NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1670270067|gb|TLZ13571|]
View 

amidohydrolase, partial [Gammaproteobacteria bacterium]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YtcJ super family cl34308
Predicted amidohydrolase YtcJ [General function prediction only];
2-95 5.06e-36

Predicted amidohydrolase YtcJ [General function prediction only];


The actual alignment was detected with superfamily member COG1574:

Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 127.61  E-value: 5.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670270067   2 DPLIEFYAAVARRSVDGYAdenWHLEQRVSRTRALKMLSSGPAYAAFQENERGSIEVGKIADFTVLSDDIMSIPEADILR 81
Cdd:COG1574   442 DPLLGIYAAVTRRTPSGRG---LGPEERLTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKD 518

                          90
                  ....*....|....
gi 1670270067  82 ARVVMTVIGGEVVY 95
Cdd:COG1574   519 IKVLLTVVGGRVVY 532
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
2-95 5.06e-36

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 127.61  E-value: 5.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670270067   2 DPLIEFYAAVARRSVDGYAdenWHLEQRVSRTRALKMLSSGPAYAAFQENERGSIEVGKIADFTVLSDDIMSIPEADILR 81
Cdd:COG1574   442 DPLLGIYAAVTRRTPSGRG---LGPEERLTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKD 518

                          90
                  ....*....|....
gi 1670270067  82 ARVVMTVIGGEVVY 95
Cdd:COG1574   519 IKVLLTVVGGRVVY 532
Amidohydro_3 pfam07969
Amidohydrolase family;
2-95 2.55e-22

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 89.51  E-value: 2.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670270067   2 DPLIEFYAAVARRSVDGYADENWhlEQRVSRTRALKMLSSGPAYAAFQENERGSIEVGKIADFTVLSDDIMSIPEADILR 81
Cdd:pfam07969 373 DPWPRIGAAVMRQTAGGGEVLGP--DEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIAD 450

                          90
                  ....*....|....
gi 1670270067  82 ARVVMTVIGGEVVY 95
Cdd:pfam07969 451 IRVRLTVVDGRVVY 464
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 2-66 6.01e-17

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 74.27  E-value: 6.01e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1670270067   2 DPLIEFYAAVARRSVDGyaDENWHLEQRVSRTRALKMLSSGPAYAAFQENERGSIEVGKIADFTV 66
Cdd:cd01300   417 DPLLGIWAAVTRKTPGG--GVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
34-97 1.31e-05

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 41.91  E-value: 1.31e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1670270067  34 RALKMLSSGPAYAAFQENERGSIEVGKIADFTVLSDDIM---SIPEADIL--------RARVVMTVIGGEVVYTE 97
Cdd:PRK07228  341 TVFEMATLGGAKAAGFEDEIGSLEEGKKADLAILDLDGLhatPSHGVDVLshlvyaahGSDVETTMVDGKIVMED 415
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
2-95 5.06e-36

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 127.61  E-value: 5.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670270067   2 DPLIEFYAAVARRSVDGYAdenWHLEQRVSRTRALKMLSSGPAYAAFQENERGSIEVGKIADFTVLSDDIMSIPEADILR 81
Cdd:COG1574   442 DPLLGIYAAVTRRTPSGRG---LGPEERLTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKD 518

                          90
                  ....*....|....
gi 1670270067  82 ARVVMTVIGGEVVY 95
Cdd:COG1574   519 IKVLLTVVGGRVVY 532
Amidohydro_3 pfam07969
Amidohydrolase family;
2-95 2.55e-22

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 89.51  E-value: 2.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670270067   2 DPLIEFYAAVARRSVDGYADENWhlEQRVSRTRALKMLSSGPAYAAFQENERGSIEVGKIADFTVLSDDIMSIPEADILR 81
Cdd:pfam07969 373 DPWPRIGAAVMRQTAGGGEVLGP--DEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIAD 450

                          90
                  ....*....|....
gi 1670270067  82 ARVVMTVIGGEVVY 95
Cdd:pfam07969 451 IRVRLTVVDGRVVY 464
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 2-66 6.01e-17

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 74.27  E-value: 6.01e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1670270067   2 DPLIEFYAAVARRSVDGyaDENWHLEQRVSRTRALKMLSSGPAYAAFQENERGSIEVGKIADFTV 66
Cdd:cd01300   417 DPLLGIWAAVTRKTPGG--GVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 30-95 6.39e-09

Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238634 [Multi-domain]  Cd Length: 359  Bit Score: 51.54  E-value: 6.39e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670270067  30 VSRTRALKMLSSGPAYAAFQENERGSIEVGKIADFTVLSDDIMSipeadiLRARVVMTVIGGEVVY 95
Cdd:cd01309   300 LSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLE------PTSKPEQVYIDGRLVY 359
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 35-97 1.89e-08

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 49.96  E-value: 1.89e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1670270067  35 ALKMLSSGPAYAAFQENERGSIEVGKIADFTVLSDDimsiPEADI-LRARVVMTVIGGEVVYTE 97
Cdd:COG1228   327 ALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGD----PLEDIaYLEDVRAVMKDGRVVDRS 386
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
35-92 4.42e-08

