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Conserved domains on  [gi|1211981011|ref|WP_088557004|]
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amidohydrolase family protein [Marinobacter sp. es.042]

Protein Classification

N-acyl-D-amino-acid deacylase family protein( domain architecture ID 10790308)

N-acyl-D-amino-acid deacylase family protein may 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

CATH:  2.30.40.10|3.20.20.140|3.30.1490.130
EC:  3.5.1.-
Gene Ontology:  GO:0047420
PubMed:  14736882
SCOP:  4002810

Graphical summary

 Zoom to residue level

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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 ...
 3-582 3.61e-150

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


:

Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 442.31  E-value: 3.61e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   3 QFDTLIVGGRYFDGTGGPSRIAHVGVKDGRVAGVLDQPPEPglATRTIDASGCWVTPGFLDTHTHYDAELLVAPSLSESV 82
Cdd:COG3653     1 MFDLLIRGGTVVDGTGAPPFRADVAIKGGRIVAVGDLAAAE--AARVIDATGLVVAPGFIDIHTHYDLQLLWDPRLEPSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011  83 RHGVTTVLIGSCSLSMVCSDPEDAS---DIFTRVETVPREKvlpilkqHKSWQTPKEWVAFMDQHPLGPNVISFLGHSDL 159
Cdd:COG3653    79 RQGVTTVVMGNCGVSFAPVRPEDRDrliDLMEGVEGIPEGL-------DWDWESFGEYLDALERRGLGVNVASLVGHGTL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 160 RAAVMGLhratdRNVTPTPEEQQKMEALLEEALQEGFLGLSTMCLkwdkvdgdrewskSLPSTYARWREVSRLNALLRRY 239
Cdd:COG3653   152 RAYVMGL-----DDRPPTPEELARMRALLREAMEAGALGLSTGLI-------------YVPGTYASTDELVALAKVVAEY 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 240 GRVHQGAP-NAANplQVTQYLKETLGWLRK---PLKTTLIAMidlKGNPTVKPMASLVGWL--ANSFGGNFRWQLLPTPF 313
Cdd:COG3653   214 GGVYQSHMrDEGD--GLLEAVDELIRIGREagvPVHISHLKA---AGKPNWGKADEVLALIeaARAEGLDVTADVYPYPA 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 314 TVYadGMDIvlfeEFGAGEMALDIRDQLERndlLKDEQYRRKFRKFYKEKLSPRVWQR-DFGDAVILDCP-DKSVVGRNF 391
Cdd:COG3653   289 GST--GLGA----LLPPWAAAGGLDERLAR---LRDPATRARIRAEIEEGLPDNLLGRgGWDNILISDSPpNEPLVGKSL 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 392 AELAADRGIHVVDFFLDMVVAH-GRSLRWFTTvgnHRKDRLRKMVTNPGALITfSDAG----AHIRNmafYNLPLRFLKL 466
Cdd:COG3653   360 AEIAAERGVDPADAALDLLLEEdGRVLIVYFI---MSEEDVRELLRHPWVMIG-SDGGlggkAHPRA---YGTFPRVLGH 432

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 467 VneSHDEGepIMSLERAVHRLTGEQADWLGV-NAGHIRVGDRADITVLDPRGLDQDLEqvewgemenFGLERmvNRVPGc 545
Cdd:COG3653   433 Y--VRERG--VLSLEEAVRKLTSLPADRLGLkDRGLLRPGYRADLVVFDPATLADRAT---------FDLPA--QRADG- 496

                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 1211981011 546 VREVLINGRPAVTNGEVQPALgresgYGHFLRAGASG 582
Cdd:COG3653   497 IRAVIVNGVVVVEDGKPTGAR-----PGRVLRGGGAA 528
 
Name Accession Description Interval E-value
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
 3-582 3.61e-150

