRAAPLRAVLKQLLQALLDWAAE 263
 
Name Accession Description Interval E-value
hutG_amidohyd TIGR02017
N-formylglutamate amidohydrolase; In some species, histidine is converted to via urocanate and ...
3-263 1.50e-147

N-formylglutamate amidohydrolase; In some species, histidine is converted to via urocanate and then formimino-L-glutamate to glutamate in four steps, where the fourth step is conversion of N-formimino-L-glutamate to L-glutamate and formamide. In others, that pathway from formimino-L-glutamate may differ, with the next enzyme being formiminoglutamate hydrolase (HutF) yielding N-formyl-L-glutamate. This model represents the enzyme N-formylglutamate deformylase, also called N-formylglutamate amidohydrolase, which then produces glutamate. [Energy metabolism, Amino acids and amines]


Pssm-ID: 131072  Cd Length: 263  Bit Score: 413.01  E-value: 1.50e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526    3 EVLSFKRGRVPLLISMPHPGTRLTPAVDAGLVEEARALTDTDWHIPRLYDFAEELGASTLAAHYSRYVVDLNRPSDDKPL 82
Cdd:TIGR02017   1 DWLEVQRGNAPLLISIPHTGTDLPDAVESGLVSPWLALRDTDWHIHQLYDFARDLGATVVRTTYSRTVIDVNRDPDGVSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526   83 YST-ATTGLYPDTLFDGRPLYREGMAPSAEERMRYLAEVWTPYHRTIAEELARLKAEFGYALLWDAHSIRSHVPHLFDGR 161
Cdd:TIGR02017  81 YPGqATTGLCPETTFDGEPLYRDGEAPSPAEIDDRRTQIFRPYHAALQAEIERLRAQHGYAVLYDAHSIRSVIPRLFEGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526  162 LPDFNLGTNAGASCDPALAARLEAVCAAAEGYSHVLNGRFKGGHITRHYGQPEQHVHAVQLELAQCTYMDEQA-PFAYRA 240
Cdd:TIGR02017 161 LPDFNIGTNDGASCDPALTDAVEAVCAKATGYSHVLNGRFKGGWITRHYGQPQNGVHAVQMELAQRGYMAEEAePFAYRP 240
                         250       260
                  ....*....|....*....|...
gi 489186526  241 DLAEATRAVIRELLESLLAWGRE 263
Cdd:TIGR02017 241 DRAAPLRAVLKQLLQALLDWAAE 263
HutG COG3741
N-formylglutamate amidohydrolase [Amino acid transport and metabolism];
1-266 7.35e-129

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


Pssm-ID: 442955  Cd Length: 273  Bit Score: 366.02  E-value: 7.35e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526   1 MDEVLSFKRG---RVPLLISMPHPGTRLTPAVDAGLVEEARAL-TDTDWHIPRLYDFAEELGASTLAAHYSRYVVDLNRP 76
Cdd:COG3741    1 MDPPFEVHRPtaqTSPLVLSSPHSGTDYPPDFLARLRLDARALrRDEDWHVDRLYDFAPALGATLLRANFSRAVIDLNRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526  77 SDDKPLY------STATTGLYPDTLFDGRPLYREgmAPSAEERMRYLAEVWTPYHRTIAEELARLKAEFGYALLWDAHSI 150
Cdd:COG3741   81 PDELDPYmfegprGQAGLGLIPRTTFDGEPIYRR--RPDVAEAERRIERYWRPYHAALAALLARLRARFGYAVLIDCHSM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526 151 RSHVPHLFDGRLPDFNLGTNAGASCDPALAARLEAVCAAAeGYSHVLNGRFKGGHITRHYGQPEQHVHAVQLELAQCTYM 230
Cdd:COG3741  159 PSVIPRLFGGRLPDFVLGDRDGASCAPALTAAVEAALAAL-GYSVVRNGPFKGGYITRHYGRPARGVHALQIEIARRLYM 237
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489186526 231 DEqAPFAYRADLAEATRAVIRELLESLLAWGRERYA 266
Cdd:COG3741  238 DE-APFEPDPAGAARLRADLAALLAALAAWARSRAA 272
FGase pfam05013
N-formylglutamate amidohydrolase; Formylglutamate amidohydrolase (FGase) catalyzes the ...
13-230 6.85e-94

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: 275.61  E-value: 6.85e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526   13 PLLISMPHPGTRLTPAVDAGL-VEEARALTDTDWHIPRLYDFAEELGASTLAAHYSRYVVDLNRPSDDKPLY--STATTG 89
Cdd:pfam05013   2 PLLLSSPHAGTAIPPDLGAGLaLDEAELHIAEDWHVDELYAFAPALGASLLVARFSRLVIDLNRPPDDLDPYmpVQSGLG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526   90 LYPDTLFDGRPLYREGMapSAEERMRYLAEVWTPYHRTIAEELARLKAEFGYALLWDAHSIRSHVPHLFDGRLPDFNLGT 169
Cdd:pfam05013  82 LIPRNTFDGEPIYDRPL--DAAERAARIERYYRPYHAALAALLARLRARHGPAVLIDCHSMPSRGPRLFGGPRPDIVLGT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489186526  170 NAGASCDPALAARLEAVCAAAeGYSHVLNGRFKGGHITRHYGQPEQHVHAVQLELAQCTYM 230
Cdd:pfam05013 160 RYGASCDPRLADALLAALEAA-GYSVGRNEPYAGGYITRHYGRPARGVHAVQIEIRRDLYM 219
 
Name Accession Description Interval E-value
hutG_amidohyd TIGR02017
N-formylglutamate amidohydrolase; In some species, histidine is converted to via urocanate and ...
3-263 1.50e-147

N-formylglutamate amidohydrolase; In some species, histidine is converted to via urocanate and then formimino-L-glutamate to glutamate in four steps, where the fourth step is conversion of N-formimino-L-glutamate to L-glutamate and formamide. In others, that pathway from formimino-L-glutamate may differ, with the next enzyme being formiminoglutamate hydrolase (HutF) yielding N-formyl-L-glutamate. This model represents the enzyme N-formylglutamate deformylase, also called N-formylglutamate amidohydrolase, which then produces glutamate. [Energy metabolism, Amino acids and amines]


Pssm-ID: 131072  Cd Length: 263  Bit Score: 413.01  E-value: 1.50e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526    3 EVLSFKRGRVPLLISMPHPGTRLTPAVDAGLVEEARALTDTDWHIPRLYDFAEELGASTLAAHYSRYVVDLNRPSDDKPL 82
Cdd:TIGR02017   1 DWLEVQRGNAPLLISIPHTGTDLPDAVESGLVSPWLALRDTDWHIHQLYDFARDLGATVVRTTYSRTVIDVNRDPDGVSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526   83 YST-ATTGLYPDTLFDGRPLYREGMAPSAEERMRYLAEVWTPYHRTIAEELARLKAEFGYALLWDAHSIRSHVPHLFDGR 161
Cdd:TIGR02017  81 YPGqATTGLCPETTFDGEPLYRDGEAPSPAEIDDRRTQIFRPYHAALQAEIERLRAQHGYAVLYDAHSIRSVIPRLFEGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526  162 LPDFNLGTNAGASCDPALAARLEAVCAAAEGYSHVLNGRFKGGHITRHYGQPEQHVHAVQLELAQCTYMDEQA-PFAYRA 240
Cdd:TIGR02017 161 LPDFNIGTNDGASCDPALTDAVEAVCAKATGYSHVLNGRFKGGWITRHYGQPQNGVHAVQMELAQRGYMAEEAePFAYRP 240
                         250       260
                  ....*....|....*....|...
gi 489186526  241 DLAEATRAVIRELLESLLAWGRE 263
Cdd:TIGR02017 241 DRAAPLRAVLKQLLQALLDWAAE 263
HutG COG3741
N-formylglutamate amidohydrolase [Amino acid transport and metabolism];
1-266 7.35e-129

