NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1027773277|ref|WP_063704983|]
View 

MULTISPECIES: amidohydrolase [Pseudoalteromonas]

Protein Classification

amidohydrolase( domain architecture ID 10101387)

metal-dependent amidohydrolase catalyzes the hydrolysis of amide bonds in target substrates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 73-442 1.17e-149

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: 430.19  E-value: 1.17e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  73 DGKVQQVGKDLSVQADKT-IDAQGKWVTPGIIDVHSHLGAYPTPSVASHQDGNEMTSPVTAEVWVEHSVWPQDPGFNRAR 151
Cdd:cd01309     1 DGKIVAVGAEITTPADAEvIDAKGKHVTPGLIDAHSHLGLDEEGGVRETSDANEETDPVTPHVRAIDGINPDDEAFKRAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 152 EGGITSLQILPGSANLIGGRGVTLKNIPSHTMqgMKFPDAPYGLKMACGENPKRVYGRKGVLPSTRMGNMAGYRTAWIDA 231
Cdd:cd01309    81 AGGVTTVQVLPGSANLIGGQGVVIKTDGGTIE--DMFIKAPAGLKMALGENPKRVYGGKGKEPATRMGVAALLRDAFIKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 232 TEYKREWDKYESdyaAGKNPaaPHRDIKLDTLAGVLEGDILIHNHCYKAEEMAMMIDLGKEFGYHsGTFHHGVEAYKIAD 311
Cdd:cd01309   159 QEYGRKYDLGKN---AKKDP--PERDLKLEALLPVLKGEIPVRIHAHRADDILTAIRIAKEFGIK-ITIEHGAEGYKLAD 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 312 LLAENGNCAALWPDWWGFKM--EAYDMVQENVAIVDAvKNSCAVVHSD-SDTTIQRLNQEAGKVMyrandvGYDISEQHA 388
Cdd:cd01309   233 ELAKHGIPVIYGPTLTLPKKveEVNDAIDTNAYLLKK-GGVAFAISSDhPVLNIRNLNLEAAKAV------KYGLSYEEA 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1027773277 389 IKWITSNAAKSLGIDDKTGSLEAGKQADVVIWNQNPFSVYAKAEQVFIDGAKVY 442
Cdd:cd01309   306 LKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLEPTSKPEQVYIDGRLVY 359
 
Name Accession Description Interval E-value
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 73-442 1.17e-149

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: 430.19  E-value: 1.17e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  73 DGKVQQVGKDLSVQADKT-IDAQGKWVTPGIIDVHSHLGAYPTPSVASHQDGNEMTSPVTAEVWVEHSVWPQDPGFNRAR 151
Cdd:cd01309     1 DGKIVAVGAEITTPADAEvIDAKGKHVTPGLIDAHSHLGLDEEGGVRETSDANEETDPVTPHVRAIDGINPDDEAFKRAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 152 EGGITSLQILPGSANLIGGRGVTLKNIPSHTMqgMKFPDAPYGLKMACGENPKRVYGRKGVLPSTRMGNMAGYRTAWIDA 231
Cdd:cd01309    81 AGGVTTVQVLPGSANLIGGQGVVIKTDGGTIE--DMFIKAPAGLKMALGENPKRVYGGKGKEPATRMGVAALLRDAFIKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 232 TEYKREWDKYESdyaAGKNPaaPHRDIKLDTLAGVLEGDILIHNHCYKAEEMAMMIDLGKEFGYHsGTFHHGVEAYKIAD 311
Cdd:cd01309   159 QEYGRKYDLGKN---AKKDP--PERDLKLEALLPVLKGEIPVRIHAHRADDILTAIRIAKEFGIK-ITIEHGAEGYKLAD 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 312 LLAENGNCAALWPDWWGFKM--EAYDMVQENVAIVDAvKNSCAVVHSD-SDTTIQRLNQEAGKVMyrandvGYDISEQHA 388
Cdd:cd01309   233 ELAKHGIPVIYGPTLTLPKKveEVNDAIDTNAYLLKK-GGVAFAISSDhPVLNIRNLNLEAAKAV------KYGLSYEEA 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1027773277 389 IKWITSNAAKSLGIDDKTGSLEAGKQADVVIWNQNPFSVYAKAEQVFIDGAKVY 442
Cdd:cd01309   306 LKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLEPTSKPEQVYIDGRLVY 359
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 40-445 1.32e-65

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 215.59  E-value: 1.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  40 TYKPLASQSTLITNATVLTGTGER-LDDADVFFVDGKVQQVGKDLSVQ---ADKTIDAQGKWVTPGIIDVHSHLGAYPTP 115
Cdd:COG1228     1 KKAPAQAGTLLITNATLVDGTGGGvIENGTVLVEDGKIAAVGPAADLAvpaGAEVIDATGKTVLPGLIDAHTHLGLGGGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 116 SVAshqdgNEMTSPVTAEVwveHSVWPQDPGFNRAREGGITSLQILPGSA-----NLIGGRGVTLKNipshtmqGMKFPD 190
Cdd:COG1228    81 AVE-----FEAGGGITPTV---DLVNPADKRLRRALAAGVTTVRDLPGGPlglrdAIIAGESKLLPG-------PRVLAA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 191 APyGLKMACGEnpkrvygrKGVLPSTrmgNMAGYRTAWIDATEYKREWDKYEsdyaagknpaapHRDIKLDTLAGVLEG- 269
Cdd:COG1228   146 GP-ALSLTGGA--------HARGPEE---ARAALRELLAEGADYIKVFAEGG------------APDFSLEELRAILEAa 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 270 ---DILIHNHCYKAEEMAMMIdlgkEFGYHSgtFHHGVEAYK-IADLLAENGnCAALWPDWWGFK--------------M 331
Cdd:COG1228   202 halGLPVAAHAHQADDIRLAV----EAGVDS--IEHGTYLDDeVADLLAEAG-TVVLVPTLSLFLallegaaapvaakaR 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 332 EAYDMVQENVAI-VDA-VKnscAVVHSDSDTTI---QRLNQEAGKVmyrandVGYDISEQHAIKWITSNAAKSLGIDDKT 406
Cdd:COG1228   275 KVREAALANARRlHDAgVP---VALGTDAGVGVppgRSLHRELALA------VEAGLTPEEALRAATINAAKALGLDDDV 345

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1027773277 407 GSLEAGKQADVVIWNQNPFSVYAKAE---QVFIDGaKVYDRN 445
Cdd:COG1228   346 GSLEPGKLADLVLLDGDPLEDIAYLEdvrAVMKDG-RVVDRS 386
pyrC PRK09357
dihydroorotase; Validated
 48-109 7.94e-13