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


Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 442.31  E-value: 3.61e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   3 QFDTLIVGGRYFDGTGGPSRIAHVGVKDGRVAGVLDQPPEPglATRTIDASGCWVTPGFLDTHTHYDAELLVAPSLSESV 82
Cdd:COG3653     1 MFDLLIRGGTVVDGTGAPPFRADVAIKGGRIVAVGDLAAAE--AARVIDATGLVVAPGFIDIHTHYDLQLLWDPRLEPSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011  83 RHGVTTVLIGSCSLSMVCSDPEDAS---DIFTRVETVPREKvlpilkqHKSWQTPKEWVAFMDQHPLGPNVISFLGHSDL 159
Cdd:COG3653    79 RQGVTTVVMGNCGVSFAPVRPEDRDrliDLMEGVEGIPEGL-------DWDWESFGEYLDALERRGLGVNVASLVGHGTL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 160 RAAVMGLhratdRNVTPTPEEQQKMEALLEEALQEGFLGLSTMCLkwdkvdgdrewskSLPSTYARWREVSRLNALLRRY 239
Cdd:COG3653   152 RAYVMGL-----DDRPPTPEELARMRALLREAMEAGALGLSTGLI-------------YVPGTYASTDELVALAKVVAEY 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 240 GRVHQGAP-NAANplQVTQYLKETLGWLRK---PLKTTLIAMidlKGNPTVKPMASLVGWL--ANSFGGNFRWQLLPTPF 313
Cdd:COG3653   214 GGVYQSHMrDEGD--GLLEAVDELIRIGREagvPVHISHLKA---AGKPNWGKADEVLALIeaARAEGLDVTADVYPYPA 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 314 TVYadGMDIvlfeEFGAGEMALDIRDQLERndlLKDEQYRRKFRKFYKEKLSPRVWQR-DFGDAVILDCP-DKSVVGRNF 391
Cdd:COG3653   289 GST--GLGA----LLPPWAAAGGLDERLAR---LRDPATRARIRAEIEEGLPDNLLGRgGWDNILISDSPpNEPLVGKSL 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 392 AELAADRGIHVVDFFLDMVVAH-GRSLRWFTTvgnHRKDRLRKMVTNPGALITfSDAG----AHIRNmafYNLPLRFLKL 466
Cdd:COG3653   360 AEIAAERGVDPADAALDLLLEEdGRVLIVYFI---MSEEDVRELLRHPWVMIG-SDGGlggkAHPRA---YGTFPRVLGH 432

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 467 VneSHDEGepIMSLERAVHRLTGEQADWLGV-NAGHIRVGDRADITVLDPRGLDQDLEqvewgemenFGLERmvNRVPGc 545
Cdd:COG3653   433 Y--VRERG--VLSLEEAVRKLTSLPADRLGLkDRGLLRPGYRADLVVFDPATLADRAT---------FDLPA--QRADG- 496

                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 1211981011 546 VREVLINGRPAVTNGEVQPALgresgYGHFLRAGASG 582
Cdd:COG3653   497 IRAVIVNGVVVVEDGKPTGAR-----PGRVLRGGGAA 528
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 5-568 1.27e-71

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: 235.65  E-value: 1.27e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   5 DTLIVGGRYFDGTGGPSRIAHVGVKDGRVAGVLDQPPEPGlaTRTIDASGCWVTPGFLDTHTHYDAELLVAPSLSESVRH 84
Cdd:cd01297     1 DLVIRNGTVVDGTGAPPFTADVGIRDGRIAAIGPILSTSA--REVIDAAGLVVAPGFIDVHTHYDGQVFWDPDLRPSSRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011  85 GVTTVLIGSCSLSMVCSDPEDASDIFTRVET-VPREKVLPIlkqhkSWQTPKEWVAFMDQHPLGPNVISFLGHSDLRAAV 163
Cdd:cd01297    79 GVTTVVLGNCGVSPAPANPDDLARLIMLMEGlVALGEGLPW-----GWATFAEYLDALEARPPAVNVAALVGHAALRRAV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 164 MGlhratDRNVTPTPEEQQKMEALLEEALQEGFLGLSTMCLKWdkvdgdrewskslPSTYARWREVSRLNALLRRYGRVH 243
Cdd:cd01297   154 MG-----LDAREATEEELAKMRELLREALEAGALGISTGLAYA-------------PRLYAGTAELVALARVAARYGGVY 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 244 QGAPnaanplqvtqylketlgwlrkplkttliamiDLKGNPTVKPMASLVGwLANSFGGNFRWQLLPTPFTVYADGMDIV 323
Cdd:cd01297   216 QTHV-------------------------------RYEGDSILEALDELLR-LGRETGRPVHISHLKSAGAPNWGKIDRL 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 324 LFEEFGAGEMALDIRDQlerndllkdeqyrrkfrkfykekLSPRVwqrdfgdavildcpdksvvgrnfAELAADrgihvv 403
Cdd:cd01297   264 LALIEAARAEGLQVTAD-----------------------VYPYG-----------------------AGSEDD------ 291

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 404 dffldmvvahgrslrwfttvgnhrkdrLRKMVTNPGALItFSDAGA----HIRNMAFYnlPLRFLKLVNEshdegEPIMS 479
Cdd:cd01297   292 ---------------------------VRRIMAHPVVMG-GSDGGAlgkpHPRSYGDF--TRVLGHYVRE-----RKLLS 336

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 480 LERAVHRLTGEQADWLGV-NAGHIRVGDRADITVLDPRGLdQDLEQVEwgemenfglerMVNRVPGCVREVLINGRPAVT 558
Cdd:cd01297   337 LEEAVRKMTGLPARVFGLaDRGRIAPGYRADIVVFDPDTL-ADRATFT-----------RPNQPAEGIEAVLVNGVPVVR 404

                         570
                  ....*....|.
gi 1211981011 559 NGEVQPAL-GR 568
Cdd:cd01297   405 DGAFTGARpGR 415
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
7-95 1.00e-12

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 69.88  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   7 LIVGGRYFDGTGGPSRIAHVGVKDGRVAGVLDQPPEPGlATRTIDASGCWVTPGFLDTHTH---------YDAELLvaps 77
Cdd:PRK09237    2 LLRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGSQ-AKKVIDLSGLYVSPGWIDLHVHvypgstpygDEPDEV---- 76

                          90
                  ....*....|....*....
gi 1211981011  78 lseSVRHGVTTVL-IGSCS 95
Cdd:PRK09237   77 ---GVRSGVTTVVdAGSAG 92
ade TIGR01178
adenine deaminase; The family described by this model includes an experimentally characterized ...
 5-91 1.92e-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: 44.38  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   5 DTLIVGGRYFDGTGGPSRIAHVGVKDGRVAGVldqppEPGLATRTIDASGCWVTPGFLDTHTHYDAELLVaPSLSES--V 82
Cdd:TIGR01178   1 DIVIKNAKIIDVYNGEIIPGDIAIANGHIAGV-----GKYNGVKVIDALGEYAVPGFIDAHIHIESSMLT-PSEFAKlvL 74


                  ....*....
gi 1211981011  83 RHGVTTVLI 91
Cdd:TIGR01178  75 PHGVTTVVS 83
Amidohydro_3 pfam07969
Amidohydrolase family;
48-557 4.60e-04

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 42.90  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011  48 RTIDASGCWVTPGFLDTHTHydaellvapslsesvrhgvttvLIGSCSLSMVCSDPEDASDIFTRVETVPREKVLPILkq 127
Cdd:pfam07969   1 EVIDAKGRLVLPGFVDPHTH----------------------LDGGGLNLRELRLPDVLPNAVVKGQAGRTPKGRWLV-- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 128 HKSWQTPK-EWVAF----------MDQHPlgPNVISFLGHSDLRAAVMgLHRATDRNVTPTPEeqqkMEALLEEALQEGF 196
Cdd:pfam07969  57 GEGWDEAQfAETRFpyaladldevAPDGP--VLLRALHTHAAVANSAA-LDLAGITKATEDPP----GGEIARDANGEGL 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 197 LGLStmclkwdkvdgdREWSKSLPSTYARWREVSRLNALLRRYGR-VHQGAPNAANPlqvTQYLKETLGWLRKPLKTTLI 275
Cdd:pfam07969 130 TGLL------------REGAYALPPLLAREAEAAAVAAALAALPGfGITSVDGGGGN---VHSLDDYEPLRELTAAEKLK 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 276 AMID-LKGNPTVKPMASL----VGWLANSFGGNFRWQLLPTPFTVYADGMDIVLFEEFG-----AGEMALDIRdqLERND 345
Cdd:pfam07969 195 ELLDaPERLGLPHSIYELrigaMKLFADGVLGSRTAALTEPYFDAPGTGWPDFEDEALAelvaaARERGLDVA--IHAIG 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 346 llkDEQYRRKFRKFykEKLSPRVWQRDFGDAV---ILDCPDKSVVGRnFAELAADRGIHVVdffldMVVAHGRSLRWFTT 422
Cdd:pfam07969 273 ---DATIDTALDAF--EAVAEKLGNQGRVRIEhaqGVVPYTYSQIER-VAALGGAAGVQPV-----FDPLWGDWLQDRLG 341

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 423 VGNHRK-DRLRKMVTNPGALITFSDAGAHIRNMAFY---NLPLRFLKLVNESHDEGEpiMSLERAVHRLTGEQADWLG-- 496
Cdd:pfam07969 342 AERARGlTPVKELLNAGVKVALGSDAPVGPFDPWPRigaAVMRQTAGGGEVLGPDEE--LSLEEALALYTSGPAKALGle 419

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1211981011 497 VNAGHIRVGDRADITVldprgLDQDLEQVEwgEMENFGLErmvnrvpgcVREVLINGRPAV 557
Cdd:pfam07969 420 DRKGTLGVGKDADLVV-----LDDDPLTVD--PPAIADIR---------VRLTVVDGRVVY 464
 
Name Accession Description Interval E-value
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
 3-582 3.61e-150

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


Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 442.31  E-value: 3.61e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   3 QFDTLIVGGRYFDGTGGPSRIAHVGVKDGRVAGVLDQPPEPglATRTIDASGCWVTPGFLDTHTHYDAELLVAPSLSESV 82
Cdd:COG3653     1 MFDLLIRGGTVVDGTGAPPFRADVAIKGGRIVAVGDLAAAE--AARVIDATGLVVAPGFIDIHTHYDLQLLWDPRLEPSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011  83 RHGVTTVLIGSCSLSMVCSDPEDAS---DIFTRVETVPREKvlpilkqHKSWQTPKEWVAFMDQHPLGPNVISFLGHSDL 159
Cdd:COG3653    79 RQGVTTVVMGNCGVSFAPVRPEDRDrliDLMEGVEGIPEGL-------DWDWESFGEYLDALERRGLGVNVASLVGHGTL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 160 RAAVMGLhratdRNVTPTPEEQQKMEALLEEALQEGFLGLSTMCLkwdkvdgdrewskSLPSTYARWREVSRLNALLRRY 239
Cdd:COG3653   152 RAYVMGL-----DDRPPTPEELARMRALLREAMEAGALGLSTGLI-------------YVPGTYASTDELVALAKVVAEY 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 240 GRVHQGAP-NAANplQVTQYLKETLGWLRK---PLKTTLIAMidlKGNPTVKPMASLVGWL--ANSFGGNFRWQLLPTPF 313
Cdd:COG3653   214 GGVYQSHMrDEGD--GLLEAVDELIRIGREagvPVHISHLKA---AGKPNWGKADEVLALIeaARAEGLDVTADVYPYPA 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 314 TVYadGMDIvlfeEFGAGEMALDIRDQLERndlLKDEQYRRKFRKFYKEKLSPRVWQR-DFGDAVILDCP-DKSVVGRNF 391
Cdd:COG3653   289 GST--GLGA----LLPPWAAAGGLDERLAR---LRDPATRARIRAEIEEGLPDNLLGRgGWDNILISDSPpNEPLVGKSL 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 392 AELAADRGIHVVDFFLDMVVAH-GRSLRWFTTvgnHRKDRLRKMVTNPGALITfSDAG----AHIRNmafYNLPLRFLKL 466
Cdd:COG3653   360 AEIAAERGVDPADAALDLLLEEdGRVLIVYFI---MSEEDVRELLRHPWVMIG-SDGGlggkAHPRA---YGTFPRVLGH 432

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 467 VneSHDEGepIMSLERAVHRLTGEQADWLGV-NAGHIRVGDRADITVLDPRGLDQDLEqvewgemenFGLERmvNRVPGc 545
Cdd:COG3653   433 Y--VRERG--VLSLEEAVRKLTSLPADRLGLkDRGLLRPGYRADLVVFDPATLADRAT---------FDLPA--QRADG- 496

                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 1211981011 546 VREVLINGRPAVTNGEVQPALgresgYGHFLRAGASG 582
Cdd:COG3653   497 IRAVIVNGVVVVEDGKPTGAR-----PGRVLRGGGAA 528
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 5-568 1.27e-71

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: 235.65  E-value: 1.27e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   5 DTLIVGGRYFDGTGGPSRIAHVGVKDGRVAGVLDQPPEPGlaTRTIDASGCWVTPGFLDTHTHYDAELLVAPSLSESVRH 84
Cdd:cd01297     1 DLVIRNGTVVDGTGAPPFTADVGIRDGRIAAIGPILSTSA--REVIDAAGLVVAPGFIDVHTHYDGQVFWDPDLRPSSRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011  85 GVTTVLIGSCSLSMVCSDPEDASDIFTRVET-VPREKVLPIlkqhkSWQTPKEWVAFMDQHPLGPNVISFLGHSDLRAAV 163
Cdd:cd01297    79 GVTTVVLGNCGVSPAPANPDDLARLIMLMEGlVALGEGLPW-----GWATFAEYLDALEARPPAVNVAALVGHAALRRAV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 164 MGlhratDRNVTPTPEEQQKMEALLEEALQEGFLGLSTMCLKWdkvdgdrewskslPSTYARWREVSRLNALLRRYGRVH 243
Cdd:cd01297   154 MG-----LDAREATEEELAKMRELLREALEAGALGISTGLAYA-------------PRLYAGTAELVALARVAARYGGVY 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 244 QGAPnaanplqvtqylketlgwlrkplkttliamiDLKGNPTVKPMASLVGwLANSFGGNFRWQLLPTPFTVYADGMDIV 323
Cdd:cd01297   216 QTHV-------------------------------RYEGDSILEALDELLR-LGRETGRPVHISHLKSAGAPNWGKIDRL 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 324 LFEEFGAGEMALDIRDQlerndllkdeqyrrkfrkfykekLSPRVwqrdfgdavildcpdksvvgrnfAELAADrgihvv 403
Cdd:cd01297   264 LALIEAARAEGLQVTAD-----------------------VYPYG-----------------------AGSEDD------ 291

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 404 dffldmvvahgrslrwfttvgnhrkdrLRKMVTNPGALItFSDAGA----HIRNMAFYnlPLRFLKLVNEshdegEPIMS 479
Cdd:cd01297   292 ---------------------------VRRIMAHPVVMG-GSDGGAlgkpHPRSYGDF--TRVLGHYVRE-----RKLLS 336

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 480 LERAVHRLTGEQADWLGV-NAGHIRVGDRADITVLDPRGLdQDLEQVEwgemenfglerMVNRVPGCVREVLINGRPAVT 558
Cdd:cd01297   337 LEEAVRKMTGLPARVFGLaDRGRIAPGYRADIVVFDPDTL-ADRATFT-----------RPNQPAEGIEAVLVNGVPVVR 404

                         570
                  ....*....|.
gi 1211981011 559 NGEVQPAL-GR 568
Cdd:cd01297   405 DGAFTGARpGR 415
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
5-89 1.52e-16

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 81.75  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   5 DTLIVGGRYFDGTGGPSRIAHVGVKDGRVAGVlDQPPEPGLATRTIDASGCWVTPGFLDTHTH---YDAELLVAPSLSeS 81
Cdd:COG3964     1 DLLIKGGRVIDPANGIDGVMDIAIKDGKIAAV-AKDIDAAEAKKVIDASGLYVTPGLIDLHTHvfpGGTDYGVDPDGV-G 78


                  ....*...
gi 1211981011  82 VRHGVTTV 89
Cdd:COG3964    79 VRSGVTTV 86
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
7-95 1.00e-12

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 69.88  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   7 LIVGGRYFDGTGGPSRIAHVGVKDGRVAGVLDQPPEPGlATRTIDASGCWVTPGFLDTHTH---------YDAELLvaps 77
Cdd:PRK09237    2 LLRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGSQ-AKKVIDLSGLYVSPGWIDLHVHvypgstpygDEPDEV---- 76

                          90
                  ....*....|....*....
gi 1211981011  78 lseSVRHGVTTVL-IGSCS 95
Cdd:PRK09237   77 ---GVRSGVTTVVdAGSAG 92
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
4-89 1.89e-12

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 69.74  E-value: 1.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   4 FDTLIVGGRYFDGTGGPSRIAHVGVKDGRVAGVLDQPPEpglATRTIDASGCWVTPGFLDTHTHYDAELLVAPSLSESV- 82
Cdd:COG1001     5 ADLVIKNGRLVNVFTGEILEGDIAIAGGRIAGVGDYIGE---ATEVIDAAGRYLVPGFIDGHVHIESSMVTPAEFARAVl 81


                  ....*..
gi 1211981011  83 RHGVTTV 89
Cdd:COG1001    82 PHGTTTV 88
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 5-95 9.09e-12

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 66.91  E-value: 9.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   5 DTLIVGGRYFDGTGG-PSRIAHVGVKDGRVAGV-----LDQPPepglATRTIDASGCWVTPGFLDTHTHY---------- 68
Cdd:COG1228     9 TLLITNATLVDGTGGgVIENGTVLVEDGKIAAVgpaadLAVPA----GAEVIDATGKTVLPGLIDAHTHLglgggravef 84

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1211981011  69 ----------DAELLVAPSLSESVRHGVTTVLIGSCS 95
Cdd:COG1228    85 eagggitptvDLVNPADKRLRRALAAGVTTVRDLPGG 121
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 7-69 2.84e-11

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: 65.88  E-value: 2.84e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1211981011   7 LIVGGRYFDGTGgpSRIAHVGVKDGRVAGVLDQPPEPGlATRTIDASGCWVTPGFLDTHTHYD 69
Cdd:COG0044     1 LIKNGRVVDPGG--LERADVLIEDGRIAAIGPDLAAPE-AAEVIDATGLLVLPGLIDLHVHLR 60
PRK09061 PRK09061
D-glutamate deacylase; Validated
 1-90 8.41e-11

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 64.33  E-value: 8.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   1 MNQFDTLIVGGRYFDGTGGPSRIAHVGVKDGRVAGVLDQppePGLATRTIDASGCWVTPGFLDTHTHYDAellvAPSLSE 80
Cdd:PRK09061   16 MAPYDLVIRNGRVVDPETGLDAVRDVGIKGGKIAAVGTA---AIEGDRTIDATGLVVAPGFIDLHAHGQS----VAAYRM 88

                          90
                  ....*....|
gi 1211981011  81 SVRHGVTTVL 90
Cdd:PRK09061   89 QAFDGVTTAL 98
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 6-77 2.15e-10

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: 63.01  E-value: 2.15e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1211981011   6 TLIVGGRYFDGTGgpSRIAHVGVKDGRVAGV-LDQPPEPGlaTRTIDASGCWVTPGFLDTHTHYDAELLVAPS 77
Cdd:cd01314     1 LIIKNGTIVTADG--SFKADILIEDGKIVAIgPNLEAPGG--VEVIDATGKYVLPGGIDPHTHLELPFMGTVT 69
pyrC PRK09357
dihydroorotase; Validated
 6-124 2.29e-09

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 59.82  E-value: 2.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   6 TLIVGGRYFDGTGGPSRiAHVGVKDGRVAGVLDQPPEPGlaTRTIDASGCWVTPGFLDTHTHY------DAELLVAPSLS 79
Cdd:PRK09357    3 ILIKNGRVIDPKGLDEV-ADVLIDDGKIAAIGENIEAEG--AEVIDATGLVVAPGLVDLHVHLrepgqeDKETIETGSRA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1211981011  80 eSVRHGVTTVLIgscslsM-----VCSDPEDASDIFTRVETVPREKVLPI 124
Cdd:PRK09357   80 -AAAGGFTTVVA------MpntkpVIDTPEVVEYVLDRAKEAGLVDVLPV 122
PRK08323 PRK08323
phenylhydantoinase; Validated
 4-69 6.51e-09

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 58.26  E-value: 6.51e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1211981011   4 FDTLIVGGRYFDGTGgpSRIAHVGVKDGRVAGVLdqppePGLATRTIDASGCWVTPGFLDTHTHYD 69
Cdd:PRK08323    1 MSTLIKNGTVVTADD--TYKADVLIEDGKIAAIG-----ANLGDEVIDATGKYVMPGGIDPHTHME 59
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 1-71 1.17e-08

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 57.79  E-value: 1.17e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1211981011   1 MNQFDTLIVGGRYFDGTGgpSRIAHVGVKDGRVAGVLDQPPEpglATRTIDASGCWVTPGFLDTHTHYDAE 71
Cdd:PRK13404    1 MMAFDLVIRGGTVVTATD--TFQADIGIRGGRIAALGEGLGP---GAREIDATGRLVLPGGVDSHCHIDQP 66
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
7-90 1.83e-08

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 56.65  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   7 LIVGGRYFDGTGGPSRIAhVGVKDGRVAGVLdqpPEPGLATRTIDASGCWVTPGFLDTHTH---------YDAELLVAps 77
Cdd:COG1820     1 AITNARIFTGDGVLEDGA-LLIEDGRIAAIG---PGAEPDAEVIDLGGGYLAPGFIDLHVHggggvdfmdGTPEALRT-- 74

                          90
                  ....*....|....
gi 1211981011  78 LSES-VRHGVTTVL 90
Cdd:COG1820    75 IARAhARHGTTSFL 88
PRK12394 PRK12394
metallo-dependent hydrolase;
3-90 3.61e-08

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 55.92  E-value: 3.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   3 QFDTLIVGGRYFDGTGGPSRIAHVGVKDGRVAGvLDQPPEPGlATRTIDASGCWVTPGFLDTHTHY---DAELLVAPSLS 79
Cdd:PRK12394    2 KNDILITNGHIIDPARNINEINNLRIINDIIVD-ADKYPVAS-ETRIIHADGCIVTPGLIDYHAHVfydGTEGGVRPDMY 79

                          90
                  ....*....|.
gi 1211981011  80 eSVRHGVTTVL 90
Cdd:PRK12394   80 -MPPNGVTTVV 89
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 5-90 4.48e-08

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: 55.60  E-value: 4.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   5 DTLIVGGR--YFDGTGGPSRIAHVGVKDGRVAGVLD--QPPEPGLATRTIDASGCWVTPGFLDTHTHY----------DA 70
Cdd:COG0402     1 DLLIRGAWvlTMDPAGGVLEDGAVLVEDGRIAAVGPgaELPARYPAAEVIDAGGKLVLPGLVNTHTHLpqtllrgladDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1211981011  71 ELL------VAP----------------SLSESVRHGVTTVL 90
Cdd:COG0402    81 PLLdwleeyIWPlearldpedvyagallALAEMLRSGTTTVA 122
PRK07572 PRK07572
cytosine deaminase; Validated
 4-72 1.42e-07

cytosine deaminase; Validated


Pssm-ID: 181039  Cd Length: 426  Bit Score: 53.87  E-value: 1.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1211981011   4 FDTLIVGGRYFDGTGGpsriAHVGVKDGRVAGVldqppEPGL---ATRTIDASGCWVTPGFLDTHTHYDAEL 72
Cdd:PRK07572    2 FDLIVRNANLPDGRTG----IDIGIAGGRIAAV-----EPGLqaeAAEEIDAAGRLVSPPFVDPHFHMDATL 64
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 5-67 1.43e-07

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: 54.22  E-value: 1.43e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1211981011   5 DTLIVGGRYFDGTGgpSRIAHVGVKDGRVAGVLDQPPEPGlATRTIDASGCWVTPGFLDTHTH 67
Cdd:cd01315     1 DLVIKNGRVVTPDG--VREADIAVKGGKIAAIGPDIANTE-AEEVIDAGGLVVMPGLIDTHVH 60
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 26-95 2.54e-07

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: 52.72  E-value: 2.54e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1211981011  26 VGVKDGRVAGVLDQPPePGLATRTIDASGCWVTPGFLDTHTH---YDAELLVAPSlSESVRHGVTTVL-IGSCS 95
Cdd:cd01307     2 VAIENGKIAAVGAALA-APAATQIVDAGGCYVSPGWIDLHVHvyqGGTRYGDRPD-MIGVKSGVTTVVdAGSAG 73
PRK07627 PRK07627
dihydroorotase; Provisional
 8-63 6.52e-07

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 51.99  E-value: 6.52e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1211981011   8 IVGGRYFDGTGGPSRIAHVGVKDGRVAGvLDQPPEPGLATRTIDASGCWVTPGFLD 63
Cdd:PRK07627    5 IKGGRLIDPAAGTDRQADLYVAAGKIAA-IGQAPAGFNADKTIDASGLIVCPGLVD 59
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 6-90 9.15e-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: 51.43  E-value: 9.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   6 TLIVGGRYFDGTGgpSRIAHVGVKDGRVAGVLDQPPEPGlATRTIDASGCWVTPGFLDTHTH-----------YDAELLV 74
Cdd:cd00854     1 LIIKNARILTPGG--LEDGAVLVEDGKIVAIGPEDELEE-ADEIIDLKGQYLVPGFIDIHIHggggadfmdgtAEALKTI 77

                          90
                  ....*....|....*.
gi 1211981011  75 APSLsesVRHGVTTVL 90
Cdd:cd00854    78 AEAL---AKHGTTSFL 90
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 26-67 1.46e-06

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: 50.72  E-value: 1.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1211981011  26 VGVKDGRVAGV---LDQPPEPGLATRTIDASGCWVTPGFLDTHTH 67
Cdd:cd01296     1 IAIRDGRIAAVgpaASLPAPGPAAAEEIDAGGRAVTPGLVDCHTH 45
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 15-67 2.01e-06

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 50.62  E-value: 2.01e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1211981011  15 DGTGGPSRIAHVGVKDGRVAGVLDQPPEPGLATRTIDASGCWVTPGFLDTHTH 67
Cdd:PRK08203   15 DAARREIADGGLVVEGGRIVEVGPGGALPQPADEVFDARGHVVTPGLVNTHHH 67
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
5-80 2.14e-06

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 50.57  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   5 DTLIVGGRYFDGTGGPSRIAHVGVKDGRVAGVLDQ---PPEPGLATRTIDASGCWVTPGFLDTHTHYD--AELLVAPSLS 79
Cdd:COG1574     9 DLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDaevRALAGPATEVIDLGGKTVLPGFIDAHVHLLggGLALLGVDLS 88


                  .
gi 1211981011  80 E 80
Cdd:COG1574    89 G 89
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 24-67 5.27e-06

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: 49.12  E-value: 5.27e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1211981011  24 AHVGVKDGRVAGVLDQPPEPGL-ATRTIDASGCWVTPGFLDTHTH 67
Cdd:cd01298    20 GDVLVEDGRIVAVGPALPLPAYpADEVIDAKGKVVMPGLVNTHTH 64
PRK09060 PRK09060
dihydroorotase; Validated
 4-89 7.92e-06

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 48.38  E-value: 7.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   4 FDTLIVGGRYF--DGTGgpsrIAHVGVKDGRVA--GVLDQPPepglATRTIDASGCWVTPGFLDTHTHY------DAELL 73
Cdd:PRK09060    5 FDLILKGGTVVnpDGEG----RADIGIRDGRIAaiGDLSGAS----AGEVIDCRGLHVLPGVIDSQVHFrepgleHKEDL 76

                          90
                  ....*....|....*.
gi 1211981011  74 VAPSLSeSVRHGVTTV 89
Cdd:PRK09060   77 ETGSRA-AVLGGVTAV 91
FwdA COG1229
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
6-67 9.12e-06

Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];


Pssm-ID: 440842  Cd Length: 554  Bit Score: 48.65  E-value: 9.12e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1211981011   6 TLIVGGRYFDGTGGPS-RIAHVGVKDGRVAgvldQPPEPGLATRTIDASGCWVTPGFLDTHTH 67
Cdd:COG1229     3 LIIKNGRVYDPANGIDgEVMDIAIKDGKIV----EEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
PRK05985 PRK05985
cytosine deaminase; Provisional
 5-82 1.37e-05

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 47.62  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   5 DTLIVGGRYFDGtggpsRIAHVGVKDGRVAGVLDQ-PPEPGLATrtIDASGCWVTPGFLDTHTHYDAELL--------VA 75
Cdd:PRK05985    3 DLLFRNVRPAGG-----AAVDILIRDGRIAAIGPAlAAPPGAEV--EDGGGALALPGLVDGHIHLDKTFWgdpwypnePG 75


                  ....*..
gi 1211981011  76 PSLSESV 82
Cdd:PRK05985   76 PSLRERI 82
ureC PRK13308
urease subunit alpha; Reviewed
 24-93 1.46e-05

urease subunit alpha; Reviewed


Pssm-ID: 183965 [Multi-domain]  Cd Length: 569  Bit Score: 47.78  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011  24 AHVGVKDGRVAGV-----------LDQPPEPGLATRTIDASGCWVTPGFLDTHTHYDAELLVAPSLSEsvrhGVTTVLIG 92
Cdd:PRK13308   87 GDIGIRDGRIVGIgkagnpdimdgVDPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQLVDHALAS----GITTMLGG 162