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


Pssm-ID: 442955  Cd Length: 273  Bit Score: 366.02  E-value: 7.35e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526   1 MDEVLSFKRG---RVPLLISMPHPGTRLTPAVDAGLVEEARAL-TDTDWHIPRLYDFAEELGASTLAAHYSRYVVDLNRP 76
Cdd:COG3741    1 MDPPFEVHRPtaqTSPLVLSSPHSGTDYPPDFLARLRLDARALrRDEDWHVDRLYDFAPALGATLLRANFSRAVIDLNRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526  77 SDDKPLY------STATTGLYPDTLFDGRPLYREgmAPSAEERMRYLAEVWTPYHRTIAEELARLKAEFGYALLWDAHSI 150
Cdd:COG3741   81 PDELDPYmfegprGQAGLGLIPRTTFDGEPIYRR--RPDVAEAERRIERYWRPYHAALAALLARLRARFGYAVLIDCHSM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526 151 RSHVPHLFDGRLPDFNLGTNAGASCDPALAARLEAVCAAAeGYSHVLNGRFKGGHITRHYGQPEQHVHAVQLELAQCTYM 230
Cdd:COG3741  159 PSVIPRLFGGRLPDFVLGDRDGASCAPALTAAVEAALAAL-GYSVVRNGPFKGGYITRHYGRPARGVHALQIEIARRLYM 237
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489186526 231 DEqAPFAYRADLAEATRAVIRELLESLLAWGRERYA 266
Cdd:COG3741  238 DE-APFEPDPAGAARLRADLAALLAALAAWARSRAA 272
FGase pfam05013
N-formylglutamate amidohydrolase; Formylglutamate amidohydrolase (FGase) catalyzes the ...
13-230 6.85e-94

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: 275.61  E-value: 6.85e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526   13 PLLISMPHPGTRLTPAVDAGL-VEEARALTDTDWHIPRLYDFAEELGASTLAAHYSRYVVDLNRPSDDKPLY--STATTG 89
Cdd:pfam05013   2 PLLLSSPHAGTAIPPDLGAGLaLDEAELHIAEDWHVDELYAFAPALGASLLVARFSRLVIDLNRPPDDLDPYmpVQSGLG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526   90 LYPDTLFDGRPLYREGMapSAEERMRYLAEVWTPYHRTIAEELARLKAEFGYALLWDAHSIRSHVPHLFDGRLPDFNLGT 169
Cdd:pfam05013  82 LIPRNTFDGEPIYDRPL--DAAERAARIERYYRPYHAALAALLARLRARHGPAVLIDCHSMPSRGPRLFGGPRPDIVLGT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489186526  170 NAGASCDPALAARLEAVCAAAeGYSHVLNGRFKGGHITRHYGQPEQHVHAVQLELAQCTYM 230
Cdd:pfam05013 160 RYGASCDPRLADALLAALEAA-GYSVGRNEPYAGGYITRHYGRPARGVHAVQIEIRRDLYM 219
HutG2 COG3931
Predicted N-formylglutamate amidohydrolase [Amino acid transport and metabolism];
54-138 2.43e-08

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


Pssm-ID: 443132  Cd Length: 252  Bit Score: 53.23  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489186526  54 AEELGASTLAAHYSRYVVDLNRPSDDkplySTATTGLYPDTLFDG-RPLyregmapSAEERMRYLAEVWTPYHRTIAEEL 132
Cdd:COG3931   65 AERLDAPLVLSRYSRLVIDCNRPPDD----PTLIPELSDGTVIPGnRGL-------SAAERAARLAAIYRPYHDAIAALL 133

                 ....*.
gi 489186526 133 ARLKAE 138
Cdd:COG3931  134 AARLAR 139
 
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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