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 69.84  E-value: 7.94e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027773277  48 STLITNATVLTGTGErLDDADVFFVDGKVQQVGKDLSVQADKTIDAQGKWVTPGIIDVHSHL 109
Cdd:PRK09357    2 MILIKNGRVIDPKGL-DEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHL 62
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 97-438 4.87e-11

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: 63.67  E-value: 4.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  97 WVTPGIIDVHSHLGAyptpSVASHQDGNEMTSPVTAEVWVEhsvwpqdpgfnRAREGGITslqilpgsanliggrgvTLK 176
Cdd:pfam01979   1 IVLPGLIDAHVHLEM----GLLRGIPVPPEFAYEALRLGIT-----------TMLKSGTT-----------------TVL 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 177 NIPSHTMQGMKFpdapygLKMACGENPK--RVYGRKGVL-----PSTRMGNM----AGYRTAWIDATEYKrewdkyesdY 245
Cdd:pfam01979  49 DMGATTSTGIEA------LLEAAEELPLglRFLGPGCSLdtdgeLEGRKALReklkAGAEFIKGMADGVV---------F 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 246 AAGKNPAAPHrdIKLDTLAGVLE----GDILIHNHCY-KAEEMAMMIDLGK---EFGYH-------------SGTFHHGV 304
Cdd:pfam01979 114 VGLAPHGAPT--FSDDELKAALEeakkYGLPVAIHALeTKGEVEDAIAAFGggiEHGTHlevaesgglldiiKLILAHGV 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 305 -----EAYKIADLLAENGNCAALWPDwwgfkmeayDMVQENV-AIVDAVKNSCAV-VHSDSDTTIQRLN-QEAGKVMY-R 375
Cdd:pfam01979 192 hlsptEANLLAEHLKGAGVAHCPFSN---------SKLRSGRiALRKALEDGVKVgLGTDGAGSGNSLNmLEELRLALeL 262

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027773277 376 ANDVGYDISEQHAIKWITSNAAKSLGIDDKTGSLEAGKQADVVIWNQNPFSVYAKAEQ------VFIDG 438
Cdd:pfam01979 263 QFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPdgnvkkVIVKG 331
hutI TIGR01224
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ...
 74-109 6.35e-03

imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273512 [Multi-domain]  Cd Length: 377  Bit Score: 38.55  E-value: 6.35e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1027773277  74 GKVQQVGKDLSV---QADKTIDAQGKWVTPGIIDVHSHL 109
Cdd:TIGR01224  11 GKIVWIGQLAALpgeEATEIIDCGGGLVTPGLVDPHTHL 49
 
Name Accession Description Interval E-value
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 73-442 1.17e-149

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: 430.19  E-value: 1.17e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  73 DGKVQQVGKDLSVQADKT-IDAQGKWVTPGIIDVHSHLGAYPTPSVASHQDGNEMTSPVTAEVWVEHSVWPQDPGFNRAR 151
Cdd:cd01309     1 DGKIVAVGAEITTPADAEvIDAKGKHVTPGLIDAHSHLGLDEEGGVRETSDANEETDPVTPHVRAIDGINPDDEAFKRAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 152 EGGITSLQILPGSANLIGGRGVTLKNIPSHTMqgMKFPDAPYGLKMACGENPKRVYGRKGVLPSTRMGNMAGYRTAWIDA 231
Cdd:cd01309    81 AGGVTTVQVLPGSANLIGGQGVVIKTDGGTIE--DMFIKAPAGLKMALGENPKRVYGGKGKEPATRMGVAALLRDAFIKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 232 TEYKREWDKYESdyaAGKNPaaPHRDIKLDTLAGVLEGDILIHNHCYKAEEMAMMIDLGKEFGYHsGTFHHGVEAYKIAD 311
Cdd:cd01309   159 QEYGRKYDLGKN---AKKDP--PERDLKLEALLPVLKGEIPVRIHAHRADDILTAIRIAKEFGIK-ITIEHGAEGYKLAD 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 312 LLAENGNCAALWPDWWGFKM--EAYDMVQENVAIVDAvKNSCAVVHSD-SDTTIQRLNQEAGKVMyrandvGYDISEQHA 388
Cdd:cd01309   233 ELAKHGIPVIYGPTLTLPKKveEVNDAIDTNAYLLKK-GGVAFAISSDhPVLNIRNLNLEAAKAV------KYGLSYEEA 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1027773277 389 IKWITSNAAKSLGIDDKTGSLEAGKQADVVIWNQNPFSVYAKAEQVFIDGAKVY 442
Cdd:cd01309   306 LKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDPLEPTSKPEQVYIDGRLVY 359
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 40-445 1.32e-65

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 215.59  E-value: 1.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  40 TYKPLASQSTLITNATVLTGTGER-LDDADVFFVDGKVQQVGKDLSVQ---ADKTIDAQGKWVTPGIIDVHSHLGAYPTP 115
Cdd:COG1228     1 KKAPAQAGTLLITNATLVDGTGGGvIENGTVLVEDGKIAAVGPAADLAvpaGAEVIDATGKTVLPGLIDAHTHLGLGGGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 116 SVAshqdgNEMTSPVTAEVwveHSVWPQDPGFNRAREGGITSLQILPGSA-----NLIGGRGVTLKNipshtmqGMKFPD 190
Cdd:COG1228    81 AVE-----FEAGGGITPTV---DLVNPADKRLRRALAAGVTTVRDLPGGPlglrdAIIAGESKLLPG-------PRVLAA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 191 APyGLKMACGEnpkrvygrKGVLPSTrmgNMAGYRTAWIDATEYKREWDKYEsdyaagknpaapHRDIKLDTLAGVLEG- 269
Cdd:COG1228   146 GP-ALSLTGGA--------HARGPEE---ARAALRELLAEGADYIKVFAEGG------------APDFSLEELRAILEAa 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 270 ---DILIHNHCYKAEEMAMMIdlgkEFGYHSgtFHHGVEAYK-IADLLAENGnCAALWPDWWGFK--------------M 331
Cdd:COG1228   202 halGLPVAAHAHQADDIRLAV----EAGVDS--IEHGTYLDDeVADLLAEAG-TVVLVPTLSLFLallegaaapvaakaR 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 332 EAYDMVQENVAI-VDA-VKnscAVVHSDSDTTI---QRLNQEAGKVmyrandVGYDISEQHAIKWITSNAAKSLGIDDKT 406
Cdd:COG1228   275 KVREAALANARRlHDAgVP---VALGTDAGVGVppgRSLHRELALA------VEAGLTPEEALRAATINAAKALGLDDDV 345