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 48.94  E-value: 4.42e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1670270067  35 ALKMLSSGPAYAAFQENERGSIEVGKIADFTVLSDDImsipeadilraRVVMTVIGGE 92
Cdd:COG1820   327 AVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDL-----------NVRATWVGGE 373
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 28-95 3.12e-07

Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440171 [Multi-domain]  Cd Length: 416  Bit Score: 46.74  E-value: 3.12e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1670270067  28 QRVSRTRALKMLSSGPAYAAFQENERGSIEVGKIADFTVLS-DDIMSIPEADIL--------RARVVMTVIGGEVVY 95
Cdd:COG0402   338 TALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDlDAPHLAPLHDPLsalvyaadGRDVRTVWVAGRVVV 414
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 34-94 3.34e-07

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 46.34  E-value: 3.34e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1670270067  34 RALKMLSSGPAYAAFQENERGSIEVGKIADFTVLSDDIMSIPEADILRARVVMTVIGGEVV 94
Cdd:pfam01979 274 EALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKVIVKGKIV 334
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 35-91 7.05e-06

N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 42.57  E-value: 7.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1670270067  35 ALKMLSSGPAYAAFQENERGSIEVGKIADFTVLSDDImsipeadilraRVVMTVIGG 91
Cdd:cd00854   329 AVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDL-----------NVKATWING 374
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
34-97 1.31e-05

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 41.91  E-value: 1.31e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1670270067  34 RALKMLSSGPAYAAFQENERGSIEVGKIADFTVLSDDIM---SIPEADIL--------RARVVMTVIGGEVVYTE 97
Cdd:PRK07228  341 TVFEMATLGGAKAAGFEDEIGSLEEGKKADLAILDLDGLhatPSHGVDVLshlvyaahGSDVETTMVDGKIVMED 415
pyrC PRK00369
dihydroorotase; Provisional
 30-97 1.42e-03

dihydroorotase; Provisional


Pssm-ID: 234738 [Multi-domain]  Cd Length: 392  Bit Score: 36.28  E-value: 1.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1670270067  30 VSRTRALKMLSSGPA------YAAFQENERGSIEVGKIADF---TVLSDDIMSIPEADILRARVVMTVIGGEVVYTE 97
Cdd:PRK00369  298 LSIDRAVELISTNPArilgipYGEIKEGYRANFTVIQFEDWrysTKYSKVIETPLDGFELKASVYATIVQGKLAYLE 374
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 34-96 1.61e-03

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 35.92  E-value: 1.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1670270067  34 RALKMLSSGPAYAAfQENERGSIEVGKIADFtVLSDDIMSIPeadilraRVVMTVIGGEVVYT 96
Cdd:PRK15446  328 QAVALVTANPARAA-GLDDRGEIAPGKRADL-VRVRRAGGLP-------VVRAVWRGGRRVFL 381
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 35-97 1.94e-03

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 35.72  E-value: 1.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1670270067  35 ALKMLSSGPAYAAFQENERGSIEVGKIADFTVLSDDImsipeadilraRVVMTVIGGEVVYTE 97
Cdd:PRK11170  331 ALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDF-----------KITKTIVNGNEVVTQ 382
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 37-97 2.63e-03

L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.


Pssm-ID: 238640 [Multi-domain]  Cd Length: 447  Bit Score: 35.34  E-value: 2.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1670270067  37 KMLSSGPAYAAFQENERGSIEVGKIADFTVLSDDIMSIPEADIL--------------RARVVMTVIGGEVVYTE 97
Cdd:cd01315   360 RLMCENPAKLFGLSHQKGRIAVGYDADFVVWDPEEEFTVDAEDLyyknkispyvgrtlKGRVHATILRGTVVYQD 434
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 35-95 3.05e-03

TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.


Pssm-ID: 238623 [Multi-domain]  Cd Length: 411  Bit Score: 35.26  E-value: 3.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670270067  35 ALKMLSSGpAYAAFQENERGSIEVGKIADFTVLS-DDIMSIPEADIL--------RARVVMTVIGGEVVY 95
Cdd:cd01298   337 ALEMATIG-GAKALGLDEIGSLEVGKKADLILIDlDGPHLLPVHDPIshlvysanGGDVDTVIVNGRVVM 405
PhnM cd01306
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ...
 31-75 3.59e-03

PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.


Pssm-ID: 238631  Cd Length: 325  Bit Score: 34.95  E-value: 3.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1670270067  31 SRTRALKMLSSGPAYAA-FQEneRGSIEVGKIADFtVLSDDIMSIP 75
Cdd:cd01306   274 SLPEAVALVSANPARAVgLTD--RGSIAPGKRADL-ILVDDMDGVP 316
pyrC PRK09357
dihydroorotase; Validated
 34-95 9.46e-03

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 33.63  E-value: 9.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670270067  34 RALKMLSSGPAyAAFQEnERGSIEVGKIADFTVL---------SDDIMSI----P-EADILRARVVMTVIGGEVVY 95
Cdd:PRK09357  348 QLLEKMTINPA-RILGL-PAGPLAEGEPADLVIFdpeaewtvdGEDFASKgkntPfIGMKLKGKVVYTIVDGKIVY 421
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH