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Conserved domains on  [gi|889437831|emb|CLN86181|]
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D-amino acid aminohydrolase [Mycobacterium tuberculosis]

Protein Classification

amidohydrolase family protein( domain architecture ID 10790308)

amidohydrolase family protein similar to Mycobacterium tuberculosis protein Rv2913c

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
2-589 9.76e-144

N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 426.51  E-value: 9.76e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   2 TYDVIIRDGLWFDGTGNAPLTRTLGIRDGVVATVaaGALDETGCPEVVDAAGKWVVPGFIDVHTHYDAEVLLDPGLRESV 81
Cdd:COG3653    1 MFDLLIRGGTVVDGTGAPPFRADVAIKGGRIVAV--GDLAAAEAARVIDATGLVVAPGFIDIHTHYDLQLLWDPRLEPSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831  82 RHGVTTVLLGNCSLSTVYANSEDA---ADLFSRVEAVPREFvlgalrdNQTWSTPAEYIEAIDALPLGPNVSSLLGHSDL 158
Cdd:COG3653   79 RQGVTTVVMGNCGVSFAPVRPEDRdrlIDLMEGVEGIPEGL-------DWDWESFGEYLDALERRGLGVNVASLVGHGTL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 159 RTAVLGLDRAtddtvRPTEAELAKMAKLLDEALEAGMLGMSGMDAAIdkldgdrfrsralPSTFATWRERRKLISVLRHR 238
Cdd:COG3653  152 RAYVMGLDDR-----PPTPEELARMRALLREAMEAGALGLSTGLIYV-------------PGTYASTDELVALAKVVAEY 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 239 GRILQSAP-----DVDNPVSALLFFLASSRIfnrrkGVRMSMLVSADAksmPLAVHVFGLGTRVLN-KLLGSQVRFQHLP 312
Cdd:COG3653  214 GGVYQSHMrdegdGLLEAVDELIRIGREAGV-----PVHISHLKAAGK---PNWGKADEVLALIEAaRAEGLDVTADVYP 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 313 VPFELYSDGIDLPvfeefgAGTAALHLRDQLQRnelLADRSYRRSFRREFDRIKLGPSLWHRDFHDAVIVECP-DKSLIG 391
Cdd:COG3653  286 YPAGSTGLGALLP------PWAAAGGLDERLAR---LRDPATRARIRAEIEEGLPDNLLGRGGWDNILISDSPpNEPLVG 356
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 392 KSFGAIADERGLHPLDAFLDVLVDNGERNVRWTTIvanHRPNQLNKLAAEPSVHMGfSDAG----AHLRNmafYNFGLRL 467
Cdd:COG3653  357 KSLAEIAAERGVDPADAALDLLLEEDGRVLIVYFI---MSEEDVRELLRHPWVMIG-SDGGlggkAHPRA---YGTFPRV 429
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 468 LKR-ARDadragQPFLSIERAVYRLTGELAEWFGI-GAGTLRQGDRADFAVIDPTHLDESVDgYHEEAvpyygglrrmvN 545
Cdd:COG3653  430 LGHyVRE-----RGVLSLEEAVRKLTSLPADRLGLkDRGLLRPGYRADLVVFDPATLADRAT-FDLPA-----------Q 492
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....
gi 889437831 546 RNDAtVVATGVGGTVVFRGGQFGGQFrdgygqnvkSGRYLRAGE 589
Cdd:COG3653  493 RADG-IRAVIVNGVVVVEDGKPTGAR---------PGRVLRGGG 526
 
Name Accession Description Interval E-value
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
2-589 9.76e-144

N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 426.51  E-value: 9.76e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   2 TYDVIIRDGLWFDGTGNAPLTRTLGIRDGVVATVaaGALDETGCPEVVDAAGKWVVPGFIDVHTHYDAEVLLDPGLRESV 81
Cdd:COG3653    1 MFDLLIRGGTVVDGTGAPPFRADVAIKGGRIVAV--GDLAAAEAARVIDATGLVVAPGFIDIHTHYDLQLLWDPRLEPSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831  82 RHGVTTVLLGNCSLSTVYANSEDA---ADLFSRVEAVPREFvlgalrdNQTWSTPAEYIEAIDALPLGPNVSSLLGHSDL 158
Cdd:COG3653   79 RQGVTTVVMGNCGVSFAPVRPEDRdrlIDLMEGVEGIPEGL-------DWDWESFGEYLDALERRGLGVNVASLVGHGTL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 159 RTAVLGLDRAtddtvRPTEAELAKMAKLLDEALEAGMLGMSGMDAAIdkldgdrfrsralPSTFATWRERRKLISVLRHR 238
Cdd:COG3653  152 RAYVMGLDDR-----PPTPEELARMRALLREAMEAGALGLSTGLIYV-------------PGTYASTDELVALAKVVAEY 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 239 GRILQSAP-----DVDNPVSALLFFLASSRIfnrrkGVRMSMLVSADAksmPLAVHVFGLGTRVLN-KLLGSQVRFQHLP 312
Cdd:COG3653  214 GGVYQSHMrdegdGLLEAVDELIRIGREAGV-----PVHISHLKAAGK---PNWGKADEVLALIEAaRAEGLDVTADVYP 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 313 VPFELYSDGIDLPvfeefgAGTAALHLRDQLQRnelLADRSYRRSFRREFDRIKLGPSLWHRDFHDAVIVECP-DKSLIG 391
Cdd:COG3653  286 YPAGSTGLGALLP------PWAAAGGLDERLAR---LRDPATRARIRAEIEEGLPDNLLGRGGWDNILISDSPpNEPLVG 356
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 392 KSFGAIADERGLHPLDAFLDVLVDNGERNVRWTTIvanHRPNQLNKLAAEPSVHMGfSDAG----AHLRNmafYNFGLRL 467
Cdd:COG3653  357 KSLAEIAAERGVDPADAALDLLLEEDGRVLIVYFI---MSEEDVRELLRHPWVMIG-SDGGlggkAHPRA---YGTFPRV 429
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 468 LKR-ARDadragQPFLSIERAVYRLTGELAEWFGI-GAGTLRQGDRADFAVIDPTHLDESVDgYHEEAvpyygglrrmvN 545
Cdd:COG3653  430 LGHyVRE-----RGVLSLEEAVRKLTSLPADRLGLkDRGLLRPGYRADLVVFDPATLADRAT-FDLPA-----------Q 492
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....
gi 889437831 546 RNDAtVVATGVGGTVVFRGGQFGGQFrdgygqnvkSGRYLRAGE 589
Cdd:COG3653  493 RADG-IRAVIVNGVVVVEDGKPTGAR---------PGRVLRGGG 526
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
4-570 3.86e-111

D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.


Pssm-ID: 238622 [Multi-domain]  Cd Length: 415  Bit Score: 338.89  E-value: 3.86e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   4 DVIIRDGLWFDGTGNAPLTRTLGIRDGVVATVaaGALDETGCPEVVDAAGKWVVPGFIDVHTHYDAEVLLDPGLRESVRH 83
Cdd:cd01297    1 DLVIRNGTVVDGTGAPPFTADVGIRDGRIAAI--GPILSTSAREVIDAAGLVVAPGFIDVHTHYDGQVFWDPDLRPSSRQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831  84 GVTTVLLGNCSLSTVYANSEDAADLFSRVEAvpreFVLGALRDNQTWSTPAEYIEAIDALPLGPNVSSLLGHSDLRTAVL 163
Cdd:cd01297   79 GVTTVVLGNCGVSPAPANPDDLARLIMLMEG----LVALGEGLPWGWATFAEYLDALEARPPAVNVAALVGHAALRRAVM 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 164 GLDRatddtVRPTEAELAKMAKLLDEALEAGMLGMSGMDAAIdkldgdrfrsralPSTFATWRERRKLISVLRHRGRILQ 243
Cdd:cd01297  155 GLDA-----REATEEELAKMRELLREALEAGALGISTGLAYA-------------PRLYAGTAELVALARVAARYGGVYQ 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 244 SAPDV--DNPVSALLFFLASSRIFNRRkgVRMSMLVSADAKSmplaVHVFGLGTRVLNKLL--GSQVRFQHLPVPFELYS 319
Cdd:cd01297  217 THVRYegDSILEALDELLRLGRETGRP--VHISHLKSAGAPN----WGKIDRLLALIEAARaeGLQVTADVYPYGAGSED 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 320 DGIDLPVFEefgagtaalhlrdqlqrnelladrsyrrsfrrefdriklgpslwhrdfhdavivecpdksligksfgaiad 399
Cdd:cd01297  291 DVRRIMAHP----------------------------------------------------------------------- 299
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 400 erglhpldafldvlvdngernvrwttivanhrpnqlnklaaepsVHMGFSDAGA----HLRNMAFynFGLRLLKRARDAD 475
Cdd:cd01297  300 --------------------------------------------VVMGGSDGGAlgkpHPRSYGD--FTRVLGHYVRERK 333
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 476 RagqpfLSIERAVYRLTGELAEWFGIGA-GTLRQGDRADFAVIDPTHLDESVDGYheeavpyygglrrMVNRNDATVVAT 554
Cdd:cd01297  334 L-----LSLEEAVRKMTGLPARVFGLADrGRIAPGYRADIVVFDPDTLADRATFT-------------RPNQPAEGIEAV 395
                        570
                 ....*....|....*.
gi 889437831 555 GVGGTVVFRGGQFGGQ 570
Cdd:cd01297  396 LVNGVPVVRDGAFTGA 411
PRK09061 PRK09061
D-glutamate deacylase; Validated
2-204 3.25e-11

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 65.87  E-value: 3.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   2 TYDVIIRDGLWFDGTGNAPLTRTLGIRDGVVATVAAGALDETgcpEVVDAAGKWVVPGFIDVHTHYDAEvlldPGLRESV 81
Cdd:PRK09061  18 PYDLVIRNGRVVDPETGLDAVRDVGIKGGKIAAVGTAAIEGD---RTIDATGLVVAPGFIDLHAHGQSV----AAYRMQA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831  82 RHGVTTVL---LGNCSLSTVYANSEDAAdlfsrveavpREFVLGAlrdNQTWsTPAEYieaidALPLGPNVSSLLghsDL 158
Cdd:PRK09061  91 FDGVTTALeleAGVLPVARWYAEQAGEG----------RPLNYGA---SVGW-TPARI-----AVLTGPQAEGTI---AD 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 889437831 159 RTAVLGLDRATDDTvrPTEAELAKMAKLLDEALEAGMLGMsGMDAA 204
Cdd:PRK09061 149 FGKALGDPRWQERA--ATPAELAEILELLEQGLDEGALGI-GIGAG 191
Amidohydro_3 pfam07969
Amidohydrolase family;
47-199 5.63e-06

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 49.07  E-value: 5.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   47 EVVDAAGKWVVPGFIDVHTH-----YDAEVLLDPGLRESVRHGvttvllgncslstvyANSEDAADLFSRVEAVPREFVL 121
Cdd:pfam07969   1 EVIDAKGRLVLPGFVDPHTHldgggLNLRELRLPDVLPNAVVK---------------GQAGRTPKGRWLVGEGWDEAQF 65
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 889437831  122 GALRDNQTWstpAEYIEAIDALPlgPNVSSLLGHSDLRTAVLgLDRATDDtvrpTEAELAKMAKLLDEALEAGMLGMS 199
Cdd:pfam07969  66 AETRFPYAL---ADLDEVAPDGP--VLLRALHTHAAVANSAA-LDLAGIT----KATEDPPGGEIARDANGEGLTGLL 133
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
23-91 3.11e-05

dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273302 [Multi-domain]  Cd Length: 411  Bit Score: 46.67  E-value: 3.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 889437831   23 RTLGIRDGVVATVAAGALDETGcpEVVDAAGKWVVPGFIDVHTHydaevLLDPGL--RESVRHGVTTVLLG 91
Cdd:TIGR00857   6 VDILVEGGRIKKIGKLRIPPDA--EVIDAKGLLVLPGFIDLHVH-----LRDPGEeyKEDIESGSKAAAHG 69
 
Name Accession Description Interval E-value
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
2-589 9.76e-144

N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 426.51  E-value: 9.76e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   2 TYDVIIRDGLWFDGTGNAPLTRTLGIRDGVVATVaaGALDETGCPEVVDAAGKWVVPGFIDVHTHYDAEVLLDPGLRESV 81
Cdd:COG3653    1 MFDLLIRGGTVVDGTGAPPFRADVAIKGGRIVAV--GDLAAAEAARVIDATGLVVAPGFIDIHTHYDLQLLWDPRLEPSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831  82 RHGVTTVLLGNCSLSTVYANSEDA---ADLFSRVEAVPREFvlgalrdNQTWSTPAEYIEAIDALPLGPNVSSLLGHSDL 158
Cdd:COG3653   79 RQGVTTVVMGNCGVSFAPVRPEDRdrlIDLMEGVEGIPEGL-------DWDWESFGEYLDALERRGLGVNVASLVGHGTL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 159 RTAVLGLDRAtddtvRPTEAELAKMAKLLDEALEAGMLGMSGMDAAIdkldgdrfrsralPSTFATWRERRKLISVLRHR 238
Cdd:COG3653  152 RAYVMGLDDR-----PPTPEELARMRALLREAMEAGALGLSTGLIYV-------------PGTYASTDELVALAKVVAEY 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 239 GRILQSAP-----DVDNPVSALLFFLASSRIfnrrkGVRMSMLVSADAksmPLAVHVFGLGTRVLN-KLLGSQVRFQHLP 312
Cdd:COG3653  214 GGVYQSHMrdegdGLLEAVDELIRIGREAGV-----PVHISHLKAAGK---PNWGKADEVLALIEAaRAEGLDVTADVYP 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 313 VPFELYSDGIDLPvfeefgAGTAALHLRDQLQRnelLADRSYRRSFRREFDRIKLGPSLWHRDFHDAVIVECP-DKSLIG 391
Cdd:COG3653  286 YPAGSTGLGALLP------PWAAAGGLDERLAR---LRDPATRARIRAEIEEGLPDNLLGRGGWDNILISDSPpNEPLVG 356
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 392 KSFGAIADERGLHPLDAFLDVLVDNGERNVRWTTIvanHRPNQLNKLAAEPSVHMGfSDAG----AHLRNmafYNFGLRL 467
Cdd:COG3653  357 KSLAEIAAERGVDPADAALDLLLEEDGRVLIVYFI---MSEEDVRELLRHPWVMIG-SDGGlggkAHPRA---YGTFPRV 429
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 468 LKR-ARDadragQPFLSIERAVYRLTGELAEWFGI-GAGTLRQGDRADFAVIDPTHLDESVDgYHEEAvpyygglrrmvN 545
Cdd:COG3653  430 LGHyVRE-----RGVLSLEEAVRKLTSLPADRLGLkDRGLLRPGYRADLVVFDPATLADRAT-FDLPA-----------Q 492
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....
gi 889437831 546 RNDAtVVATGVGGTVVFRGGQFGGQFrdgygqnvkSGRYLRAGE 589
Cdd:COG3653  493 RADG-IRAVIVNGVVVVEDGKPTGAR---------PGRVLRGGG 526
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
4-570 3.86e-111

D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.


Pssm-ID: 238622 [Multi-domain]  Cd Length: 415  Bit Score: 338.89  E-value: 3.86e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   4 DVIIRDGLWFDGTGNAPLTRTLGIRDGVVATVaaGALDETGCPEVVDAAGKWVVPGFIDVHTHYDAEVLLDPGLRESVRH 83
Cdd:cd01297    1 DLVIRNGTVVDGTGAPPFTADVGIRDGRIAAI--GPILSTSAREVIDAAGLVVAPGFIDVHTHYDGQVFWDPDLRPSSRQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831  84 GVTTVLLGNCSLSTVYANSEDAADLFSRVEAvpreFVLGALRDNQTWSTPAEYIEAIDALPLGPNVSSLLGHSDLRTAVL 163
Cdd:cd01297   79 GVTTVVLGNCGVSPAPANPDDLARLIMLMEG----LVALGEGLPWGWATFAEYLDALEARPPAVNVAALVGHAALRRAVM 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 164 GLDRatddtVRPTEAELAKMAKLLDEALEAGMLGMSGMDAAIdkldgdrfrsralPSTFATWRERRKLISVLRHRGRILQ 243
Cdd:cd01297  155 GLDA-----REATEEELAKMRELLREALEAGALGISTGLAYA-------------PRLYAGTAELVALARVAARYGGVYQ 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 244 SAPDV--DNPVSALLFFLASSRIFNRRkgVRMSMLVSADAKSmplaVHVFGLGTRVLNKLL--GSQVRFQHLPVPFELYS 319
Cdd:cd01297  217 THVRYegDSILEALDELLRLGRETGRP--VHISHLKSAGAPN----WGKIDRLLALIEAARaeGLQVTADVYPYGAGSED 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 320 DGIDLPVFEefgagtaalhlrdqlqrnelladrsyrrsfrrefdriklgpslwhrdfhdavivecpdksligksfgaiad 399
Cdd:cd01297  291 DVRRIMAHP----------------------------------------------------------------------- 299
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 400 erglhpldafldvlvdngernvrwttivanhrpnqlnklaaepsVHMGFSDAGA----HLRNMAFynFGLRLLKRARDAD 475
Cdd:cd01297  300 --------------------------------------------VVMGGSDGGAlgkpHPRSYGD--FTRVLGHYVRERK 333
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 476 RagqpfLSIERAVYRLTGELAEWFGIGA-GTLRQGDRADFAVIDPTHLDESVDGYheeavpyygglrrMVNRNDATVVAT 554
Cdd:cd01297  334 L-----LSLEEAVRKMTGLPARVFGLADrGRIAPGYRADIVVFDPDTLADRATFT-------------RPNQPAEGIEAV 395
                        570
                 ....*....|....*.
gi 889437831 555 GVGGTVVFRGGQFGGQ 570
Cdd:cd01297  396 LVNGVPVVRDGAFTGA 411
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
1-88 1.15e-12

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 69.99  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   1 MTYDVIIRDGLWFDGTGNAPLTR-TLGIRDGVVatVAAGALDETGCP---EVVDAAGKWVVPGFIDVHTHY--------- 67
Cdd:COG1228    6 QAGTLLITNATLVDGTGGGVIENgTVLVEDGKI--AAVGPAADLAVPagaEVIDATGKTVLPGLIDAHTHLglgggrave 83
                         90       100       110
                 ....*....|....*....|....*....|..
gi 889437831  68 -----------DAEVLLDPGLRESVRHGVTTV 88
Cdd:COG1228   84 feagggitptvDLVNPADKRLRRALAAGVTTV 115
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
4-88 8.08e-12

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 67.11  E-value: 8.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   4 DVIIRDGLWFDGTGNAPLTRTLGIRDGVVATVAAgALDETGCPEVVDAAGKWVVPGFIDVHTH--YDAEVLLDPGLRESV 81
Cdd:COG3964    1 DLLIKGGRVIDPANGIDGVMDIAIKDGKIAAVAK-DIDAAEAKKVIDASGLYVTPGLIDLHTHvfPGGTDYGVDPDGVGV 79

                 ....*..
gi 889437831  82 RHGVTTV 88
Cdd:COG3964   80 RSGVTTV 86
PRK09061 PRK09061
D-glutamate deacylase; Validated
2-204 3.25e-11

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 65.87  E-value: 3.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   2 TYDVIIRDGLWFDGTGNAPLTRTLGIRDGVVATVAAGALDETgcpEVVDAAGKWVVPGFIDVHTHYDAEvlldPGLRESV 81
Cdd:PRK09061  18 PYDLVIRNGRVVDPETGLDAVRDVGIKGGKIAAVGTAAIEGD---RTIDATGLVVAPGFIDLHAHGQSV----AAYRMQA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831  82 RHGVTTVL---LGNCSLSTVYANSEDAAdlfsrveavpREFVLGAlrdNQTWsTPAEYieaidALPLGPNVSSLLghsDL 158
Cdd:PRK09061  91 FDGVTTALeleAGVLPVARWYAEQAGEG----------RPLNYGA---SVGW-TPARI-----AVLTGPQAEGTI---AD 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 889437831 159 RTAVLGLDRATDDTvrPTEAELAKMAKLLDEALEAGMLGMsGMDAA 204
Cdd:PRK09061 149 FGKALGDPRWQERA--ATPAELAEILELLEQGLDEGALGI-GIGAG 191
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
5-88 1.50e-10

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 63.33  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   5 VIIRDGLWFDGTGNAPLTRTLGIRDGVVATVAaGALDETGCPEVVDAAGKWVVPGFIDVHTH--YDAEVLLDPGLRESVR 82
Cdd:PRK09237   1 LLLRGGRVIDPANGIDGVIDIAIEDGKIAAVA-GDIDGSQAKKVIDLSGLYVSPGWIDLHVHvyPGSTPYGDEPDEVGVR 79

                 ....*.
gi 889437831  83 HGVTTV 88
Cdd:PRK09237  80 SGVTTV 85
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
6-89 2.34e-10

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439814 [Multi-domain]  Cd Length: 439  Bit Score: 62.80  E-value: 2.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   6 IIRDGLWFDGTGNAPltRTLGIRDGVVATVAAGALDETGCpEVVDAAGKWVVPGFIDVHTHYDaevllDPGL--RESVRH 83
Cdd:COG0044    1 LIKNGRVVDPGGLER--ADVLIEDGRIAAIGPDLAAPEAA-EVIDATGLLVLPGLIDLHVHLR-----EPGLehKEDIET 72
                         90
                 ....*....|....
gi 889437831  84 --------GVTTVL 89
Cdd:COG0044   73 gtraaaagGVTTVV 86
PRK08323 PRK08323
phenylhydantoinase; Validated
3-68 2.75e-08

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 56.33  E-value: 2.75e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 889437831   3 YDVIIRDGLWF--DGTGNApltrTLGIRDGVVATVAAGALDEtgcpeVVDAAGKWVVPGFIDVHTHYD 68
Cdd:PRK08323   1 MSTLIKNGTVVtaDDTYKA----DVLIEDGKIAAIGANLGDE-----VIDATGKYVMPGGIDPHTHME 59
pyrC PRK09357
dihydroorotase; Validated
27-90 3.60e-08

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 55.97  E-value: 3.60e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831  27 IRDGVVATVAAGALDETGcpEVVDAAGKWVVPGFIDVHTHY------DAEVLLDpGLRESVRHGVTTVLL 90
Cdd:PRK09357  24 IDDGKIAAIGENIEAEGA--EVIDATGLVVAPGLVDLHVHLrepgqeDKETIET-GSRAAAAGGFTTVVA 90
PRK09060 PRK09060
dihydroorotase; Validated
1-127 8.78e-08

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 54.93  E-value: 8.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   1 MTYDVIIRDGLWF--DGTGnaplTRTLGIRDGVVATVaaGALDETGCPEVVDAAGKWVVPGFIDVHTHYDaevllDPGL- 77
Cdd:PRK09060   3 QTFDLILKGGTVVnpDGEG----RADIGIRDGRIAAI--GDLSGASAGEVIDCRGLHVLPGVIDSQVHFR-----EPGLe 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 889437831  78 ---------RESVRHGVTTVL-LGNCSLSTVYAnsEDAADLFSRVEA---VPREFVLGALRDN 127
Cdd:PRK09060  72 hkedletgsRAAVLGGVTAVFeMPNTNPLTTTA--EALADKLARARHrmhCDFAFYVGGTRDN 132
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
4-88 1.01e-07

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 54.72  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   4 DVIIRDGLWFDgtgnaPLTRTL-----GIRDGVVATVAAGALDETgcpEVVDAAGKWVVPGFIDVHTH----------YD 68
Cdd:COG1001    6 DLVIKNGRLVN-----VFTGEIlegdiAIAGGRIAGVGDYIGEAT---EVIDAAGRYLVPGFIDGHVHiessmvtpaeFA 77
                         90       100
                 ....*....|....*....|
gi 889437831  69 AEVLLdpglresvrHGVTTV 88
Cdd:COG1001   78 RAVLP---------HGTTTV 88
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
25-89 1.09e-07

D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.


Pssm-ID: 238639 [Multi-domain]  Cd Length: 447  Bit Score: 54.53  E-value: 1.09e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 889437831  25 LGIRDGVVATVAAGaLDETGCPEVVDAAGKWVVPGFIDVHTHYDAEVLLDP-------GLRESVRHGVTTVL 89
Cdd:cd01314   19 ILIEDGKIVAIGPN-LEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVtaddfesGTRAAAAGGTTTII 89
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
5-89 2.13e-07

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: 53.35  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   5 VIIRDGLWFDGTGNAPLTrtLGIRDGVVATVAAGALDETgCPEVVDAAGKWVVPGFIDVHTH----YDAEVLLDPGLRES 80
Cdd:cd00854    1 LIIKNARILTPGGLEDGA--VLVEDGKIVAIGPEDELEE-ADEIIDLKGQYLVPGFIDIHIHggggADFMDGTAEALKTI 77
                         90
                 ....*....|...
gi 889437831  81 ----VRHGVTTVL 89
Cdd:cd00854   78 aealAKHGTTSFL 90
PRK06189 PRK06189
allantoinase; Provisional
1-68 2.30e-07

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 53.55  E-value: 2.30e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   1 MTYDVIIRDGLWF--DGTGNApltrTLGIRDGVVATVAAGAldETGCPEVVDAAGKWVVPGFIDVHTHYD 68
Cdd:PRK06189   1 MMYDLIIRGGKVVtpEGVYRA----DIGIKNGKIAEIAPEI--SSPAREIIDADGLYVFPGMIDVHVHFN 64
PRK12394 PRK12394
metallo-dependent hydrolase;
1-67 6.59e-07

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 51.68  E-value: 6.59e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 889437831   1 MTYDVIIRDGLWFDGTGNAPLTRTLGIRDG-VVATVAAGALDETgcpEVVDAAGKWVVPGFIDVHTHY 67
Cdd:PRK12394   1 MKNDILITNGHIIDPARNINEINNLRIINDiIVDADKYPVASET---RIIHADGCIVTPGLIDYHAHV 65
PRK13404 PRK13404
dihydropyrimidinase; Provisional
1-70 9.94e-07

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 51.62  E-value: 9.94e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   1 MTYDVIIRDGLWFDGTGNapLTRTLGIRDGVVATVAAGAldeTGCPEVVDAAGKWVVPGFIDVHTHYDAE 70
Cdd:PRK13404   2 MAFDLVIRGGTVVTATDT--FQADIGIRGGRIAALGEGL---GPGAREIDATGRLVLPGGVDSHCHIDQP 66
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
6-89 1.31e-06

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 50.87  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   6 IIRDGLWFDGTGNAPlTRTLGIRDGVVATVAAGALDETgcpEVVDAAGKWVVPGFIDVHTH---------YDAEVLLDpG 76
Cdd:COG1820    1 AITNARIFTGDGVLE-DGALLIEDGRIAAIGPGAEPDA---EVIDLGGGYLAPGFIDLHVHggggvdfmdGTPEALRT-I 75
                         90
                 ....*....|...
gi 889437831  77 LRESVRHGVTTVL 89
Cdd:COG1820   76 ARAHARHGTTSFL 88
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
4-106 4.70e-06

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: 49.05  E-value: 4.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   4 DVIIRDGLWFDGTGNAPLTR--TLGIRDGVVATVAAGALDETGCP--EVVDAAGKWVVPGFIDVHTH------------- 66
Cdd:COG0402    1 DLLIRGAWVLTMDPAGGVLEdgAVLVEDGRIAAVGPGAELPARYPaaEVIDAGGKLVLPGLVNTHTHlpqtllrgladdl 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 889437831  67 ----------YDAEVLLDP---------GLRESVRHGVTTVllgnCSLSTVYANSEDAA 106
Cdd:COG0402   81 plldwleeyiWPLEARLDPedvyagallALAEMLRSGTTTV----ADFYYVHPESADAL 135
Amidohydro_3 pfam07969
Amidohydrolase family;
47-199 5.63e-06

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 49.07  E-value: 5.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   47 EVVDAAGKWVVPGFIDVHTH-----YDAEVLLDPGLRESVRHGvttvllgncslstvyANSEDAADLFSRVEAVPREFVL 121
Cdd:pfam07969   1 EVIDAKGRLVLPGFVDPHTHldgggLNLRELRLPDVLPNAVVK---------------GQAGRTPKGRWLVGEGWDEAQF 65
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 889437831  122 GALRDNQTWstpAEYIEAIDALPlgPNVSSLLGHSDLRTAVLgLDRATDDtvrpTEAELAKMAKLLDEALEAGMLGMS 199
Cdd:pfam07969  66 AETRFPYAL---ADLDEVAPDGP--VLLRALHTHAAVANSAA-LDLAGIT----KATEDPPGGEIARDANGEGLTGLL 133
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
25-66 1.06e-05

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 48.02  E-value: 1.06e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 889437831  25 LGIRDGVVATV----AAGALDETGCpEVVDAAGKWVVPGFIDVHTH 66
Cdd:cd01296    1 IAIRDGRIAAVgpaaSLPAPGPAAA-EEIDAGGRAVTPGLVDCHTH 45
PRK09236 PRK09236
dihydroorotase; Reviewed
27-77 1.25e-05

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 47.94  E-value: 1.25e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 889437831  27 IRDGVVATVAaGALDETGCPEVVDAAGKWVVPGFIDVHTHYDaevllDPGL 77
Cdd:PRK09236  24 IENGRIAKIA-SSISAKSADTVIDAAGRYLLPGMIDDQVHFR-----EPGL 68
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
24-89 2.65e-05

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 46.71  E-value: 2.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 889437831  24 TLGIRDGVVATVAAGAldeTGCPEVVDAAGKWVVPGFIDVHT-HYDAEVL--------LDPGLRES----VRHGVTTVL 89
Cdd:PRK15446  21 SLLIEDGRIAAIDPGA---SALPGAIDAEGDYLLPGLVDLHTdNLEKHLAprpgvdwpADAALAAHdaqlAAAGITTVF 96
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
27-88 3.09e-05

Metallo-dependent hydrolases, subgroup B 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: 238632 [Multi-domain]  Cd Length: 338  Bit Score: 46.55  E-value: 3.09e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 889437831  27 IRDGVVATVAAgALDETGCPEVVDAAGKWVVPGFIDVHTH--YDAEVLLDPGLRESVRHGVTTV 88
Cdd:cd01307    4 IENGKIAAVGA-ALAAPAATQIVDAGGCYVSPGWIDLHVHvyQGGTRYGDRPDMIGVKSGVTTV 66
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
23-91 3.11e-05

dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273302 [Multi-domain]  Cd Length: 411  Bit Score: 46.67  E-value: 3.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 889437831   23 RTLGIRDGVVATVAAGALDETGcpEVVDAAGKWVVPGFIDVHTHydaevLLDPGL--RESVRHGVTTVLLG 91
Cdd:TIGR00857   6 VDILVEGGRIKKIGKLRIPPDA--EVIDAKGLLVLPGFIDLHVH-----LRDPGEeyKEDIESGSKAAAHG 69
PRK02382 PRK02382
dihydroorotase; Provisional
4-88 3.21e-05

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 46.57  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   4 DVIIRDGLWFdgTGNAPLTRTLGIRDGVVATVAaGALDETGCPEVVDAAGKWVVPGFIDVHTHYDaevllDPGL------ 77
Cdd:PRK02382   3 DALLKDGRVY--YNNSLQPRDVRIDGGKITAVG-KDLDGSSSEEVIDARGMLLLPGGIDVHVHFR-----EPGYthketw 74
                         90
                 ....*....|....*
gi 889437831  78 ----RESVRHGVTTV 88
Cdd:PRK02382  75 ytgsRSAAAGGVTTV 89
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
1-66 3.25e-05

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 46.72  E-value: 3.25e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 889437831   1 MTYDVIIRDGLWFDGT-----GNAPLTRTLGIRDGVVatVAAGALDE-----TGCPEVVDAAGKWVVPGFIDVHTH 66
Cdd:COG1574    1 MKLAAAAADLLLTNGRiytmdPAQPVAEAVAVRDGRI--VAVGSDAEvralaGPATEVIDLGGKTVLPGFIDAHVH 74
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
47-91 4.84e-05

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: 45.77  E-value: 4.84e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 889437831  47 EVVDAAGKWVVPGFIDVHTH---YDAEVL-------------------------LDPGLRESVRHGVTTVLLG 91
Cdd:cd01309   18 EVIDAKGKHVTPGLIDAHSHlglDEEGGVretsdaneetdpvtphvraidginpDDEAFKRARAGGVTTVQVL 90
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
4-79 5.09e-05

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: 46.13  E-value: 5.09e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 889437831   4 DVIIRDGLWFdgTGNAPLTRTLGIRDGVVATVAAGALDETGcPEVVDAAGKWVVPGFIDVHTHYDaevllDPGLRE 79
Cdd:cd01315    1 DLVIKNGRVV--TPDGVREADIAVKGGKIAAIGPDIANTEA-EEVIDAGGLVVMPGLIDTHVHIN-----EPGRTE 68
PRK07572 PRK07572
cytosine deaminase; Validated
2-69 5.87e-05

cytosine deaminase; Validated


Pssm-ID: 181039  Cd Length: 426  Bit Score: 45.78  E-value: 5.87e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 889437831   2 TYDVIIRDGLWFDGTGNApltrTLGIRDGVVATVAAGaLDETGcPEVVDAAGKWVVPGFIDVHTHYDA 69
Cdd:PRK07572   1 MFDLIVRNANLPDGRTGI----DIGIAGGRIAAVEPG-LQAEA-AEEIDAAGRLVSPPFVDPHFHMDA 62
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
25-66 7.15e-05

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: 45.76  E-value: 7.15e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 889437831  25 LGIRDGVV------ATVAAGALDETgcpEVVDAAGKWVVPGFIDVHTH 66
Cdd:cd01300    2 VAVRDGRIvavgsdAEAKALKGPAT---EVIDLKGKTVLPGFIDSHSH 46
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
25-89 1.24e-04

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: 44.89  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831  25 LGIRDGVVATVAAGA-LDETGCPEVVDAAGKWVVPGFIDVHTH-----------------------YDAEVLLDP----- 75
Cdd:cd01298   22 VLVEDGRIVAVGPALpLPAYPADEVIDAKGKVVMPGLVNTHTHlamtllrgladdlplmewlkdliWPLERLLTEedvyl 101
                         90
                 ....*....|....*...
gi 889437831  76 ----GLRESVRHGVTTVL 89
Cdd:cd01298  102 gallALAEMIRSGTTTFA 119
PRK09228 PRK09228
guanine deaminase; Provisional
27-109 1.33e-04

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 44.80  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831  27 IRDGVVatVAAGALDE--TGCP---EVVDAAGKWVVPGFIDVHTHYD--------AEVLL---------------DPG-- 76
Cdd:PRK09228  36 VEDGRI--VAAGPYAElrAQLPadaEVTDYRGKLILPGFIDTHIHYPqtdmiasyGEQLLdwlntytfpeerrfaDPAya 113
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 889437831  77 -------LRESVRHGVTTVLlgncSLSTVYANSEDAadLF 109
Cdd:PRK09228 114 revaeffLDELLRNGTTTAL----VFGTVHPQSVDA--LF 147
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
47-88 1.58e-04

Metallo-dependent hydrolases, subgroup A 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: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 44.21  E-value: 1.58e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 889437831  47 EVVDAAGKWVVPGFIDVHTH------YDAEVLLDPG----------LRESVRHGVTTV 88
Cdd:cd01299    2 QVIDLGGKTLMPGLIDAHTHlgsdpgDLPLDLALPVeyrtiratrqARAALRAGFTTV 59
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
47-90 2.46e-04

Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.


Pssm-ID: 238642 [Multi-domain]  Cd Length: 374  Bit Score: 43.76  E-value: 2.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 889437831  47 EVVDAAGKWVVPGFIDVHTHydaevLLDPGL----------RESVRHGVTTVLL 90
Cdd:cd01317    3 EVIDAEGKILAPGLVDLHVH-----LREPGFeyketlesgaKAAAAGGFTTVVC 51
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
25-68 2.74e-04

Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.


Pssm-ID: 238618 [Multi-domain]  Cd Length: 398  Bit Score: 43.39  E-value: 2.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 889437831  25 LGIRDGVVATVAAgALDETGCPEVVDAAGKWVVPGFIDVHTHYD 68
Cdd:cd01293   17 IAIEDGRIAAIGP-ALAVPPDAEEVDAKGRLVLPAFVDPHIHLD 59
ade TIGR01178
adenine deaminase; The family described by this model includes an experimentally characterized ...
27-89 6.27e-04

adenine deaminase; The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130246 [Multi-domain]  Cd Length: 552  Bit Score: 42.84  E-value: 6.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 889437831   27 IRDGVVATVaagalDETGCPEVVDAAGKWVVPGFIDVHTHYDAEVLLDPGL-RESVRHGVTTVL 89
Cdd:TIGR01178  24 IANGHIAGV-----GKYNGVKVIDALGEYAVPGFIDAHIHIESSMLTPSEFaKLVLPHGVTTVV 82
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
481-570 8.33e-04

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: 42.28  E-value: 8.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831 481 FLSIERAVYRLTGELAEWFGIGA--GTLRQGDRADFAVIDPTH---LDESVDGYHEEAVPYYGglrrmvNRNDATVVATG 555
Cdd:cd01315  352 GLSLEDIARLMCENPAKLFGLSHqkGRIAVGYDADFVVWDPEEeftVDAEDLYYKNKISPYVG------RTLKGRVHATI 425
                         90
                 ....*....|....*
gi 889437831 556 VGGTVVFRGGQFGGQ 570
Cdd:cd01315  426 LRGTVVYQDGEVVGE 440
AdeC cd01295
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ...
50-88 1.46e-03

Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.


Pssm-ID: 238620 [Multi-domain]  Cd Length: 422  Bit Score: 41.44  E-value: 1.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 889437831  50 DAAGKWVVPGFIDVHTHYDAEVLLDPGLRESV-RHGVTTV 88
Cdd:cd01295    1 DAEGKYIVPGFIDAHLHIESSMLTPSEFAKAVlPHGTTTV 40
PLN02942 PLN02942
dihydropyrimidinase
27-72 1.55e-03

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 41.37  E-value: 1.55e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 889437831  27 IRDGVVATVAAGaLDETGCPEVVDAAGKWVVPGFIDVHTHYDAEVL 72
Cdd:PLN02942  27 VEDGIIVAVAPN-LKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFM 71
PRK05985 PRK05985
cytosine deaminase; Provisional
4-68 2.32e-03

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 40.69  E-value: 2.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 889437831   4 DVIIRDGLWFDGTgnaplTRTLGIRDGVVATVAAGALDETGCpEVVDAAGKWVVPGFIDVHTHYD 68
Cdd:PRK05985   3 DLLFRNVRPAGGA-----AVDILIRDGRIAAIGPALAAPPGA-EVEDGGGALALPGLVDGHIHLD 61
PRK07213 PRK07213
chlorohydrolase; Provisional
24-109 4.01e-03

chlorohydrolase; Provisional


Pssm-ID: 235969 [Multi-domain]  Cd Length: 375  Bit Score: 39.64  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831  24 TLGIRDGVVAtvaaGALDETGCPEVVDAAGKwVVPGFIDVHTHYDAEVLLDPG----LRESVR--HGVTTVLLGNCSLST 97
Cdd:PRK07213  21 NLVIEDGIIK----GFTNEVHEGNVIDAKGL-VIPPLINAHTHIGDSSIKDIGigksLDELVKppNGLKHKFLNSCSDKE 95
                         90
                 ....*....|...
gi 889437831  98 -VYANSEDAADLF 109
Cdd:PRK07213  96 lVEGMKEGLYDMY 108
PRK08044 PRK08044
allantoinase AllB;
1-89 4.38e-03

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 39.84  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889437831   1 MTYDVIIRDGLWFdgTGNAPLTRTLGIRDGVVATVAagalDETGCPE-VVDAAGKWVVPGFIDVHTHydaevLLDP---- 75
Cdd:PRK08044   1 MSFDLIIKNGTVI--LENEARVVDIAVKGGKIAAIG----QDLGDAKeVMDASGLVVSPGMVDAHTH-----ISEPgrsh 69
                         90       100
                 ....*....|....*....|
gi 889437831  76 ------GLRESVRHGVTTVL 89
Cdd:PRK08044  70 wegyetGTRAAAKGGITTMI 89
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
27-66 5.13e-03

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 39.45  E-value: 5.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 889437831  27 IRDGVVATVAAGALDETGCPEVVDAAGKWVVPGFIDVHTH 66
Cdd:PRK08203  28 VEGGRIVEVGPGGALPQPADEVFDARGHVVTPGLVNTHHH 67
FMDH_A cd01304
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ...
23-66 6.60e-03

Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.


Pssm-ID: 238629 [Multi-domain]  Cd Length: 541  Bit Score: 39.32  E-value: 6.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 889437831  23 RTLGIRDGVVATVAAGALDEtgcpEVVDAAGKWVVPGFIDVHTH 66
Cdd:cd01304   18 MDIFIRDGKIVESSSGAKPA----KVIDASGKVVMAGGVDMHSH 57
 
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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