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1027773277 407 GSLEAGKQADVVIWNQNPFSVYAKAE---QVFIDGaKVYDRN 445
Cdd:COG1228   346 GSLEPGKLADLVLLDGDPLEDIAYLEdvrAVMKDG-RVVDRS 386
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 48-444 2.86e-16

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: 80.26  E-value: 2.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  48 STLITNATVLTGTGER--LDDADVFFVDGKVQQVGKDLSV----QADKTIDAQGKWVTPGIIDVHSHLGAYPTPSVAshQ 121
Cdd:COG0402     1 DLLIRGAWVLTMDPAGgvLEDGAVLVEDGRIAAVGPGAELparyPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLA--D 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 122 DGNEMTspvtaevWVEHSVWPQ----DPGFNRAR---------EGGITSLQ----ILPGSANLI-------GGRGVTLKn 177
Cdd:COG0402    79 DLPLLD-------WLEEYIWPLearlDPEDVYAGallalaemlRSGTTTVAdfyyVHPESADALaeaaaeaGIRAVLGR- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 178 ipshTMQGMKFPDAPyglkmacGENPKRVYGrkgvlpstrmgnmagyrtawiDATEYKREWDKYESD---YAAGknPAAP 254
Cdd:COG0402   151 ----GLMDRGFPDGL-------REDADEGLA---------------------DSERLIERWHGAADGrirVALA--PHAP 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 255 ---HRDIKLDTLAGVLEGDILIHNHCykAE---EMAMMI------------DLGkEFGYHSgTFHHGV-----EaykiAD 311
Cdd:COG0402   197 ytvSPELLRAAAALARELGLPLHTHL--AEtrdEVEWVLelygkrpveyldELG-LLGPRT-LLAHCVhltdeE----IA 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 312 LLAENGNCAALWP-----------DWwgFKMEAYDMvqeNVAI-VDavknSCAVVHSDS--DT-----TIQRLNQEAGKV 372
Cdd:COG0402   269 LLAETGASVAHCPtsnlklgsgiaPV--PRLLAAGV---RVGLgTD----GAASNNSLDmfEEmrlaaLLQRLRGGDPTA 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 373 MyrandvgydiSEQHAIKWITSNAAKSLGIDDKTGSLEAGKQADVVIWN---------QNPFS--VYA----KAEQVFID 437
Cdd:COG0402   340 L----------SAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDldaphlaplHDPLSalVYAadgrDVRTVWVA 409


                  ....*..
gi 1027773277 438 GAKVYDR 444
Cdd:COG0402   410 GRVVVRD 416
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
 49-108 3.53e-15

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


Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 77.52  E-value: 3.53e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  49 TLITNATVLTGTGERLDDADVFFVDGKVQQVGKDLSVQADKTIDAQGKWVTPGIIDVHSH 108
Cdd:COG3653     4 LLIRGGTVVDGTGAPPFRADVAIKGGRIVAVGDLAAAEAARVIDATGLVVAPGFIDIHTH 63
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 50-110 3.07e-14

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: 74.36  E-value: 3.07e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027773277  50 LITNATVLTGTGERldDADVFFVDGKVQQVGKDLSV-QADKTIDAQGKWVTPGIIDVHSHLG 110
Cdd:COG0044     1 LIKNGRVVDPGGLE--RADVLIEDGRIAAIGPDLAApEAAEVIDATGLLVLPGLIDLHVHLR 60
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 49-108 4.85e-14

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: 73.49  E-value: 4.85e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  49 TLITNATVLTGTGERLDDADVFFVDGKVQQVGKDLSVQADKTIDAQGKWVTPGIIDVHSH 108
Cdd:cd01297     2 LVIRNGTVVDGTGAPPFTADVGIRDGRIAAIGPILSTSAREVIDAAGLVVAPGFIDVHTH 61
pyrC PRK09357
dihydroorotase; Validated
 48-109 7.94e-13

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 69.84  E-value: 7.94e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027773277  48 STLITNATVLTGTGErLDDADVFFVDGKVQQVGKDLSVQADKTIDAQGKWVTPGIIDVHSHL 109
Cdd:PRK09357    2 MILIKNGRVIDPKGL-DEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHL 62
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
50-115 2.29e-12

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 68.27  E-value: 2.29e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027773277  50 LITNATVLTGTGERLDDADVFFVDGKVQQVGKDLSV-QADKTIDAQGKWVTPGIIDVHSHLGAYPTP 115
Cdd:COG3964     3 LIKGGRVIDPANGIDGVMDIAIKDGKIAAVAKDIDAaEAKKVIDASGLYVTPGLIDLHTHVFPGGTD 69
PRK08323 PRK08323
phenylhydantoinase; Validated
 48-109 8.47e-12

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 66.73  E-value: 8.47e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027773277  48 STLITNATVLTGTGERldDADVFFVDGKVQQVGKDlsvQADKTIDAQGKWVTPGIIDVHSHL 109
Cdd:PRK08323    2 STLIKNGTVVTADDTY--KADVLIEDGKIAAIGAN---LGDEVIDATGKYVMPGGIDPHTHM 58
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 49-109 9.82e-12

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: 66.47  E-value: 9.82e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027773277  49 TLITNATVLTGTGERLddADVFFVDGKVQQVGKDLSVQAD-KTIDAQGKWVTPGIIDVHSHL 109
Cdd:cd01314     1 LIIKNGTIVTADGSFK--ADILIEDGKIVAIGPNLEAPGGvEVIDATGKYVLPGGIDPHTHL 60
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
388-445 1.34e-11

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 66.36  E-value: 1.34e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027773277 388 AIKWITSNAAKSLGIDDKTGSLEAGKQADVVIWNQNPFSVYA------KAEQVFIDGAKVYDRN 445
Cdd:COG1574   472 ALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPeeikdiKVLLTVVGGRVVYEAE 535
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 49-442 2.06e-11

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: 65.30  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  49 TLITNATVLT-GTGERLDDADVFFVDGKVQQVGKDLSV---QADKTIDAQGKWVTPGIIDVHSHLGAYPTPSVAshqDGN 124
Cdd:cd01298     1 ILIRNGTIVTtDPRRVLEDGDVLVEDGRIVAVGPALPLpayPADEVIDAKGKVVMPGLVNTHTHLAMTLLRGLA---DDL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 125 EMTSPVTAEVWVEHSVWPQDPGFNRAREGGITSLQilpgsanliggRGVTlknipshTMQGMKF--PDApygLKMACGEN 202
Cdd:cd01298    78 PLMEWLKDLIWPLERLLTEEDVYLGALLALAEMIR-----------SGTT-------TFADMYFfyPDA---VAEAAEEL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 203 PKRVYGRKGV--LPSTRMGNMAGYrtawIDATEykREWDKYESDYAAGKNPA-APH------RDIKLDTLAGVLEGDILI 273
Cdd:cd01298   137 GIRAVLGRGImdLGTEDVEETEEA----LAEAE--RLIREWHGAADGRIRVAlAPHapytcsDELLREVAELAREYGVPL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 274 HNHCYK-AEEMAMMIDL-GK-------EFGYHSG-TFH-HGVEA-YKIADLLAENGNCAALWPD-----WWGF----KME 332
Cdd:cd01298   211 HIHLAEtEDEVEESLEKyGKrpveyleELGLLGPdVVLaHCVWLtDEEIELLAETGTGVAHNPAsnmklASGIapvpEML 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 333 AYDMvqeNVAI-VD--AVKNSCAVVHS-DSDTTIQRLNQEAGKVMyrandvgydiSEQHAIKWITSNAAKSLGIDDkTGS 408
Cdd:cd01298   291 EAGV---NVGLgTDgaASNNNLDMFEEmRLAALLQKLAHGDPTAL----------PAEEALEMATIGGAKALGLDE-IGS 356

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1027773277 409 LEAGKQADVVIWN---------QNPFS---VYAKAEQV---FIDGAKVY 442
Cdd:cd01298   357 LEVGKKADLILIDldgphllpvHDPIShlvYSANGGDVdtvIVNGRVVM 405
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 97-438 4.87e-11

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: 63.67  E-value: 4.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  97 WVTPGIIDVHSHLGAyptpSVASHQDGNEMTSPVTAEVWVEhsvwpqdpgfnRAREGGITslqilpgsanliggrgvTLK 176
Cdd:pfam01979   1 IVLPGLIDAHVHLEM----GLLRGIPVPPEFAYEALRLGIT-----------TMLKSGTT-----------------TVL 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 177 NIPSHTMQGMKFpdapygLKMACGENPK--RVYGRKGVL-----PSTRMGNM----AGYRTAWIDATEYKrewdkyesdY 245
Cdd:pfam01979  49 DMGATTSTGIEA------LLEAAEELPLglRFLGPGCSLdtdgeLEGRKALReklkAGAEFIKGMADGVV---------F 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 246 AAGKNPAAPHrdIKLDTLAGVLE----GDILIHNHCY-KAEEMAMMIDLGK---EFGYH-------------SGTFHHGV 304
Cdd:pfam01979 114 VGLAPHGAPT--FSDDELKAALEeakkYGLPVAIHALeTKGEVEDAIAAFGggiEHGTHlevaesgglldiiKLILAHGV 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 305 -----EAYKIADLLAENGNCAALWPDwwgfkmeayDMVQENV-AIVDAVKNSCAV-VHSDSDTTIQRLN-QEAGKVMY-R 375
Cdd:pfam01979 192 hlsptEANLLAEHLKGAGVAHCPFSN---------SKLRSGRiALRKALEDGVKVgLGTDGAGSGNSLNmLEELRLALeL 262

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027773277 376 ANDVGYDISEQHAIKWITSNAAKSLGIDDKTGSLEAGKQADVVIWNQNPFSVYAKAEQ------VFIDG 438
Cdd:pfam01979 263 QFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPdgnvkkVIVKG 331
PRK06687 PRK06687
TRZ/ATZ family protein;
73-419 6.14e-11

TRZ/ATZ family protein;


Pssm-ID: 180657 [Multi-domain]  Cd Length: 419  Bit Score: 63.87  E-value: 6.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  73 DGKVQQVGKDLSV---QADKTIDAQGKWVTPGIIDVHSHLGAYPTPSVASHQDGNEmtspvtaevWVEHSVWPQDPGFN- 148
Cdd:PRK06687   28 DSQIVYVGQDKPAfleQAEQIIDYQGAWIMPGLVNCHTHSAMTGLRGIRDDSNLHE---------WLNDYIWPAESEFTp 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 149 ----RAREGGITSLqILPGSA---NLIGGRGVTLKNIPSHTMQGmkfpdapyglKMACGENPKRVYGRKGVLPSTrmgnM 221
Cdd:PRK06687   99 dmttNAVKEALTEM-LQSGTTtfnDMYNPNGVDIQQIYQVVKTS----------KMRCYFSPTLFSSETETTAET----I 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 222 AGYRTAWIDATEYKrewDKYESDYAAGKNPAAPHRDIKLDTLAGVLEGDILIHNHCYKAEEMAMMI---------DLGKE 292
Cdd:PRK06687  164 SRTRSIIDEILKYK---NPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIIlkrygkrplAFLEE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 293 FGY--HSGTFHHGVE--AYKIADLLAENGNCAAlwpdwwgFKMEAYDMVQENVAIVDAVKNSCAV-VHSDSDTTIQRLNQ 367
Cdd:PRK06687  241 LGYldHPSVFAHGVElnEREIERLASSQVAIAH-------NPISNLKLASGIAPIIQLQKAGVAVgIATDSVASNNNLDM 313

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1027773277 368 -EAGKVM-----YRANDVGYDISEQhAIKWITSNAAKSLGIDDKTGSLEAGKQADVVI 419
Cdd:PRK06687  314 fEEGRTAallqkMKSGDASQFPIET-ALKVLTIEGAKALGMENQIGSLEVGKQADFLV 370
PRK08204 PRK08204
hypothetical protein; Provisional
 49-419 1.26e-10

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 63.10  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  49 TLITNATVLTGTGER--LDDADVFFVDGKVQQVGKDLSVQADKTIDAQGKWVTPGIIDVHSHLGAYPTPSVASHQDGNEM 126
Cdd:PRK08204    4 TLIRGGTVLTMDPAIgdLPRGDILIEGDRIAAVAPSIEAPDAEVVDARGMIVMPGLVDTHRHTWQSVLRGIGADWTLQTY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 127 TSPVTAEVWVEHSvwPQDpgfnrareggiTSLQILPGSANLIGGrGVTLKNIPSHTMQGMKFPDAPY-GLKMA------- 198
Cdd:PRK08204   84 FREIHGNLGPMFR--PED-----------VYIANLLGALEALDA-GVTTLLDWSHINNSPEHADAAIrGLAEAgiravfa 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 199 ---CGENP--------------KRVygRKGVLPSTR----MGnMA----GYRT--AWIDATEYKREWDKYESDYAAGKNP 251
Cdd:PRK08204  150 hgsPGPSPywpfdsvphprediRRV--KKRYFSSDDglltLG-LAirgpEFSSweVARADFRLARELGLPISMHQGFGPW 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 252 AAPHRDIKLDTLAGVLEGDI-LIHNHCYKAEEMAMMIDLGkefgyhsGTF----------HHGveaYKIADLLAENGNCA 320
Cdd:PRK08204  227 GATPRGVEQLHDAGLLGPDLnLVHGNDLSDDELKLLADSG-------GSFsvtpeiemmmGHG---YPVTGRLLAHGVRP 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 321 ALwpdwwGFKMEAY---DMVQENVAIVDAVKNSCAVVHSDSDTTIqrlnqeAGKVMYRANDVgydiseqhaIKWITSNAA 397
Cdd:PRK08204  297 SL-----GVDVVTStggDMFTQMRFALQAERARDNAVHLREGGMP------PPRLTLTARQV---------LEWATIEGA 356

                         410       420
                  ....*....|....*....|..
gi 1027773277 398 KSLGIDDKTGSLEAGKQADVVI 419
Cdd:PRK08204  357 RALGLEDRIGSLTPGKQADLVL 378
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
50-113 7.36e-10

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 60.63  E-value: 7.36e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027773277  50 LITNATVLTGTGERLDDADVFFVDGKVQQVGKDLSV-QADKTIDAQGKWVTPGIIDVHSHlgAYP 113
Cdd:PRK09237    2 LLRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGsQAKKVIDLSGLYVSPGWIDLHVH--VYP 64
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
50-108 9.07e-10

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 60.11  E-value: 9.07e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1027773277  50 LITNATVLTGTGErLDDADVFFVDGKVQQVGKDLSVQADkTIDAQGKWVTPGIIDVHSH 108
Cdd:COG1820     1 AITNARIFTGDGV-LEDGALLIEDGRIAAIGPGAEPDAE-VIDLGGGYLAPGFIDLHVH 57
PRK06189 PRK06189
allantoinase; Provisional
 50-109 4.95e-09

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 58.17  E-value: 4.95e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  50 LITNATVLTGTGERldDADVFFVDGKVQQVGKDLSVQADKTIDAQGKWVTPGIIDVHSHL 109
Cdd:PRK06189    6 IIRGGKVVTPEGVY--RADIGIKNGKIAEIAPEISSPAREIIDADGLYVFPGMIDVHVHF 63
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 48-110 5.17e-09

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 58.22  E-value: 5.17e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1027773277  48 STLITNATVLTGTGERLDDADVFFVDGKVQQVGKDLSVQADKTIDAQGKWVTPGIIDVHSHLG 110
Cdd:PRK06038    3 DIIIKNAYVLTMDAGDLKKGSVVIEDGTITEVSESTPGDADTVIDAKGSVVMPGLVNTHTHAA 65
Amidohydro_3 pfam07969
Amidohydrolase family;
370-442 5.18e-09

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 58.31  E-value: 5.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 370 GKVMYRANDVGYD--ISEQHAIKWITSNAAKSLGIDDKTGSLEAGKQADVVIWNQNPFSV------YAKAEQVFIDGAKV 441
Cdd:pfam07969 384 RQTAGGGEVLGPDeeLSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVdppaiaDIRVRLTVVDGRVV 463


                  .
gi 1027773277 442 Y 442
Cdd:pfam07969 464 Y 464
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 49-109 7.79e-09

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: 57.68  E-value: 7.79e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027773277  49 TLITNATVLTGTGERldDADVFFVDGKVQQVGKDLS-VQADKTIDAQGKWVTPGIIDVHSHL 109
Cdd:cd01315     2 LVIKNGRVVTPDGVR--EADIAVKGGKIAAIGPDIAnTEAEEVIDAGGLVVMPGLIDTHVHI 61
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 88-424 8.57e-09

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: 56.92  E-value: 8.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  88 DKTIDAQGKWVTPGIIDVHSHLGAYPTPSVASHQDGNEMTSpVTAEVWVEHsvwpqdpgfnrAREGGITSLQILPGSANL 167
Cdd:cd01299     1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVEYRT-IRATRQARA-----------ALRAGFTTVRDAGGADYG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 168 IGGRGVTLKNIPS----HTMQGMK--------FPDAPYGLKMACGENPKRVYG-RKGVLPSTRMGN-----MAGYRTAW- 228
Cdd:cd01299    69 LLRDAIDAGLIPGprvfASGRALSqtgghgdpRGLSGLFPAGGLAAVVDGVEEvRAAVREQLRRGAdqikiMATGGVLSp 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 229 ---IDATEYKREWDKYESDYAAGKN-PAAPH----RDIKLDTLAGVlegDILIHNHCYKAEEMAMMIDLGkefgyhsgtf 300
Cdd:cd01299   149 gdpPPDTQFSEEELRAIVDEAHKAGlYVAAHaygaEAIRRAIRAGV---DTIEHGFLIDDETIELMKEKG---------- 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 301 hhgveAYKIADLLA----ENGNCAALWPDWWGFKM-EAYDMVQENVAIvdAVKnscAVVH----SDSDTTIQRLNQEAGK 371
Cdd:cd01299   216 -----IFLVPTLATyealAAEGAAPGLPADSAEKVaLVLEAGRDALRR--AHK---AGVKiafgTDAGFPVPPHGWNARE 285

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1027773277 372 VMYRAnDVGYDISEqhAIKWITSNAAKSLGIDDKTGSLEAGKQADVVIWNQNP 424
Cdd:cd01299   286 LELLV-KAGGTPAE--ALRAATANAAELLGLSDELGVIEAGKLADLLVVDGDP 335
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
382-438 1.22e-08

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 56.65  E-value: 1.22e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1027773277 382 DISEQHAIKWITSNAAKSLGIDDKTGSLEAGKQADVVIWNQNpFSVyakaEQVFIDG 438
Cdd:COG1820   321 GLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD-LNV----RATWVGG 372
PRK09236 PRK09236
dihydroorotase; Reviewed
 47-106 2.34e-08

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 56.03  E-value: 2.34e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027773277  47 QSTLITNATVLTgtgE-RLDDADVFFVDGKVQQVGKDLS-VQADKTIDAQGKWVTPGIID--VH 106
Cdd:PRK09236    2 KRILIKNARIVN---EgKIFEGDVLIENGRIAKIASSISaKSADTVIDAAGRYLLPGMIDdqVH 62
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
 48-149 4.60e-08

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 55.19  E-value: 4.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  48 STLITNATVLTGTGERLDDADVFFVDGKVQQVGKDLSVQADKTIDAQGKWVTPGIIDVHSHlgaypTPSVASHQdgneMT 127
Cdd:PRK08393    2 SILIKNGYVIYGENLKVIRADVLIEGNKIVEVKRNINKPADTVIDASGSVVSPGFINAHTH-----SPMVLLRG----LA 72

                          90       100
                  ....*....|....*....|..
gi 1027773277 128 SPVTAEVWVEHSVWPQDPGFNR 149
Cdd:PRK08393   73 DDVPLMEWLQNYIWPRERKLKR 94
PRK02382 PRK02382
dihydroorotase; Provisional
 51-108 7.94e-08

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 54.27  E-value: 7.94e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027773277  51 ITNATVLTG---TGERLDDADVFFVDGKVQQVGKDLSV-QADKTIDAQGKWVTPGIIDVHSH 108
Cdd:PRK02382    1 MRDALLKDGrvyYNNSLQPRDVRIDGGKITAVGKDLDGsSSEEVIDARGMLLLPGGIDVHVH 62
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 379-421 7.99e-08

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: 54.19  E-value: 7.99e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1027773277 379 VGYDISEQHAIKWITSNAAKSLGIDDKTGSLEAGKQADVVIWN 421
Cdd:cd01296   306 RLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 383-438 8.07e-08

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: 54.12  E-value: 8.07e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1027773277 383 ISEQHAIKWITSNAAKSLGIDDKTGSLEAGKQADVVIWNQNpFSVyakaEQVFIDG 438
Cdd:cd00854   324 CPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD-LNV----KATWING 374
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 49-109 9.63e-08

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 54.32  E-value: 9.63e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027773277  49 TLITNATVLTGTGERldDADVFFVDGKVQQVGKDLSvQADKTIDAQGKWVTPGIIDVHSHL 109
Cdd:PRK13404    6 LVIRGGTVVTATDTF--QADIGIRGGRIAALGEGLG-PGAREIDATGRLVLPGGVDSHCHI 63
PRK09061 PRK09061
D-glutamate deacylase; Validated
 49-108 2.40e-07

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 53.16  E-value: 2.40e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027773277  49 TLITNATVLT-GTGerLDD-ADVFFVDGKVQQVGKDLsVQADKTIDAQGKWVTPGIIDVHSH 108
Cdd:PRK09061   21 LVIRNGRVVDpETG--LDAvRDVGIKGGKIAAVGTAA-IEGDRTIDATGLVVAPGFIDLHAH 79
PLN02942 PLN02942
dihydropyrimidinase
 44-109 3.01e-07

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 52.54  E-value: 3.01e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027773277  44 LASQSTLITNATVLTGTGERLddADVFFVDGKVQQVGKDLSVQAD-KTIDAQGKWVTPGIIDVHSHL 109
Cdd:PLN02942    2 ASSTKILIKGGTVVNAHHQEL--ADVYVEDGIIVAVAPNLKVPDDvRVIDATGKFVMPGGIDPHTHL 66
PRK07575 PRK07575
dihydroorotase; Provisional
 46-106 3.77e-07

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 52.37  E-value: 3.77e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027773277  46 SQSTLITNATVLTGTGErLDDADVFFVDGKVQQVGKDLSVQA-DKTIDAQGKWVTPGIID--VH 106
Cdd:PRK07575    2 MMSLLIRNARILLPSGE-LLLGDVLVEDGKIVAIAPEISATAvDTVIDAEGLTLLPGVIDpqVH 64
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
388-418 6.65e-07

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 51.45  E-value: 6.65e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1027773277 388 AIKWITSNAAKSLGIDDKTGSLEAGKQADVV 418
Cdd:PRK09045  345 ALRMATLNGARALGLDDEIGSLEPGKQADLV 375
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
49-108 6.85e-07

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 51.64  E-value: 6.85e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027773277  49 TLITNATVL-TGTGERLDdADVFFVDGKVQQVGkDLSVQADKTIDAQGKWVTPGIIDVHSH 108
Cdd:COG1001     7 LVIKNGRLVnVFTGEILE-GDIAIAGGRIAGVG-DYIGEATEVIDAAGRYLVPGFIDGHVH 65
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
48-109 7.75e-07

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 51.15  E-value: 7.75e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027773277  48 STLITNATVLTGTGER-LDDADVFFVDGKVQQVGKDLSVQ-ADKTIDAQGKWVTPGIIDVHSHL 109
Cdd:PRK07228    2 TILIKNAGIVTMNAKReIVDGDVLIEDDRIAAVGDRLDLEdYDDHIDATGKVVIPGLIQGHIHL 65
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
 48-110 1.76e-06

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 49.88  E-value: 1.76e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027773277  48 STLITNATVLT-GTGERLDDADVFFVDGKVQQVGKDlSVQADKTIDAQGKWVTPGIIDVHSHLG 110
Cdd:PRK06380    2 SILIKNAWIVTqNEKREILQGNVYIEGNKIVYVGDV-NEEADYIIDATGKVVMPGLINTHAHVG 64
FwdA COG1229
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
49-110 2.84e-06

Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];


Pssm-ID: 440842  Cd Length: 554  Bit Score: 49.81  E-value: 2.84e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1027773277  49 TLITNATV---LTG-TGERlddADVFFVDGKVqqVGKDLSVQADKTIDAQGKWVTPGIIDVHSHLG 110
Cdd:COG1229     3 LIIKNGRVydpANGiDGEV---MDIAIKDGKI--VEEPSDPKDAKVIDASGKVVMAGGVDIHTHIA 63
PRK08044 PRK08044
allantoinase AllB;
49-109 4.23e-06

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 49.08  E-value: 4.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027773277  49 TLITNATVLTGTGERLDDADVFfvDGKVQQVGKDLSvQADKTIDAQGKWVTPGIIDVHSHL 109
Cdd:PRK08044    5 LIIKNGTVILENEARVVDIAVK--GGKIAAIGQDLG-DAKEVMDASGLVVSPGMVDAHTHI 62
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 68-115 4.81e-06

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: 48.48  E-value: 4.81e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1027773277  68 DVFFVDGKVQQVGKDLSVQADKTI-DAQGKWVTPGIIDVHSHLGAYPTP 115
Cdd:cd01307     1 DVAIENGKIAAVGAALAAPAATQIvDAGGCYVSPGWIDLHVHVYQGGTR 49
ureC PRK13308
urease subunit alpha; Reviewed
 393-442 5.78e-06

urease subunit alpha; Reviewed


Pssm-ID: 183965 [Multi-domain]  Cd Length: 569  Bit Score: 48.55  E-value: 5.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1027773277 393 TSNAAKSLGIDDKTGSLEAGKQADVVIWNQNPFSVyaKAEQVFIDGAKVY 442
Cdd:PRK13308  410 TINPAITFGIDDHIGSLEPGKLADIVLWRPAFFGI--KPELVIKGGFPAW 457
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 48-107 9.56e-06

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 47.48  E-value: 9.56e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  48 STLITNATVLTGTGERldDADVFFVDGKVQQVGKDlSVQADKTIDAQGKWVTPGIIDVHS 107
Cdd:PRK15446    3 EMILSNARLVLPDEVV--DGSLLIEDGRIAAIDPG-ASALPGAIDAEGDYLLPGLVDLHT 59
PRK09060 PRK09060
dihydroorotase; Validated
 49-109 1.22e-05

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 47.61  E-value: 1.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027773277  49 TLITNATVLTGTGErlDDADVFFVDGKVQQVGKDLSVQADKTIDAQGKWVTPGIIDVHSHL 109
Cdd:PRK09060    7 LILKGGTVVNPDGE--GRADIGIRDGRIAAIGDLSGASAGEVIDCRGLHVLPGVIDSQVHF 65
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 50-109 1.93e-05

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: 46.86  E-value: 1.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027773277  50 LITNATVLTGTGERlddADVFFVDGKVQQVGKDLSVQADKT-IDAQGKWVTPGIIDVHSHL 109
Cdd:cd01293     1 LLRNARLADGGTAL---VDIAIEDGRIAAIGPALAVPPDAEeVDAKGRLVLPAFVDPHIHL 58
PRK07627 PRK07627
dihydroorotase; Provisional
 51-162 3.29e-05

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 46.21  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  51 ITNATVLTGTGERLDDADVFFVDGKVQQVGKDLS-VQADKTIDAQGKWVTPGIIDVHSHLgayptpsvasHQDGNEMTSP 129
Cdd:PRK07627    5 IKGGRLIDPAAGTDRQADLYVAAGKIAAIGQAPAgFNADKTIDASGLIVCPGLVDLSARL----------REPGYEYKAT 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1027773277 130 VTAEVwvehsvwpqdpgfNRAREGGITSLQILP 162
Cdd:PRK07627   75 LESEM-------------AAAVAGGVTSLVCPP 94
FMDH_A cd01304
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ...
 51-110 4.47e-05

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: 45.87  E-value: 4.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027773277  51 ITNATVLTGTGERLDDA-DVFFVDGKVqqVGKDLSVQADKTIDAQGKWVTPGIIDVHSHLG 110
Cdd:cd01304     1 IKNGTVYDPLNGINGEKmDIFIRDGKI--VESSSGAKPAKVIDASGKVVMAGGVDMHSHIA 59
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 388-419 4.49e-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: 4.49e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1027773277 388 AIKWITSNAAKSLGIDDKTGSLEAGKQADVVI 419
Cdd:cd01300   448 ALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
PRK12394 PRK12394
metallo-dependent hydrolase;
50-108 6.19e-05

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 45.14  E-value: 6.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1027773277  50 LITNATVLTGTGERLDDADVFFVDGKVQQVGKDLSVQADKTIDAQGKWVTPGIIDVHSH 108
Cdd:PRK12394    6 LITNGHIIDPARNINEINNLRIINDIIVDADKYPVASETRIIHADGCIVTPGLIDYHAH 64
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 73-109 9.94e-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: 44.61  E-value: 9.94e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1027773277  73 DGKVQQVG-----KDLSVQADKTIDAQGKWVTPGIIDVHSHL 109
Cdd:cd01300     6 DGRIVAVGsdaeaKALKGPATEVIDLKGKTVLPGFIDSHSHL 47
PRK07572 PRK07572
cytosine deaminase; Validated
 50-111 1.51e-04

cytosine deaminase; Validated


Pssm-ID: 181039  Cd Length: 426  Bit Score: 43.85  E-value: 1.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027773277  50 LITNATVLTGTGerldDADVFFVDGKVQQVGKDLSVQADKTIDAQGKWVTPGIIDVHSHLGA 111
Cdd:PRK07572    5 IVRNANLPDGRT----GIDIGIAGGRIAAVEPGLQAEAAEEIDAAGRLVSPPFVDPHFHMDA 62
PRK09228 PRK09228
guanine deaminase; Provisional
 380-419 1.65e-04

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 43.64  E-value: 1.65e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1027773277 380 GYDISEQHAIKWITSNAAKSLGIDDKTGSLEAGKQADVVI 419
Cdd:PRK09228  345 GYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVV 384
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
393-444 2.03e-04

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 43.45  E-value: 2.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027773277 393 TSNAAKSLGIDDKTGSLEAGKQADVVIWN-----------QNPFS--VY-AKAEQV---FIDGAKVYDR 444
Cdd:PRK07228  347 TLGGAKAAGFEDEIGSLEEGKKADLAILDldglhatpshgVDVLShlVYaAHGSDVettMVDGKIVMED 415
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 50-109 2.11e-04

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 43.69  E-value: 2.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027773277  50 LITNATVLTGTGERLDDAD--VFFVDGKVQQVGK--DLSVQADKTIDAQGKWVTPGIIDVHSHL 109
Cdd:PRK08203    5 IKNPLAIVTMDAARREIADggLVVEGGRIVEVGPggALPQPADEVFDARGHVVTPGLVNTHHHF 68
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 376-442 3.16e-04

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 42.86  E-value: 3.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027773277 376 ANDVGYDISEqhAIKWITSNAAKSLGIDDKtGSLEAGKQADVVIWNQNPFSVYAKAeqVFIDGAKVY 442
Cdd:PRK15446  319 ADDGGLDLPQ--AVALVTANPARAAGLDDR-GEIAPGKRADLVRVRRAGGLPVVRA--VWRGGRRVF 380
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 87-110 8.19e-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: 41.45  E-value: 8.19e-04
                          10        20
                  ....*....|....*....|....
gi 1027773277  87 ADKTIDAQGKWVTPGIIDVHSHLG 110
Cdd:cd01317     1 DAEVIDAEGKILAPGLVDLHVHLR 24
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 383-420 9.96e-04

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 41.38  E-value: 9.96e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1027773277 383 ISEQHAIKWITSNAAKSLGIDDkTGSLEAGKQADVVIW 420
Cdd:PRK08203  351 MTAREALEWATLGGARVLGRDD-IGSLAPGKLADLALF 387
PRK12393 PRK12393
amidohydrolase; Provisional
 46-109 1.20e-03

amidohydrolase; Provisional


Pssm-ID: 237088 [Multi-domain]  Cd Length: 457  Bit Score: 41.21  E-value: 1.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027773277  46 SQSTLITNA----TVLTGTGERLDDADVFFVDGKVQQVGKdLSVQADKT-IDAQGKWVTPGIIDVHSHL 109
Cdd:PRK12393    1 MPSLLIRNAaaimTGLPGDAARLGGPDIRIRDGRIAAIGA-LTPLPGERvIDATDCVVYPGWVNTHHHL 68
PRK15493 PRK15493
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
86-161 1.69e-03

bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;


Pssm-ID: 185390 [Multi-domain]  Cd Length: 435  Bit Score: 40.81  E-value: 1.69e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1027773277  86 QADKTIDAQGKWVTPGIIDVHSHLgayptpsVASHQDGneMTSPVTAEVWVEHSVWPQDPGFNRAREGGITSLQIL 161
Cdd:PRK15493   45 EVDEVIDMKGKWVLPGLVNTHTHV-------VMSLLRG--IGDDMLLQPWLETRIWPLESQFTPELAVASTELGLL 111
PRK05985 PRK05985
cytosine deaminase; Provisional
 49-109 1.88e-03

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 40.30  E-value: 1.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027773277  49 TLITNAtvltgtgeRLDDA---DVFFVDGKVQQVGKDLSVQADKT-IDAQGKWVTPGIIDVHSHL 109
Cdd:PRK05985    4 LLFRNV--------RPAGGaavDILIRDGRIAAIGPALAAPPGAEvEDGGGALALPGLVDGHIHL 60
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 393-421 2.20e-03

Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.


Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 40.34  E-value: 2.20e-03
                          10        20
                  ....*....|....*....|....*....
gi 1027773277 393 TSNAAKSLGIDDKTGSLEAGKQADVVIWN 421
Cdd:cd01303   361 TLGGAEALGLDDKIGNFEVGKEFDAVVID 389
PRK06151 PRK06151
N-ethylammeline chlorohydrolase; Provisional
 48-152 3.03e-03

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180428 [Multi-domain]  Cd Length: 488  Bit Score: 40.03  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277  48 STLITNATVL--TGTGERL-DDADVFFVDGKVQQVGKDLSVQADKTIDAQGKWVTPGIIDVHSHLGAYPTPSVASHQDGn 124
Cdd:PRK06151    2 RTLIKARWVLgfDDGDHRLlRDGEVVFEGDRILFVGHRFDGEVDRVIDAGNALVGPGFIDLDALSDLDTTILGLDNGPG- 80

                          90       100
                  ....*....|....*....|....*...
gi 1027773277 125 emtspvtaevWVEHSVWPQDPGFNRARE 152
Cdd:PRK06151   81 ----------WAKGRVWSRDYVEAGRRE 98
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 49-109 4.86e-03

Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.


Pssm-ID: 238633 [Multi-domain]  Cd Length: 387  Bit Score: 38.91  E-value: 4.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027773277  49 TLITNATVLTGtgERLDDADVFFVDGKVQQVGKDLS---VQADKTIDAQGKWVTPGIIDVHSHL 109
Cdd:cd01308     2 TLIKNAEVYAP--EYLGKKDILIAGGKILAIEDQLNlpgYENVTVVDLHGKILVPGFIDQHVHI 63
FMDH_A cd01304
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ...
 359-435 6.35e-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: 38.93  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027773277 359 DTTIQRLNQEAGKVMYRAN-DVGYDISEqhaIKWIT-SNAAKSLGIDDKtGSLEAGKQADVVIWNQNP----FSVYAKAE 432
Cdd:cd01304   404 AEEIATLHKWAQDRSALPGiDREYSLYE---IAIMTrAGPAKLLGLSDK-GHLGVGADADIAIYDDDPdqvdPSDYEKVE 479


                  ...
gi 1027773277 433 QVF 435
Cdd:cd01304   480 KAF 482
hutI TIGR01224
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ...
 74-109 6.35e-03

imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273512 [Multi-domain]  Cd Length: 377  Bit Score: 38.55  E-value: 6.35e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1027773277  74 GKVQQVGKDLSV---QADKTIDAQGKWVTPGIIDVHSHL 109
Cdd:TIGR01224  11 GKIVWIGQLAALpgeEATEIIDCGGGLVTPGLVDPHTHL 49
Urease_alpha cd00375
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ...
 393-442 7.21e-03

Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.


Pssm-ID: 238221 [Multi-domain]  Cd Length: 567  Bit Score: 38.85  E-value: 7.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1027773277 393 TSNAAKSLGIDDKTGSLEAGKQADVVIWNQNPFSVyaKAEQVFIDGAKVY 442
Cdd:cd00375   409 TINPAIAHGISHEVGSVEVGKLADLVLWEPAFFGV--KPEMVLKGGFIAY 456
PRK08507 PRK08507
prephenate dehydrogenase; Validated
 379-419 7.87e-03

prephenate dehydrogenase; Validated


Pssm-ID: 181452 [Multi-domain]  Cd Length: 275  Bit Score: 37.95  E-value: 7.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1027773277 379 VGYDISEQHAIKwitsnaAKSLGIDDKTGSLEAGKQADVVI 419
Cdd:PRK08507   29 YGYDHNELHLKK------ALELGLVDEIVSFEELKKCDVIF 63
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 372-421 8.43e-03

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: 38.37  E-value: 8.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1027773277 372 VMYRANDVGYDISEQHAIKWITSNAAKSLGIDDktGSLEAGKQADVVIWN 421
Cdd:cd01317   294 LLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFD 341
PRK07203 PRK07203
putative aminohydrolase SsnA;
50-109 9.44e-03

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 38.38  E-value: 9.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1027773277  50 LITNATVLTGTGER--LDDADVFFVDGKVQQVGKDLSVQAD----KTIDAQGKWVTPGIIDVHSHL 109
Cdd:PRK07203    3 LIGNGTAITRDPAKpvIEDGAIAIEGNVIVEIGTTDELKAKypdaEFIDAKGKLIMPGLINSHNHI 68
 
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