                  .
gi 1211981011  93 S 93
Cdd:PRK13308  163 G 163
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 25-67 1.58e-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: 47.69  E-value: 1.58e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1211981011  25 HVGVKDGRVAGV---LDQPPEPGLATRTIDASGCWVTPGFLDTHTH 67
Cdd:cd01300     1 AVAVRDGRIVAVgsdAEAKALKGPATEVIDLKGKTVLPGFIDSHSH 46
PRK07627 PRK07627
dihydroorotase; Provisional
 478-556 4.90e-05

dihydroorotase; Provisional


Pssm-ID: 181059 [Multi-domain]  Cd Length: 425  Bit Score: 45.82  E-value: 4.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 478 MSLERAVHRLTGEQADWLGVNAGHIRVGDRADITVLDP--------RGLDQDLEQVEWGEMEnfglermvnrVPGCVREV 549
Cdd:PRK07627  345 VPLARALARITSAPARVLGLPAGRLAEGAPADLCVFDPdahwrvepRALKSQGKNTPFLGYE----------LPGRVRAT 414


                  ....*..
gi 1211981011 550 LINGRPA 556
Cdd:PRK07627  415 LVAGQVA 421
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 17-69 7.21e-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: 45.32  E-value: 7.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1211981011  17 TGGPSRIAHVGVKDGRVAGVLDQPPEPGLATRtIDASGCWVTPGFLDTHTHYD 69
Cdd:cd01293     8 ADGGTALVDIAIEDGRIAAIGPALAVPPDAEE-VDAKGRLVLPAFVDPHIHLD 59
PRK12393 PRK12393
amidohydrolase; Provisional
 17-67 1.29e-04

amidohydrolase; Provisional


Pssm-ID: 237088 [Multi-domain]  Cd Length: 457  Bit Score: 44.67  E-value: 1.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1211981011  17 TGGPSRIAHVG-----VKDGRVAGVLDQPPEPGlaTRTIDASGCWVTPGFLDTHTH 67
Cdd:PRK12393   14 TGLPGDAARLGgpdirIRDGRIAAIGALTPLPG--ERVIDATDCVVYPGWVNTHHH 67
PRK08044 PRK08044
allantoinase AllB;
3-67 1.86e-04

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 44.08  E-value: 1.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1211981011   3 QFDTLIVGGRYFDGTGgpSRIAHVGVKDGRVAGVLDqppEPGLATRTIDASGCWVTPGFLDTHTH 67
Cdd:PRK08044    2 SFDLIIKNGTVILENE--ARVVDIAVKGGKIAAIGQ---DLGDAKEVMDASGLVVSPGMVDAHTH 61
ade TIGR01178
adenine deaminase; The family described by this model includes an experimentally characterized ...
 5-91 1.92e-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: 44.38  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   5 DTLIVGGRYFDGTGGPSRIAHVGVKDGRVAGVldqppEPGLATRTIDASGCWVTPGFLDTHTHYDAELLVaPSLSES--V 82
Cdd:TIGR01178   1 DIVIKNAKIIDVYNGEIIPGDIAIANGHIAGV-----GKYNGVKVIDALGEYAVPGFIDAHIHIESSMLT-PSEFAKlvL 74


                  ....*....
gi 1211981011  83 RHGVTTVLI 91
Cdd:TIGR01178  75 PHGVTTVVS 83
PRK06189 PRK06189
allantoinase; Provisional
 4-69 2.21e-04

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 43.92  E-value: 2.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1211981011   4 FDTLIVGGRYFDGTGgpSRIAHVGVKDGRVAGVLDQPPEPglATRTIDASGCWVTPGFLDTHTHYD 69
Cdd:PRK06189    3 YDLIIRGGKVVTPEG--VYRADIGIKNGKIAEIAPEISSP--AREIIDADGLYVFPGMIDVHVHFN 64
PLN02303 PLN02303
urease
 5-92 3.01e-04

urease


Pssm-ID: 215172 [Multi-domain]  Cd Length: 837  Bit Score: 43.97  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   5 DTLIVGGRYFDGTGgpsrI--AHVGVKDGRVAG--------VLDQPPEP---GLATRTIDASGCWVTPGFLDTHTHYdae 71
Cdd:PLN02303  335 DTVITNAVIIDYTG----IykADIGIKDGLIVGigkagnpdVMDGVTSNmivGVNTEVIAGEGMIVTAGGIDCHVHF--- 407

                          90       100
                  ....*....|....*....|..
gi 1211981011  72 llVAPSLS-ESVRHGVTTVLIG 92
Cdd:PLN02303  408 --ICPQLAtEAIASGITTLVGG 427
FMDH_A cd01304
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ...
 8-67 3.17e-04

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: 43.56  E-value: 3.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1211981011   8 IVGGRYFDGTGG-PSRIAHVGVKDGRVAgvldQPPEPGLATRTIDASGCWVTPGFLDTHTH 67
Cdd:cd01304     1 IKNGTVYDPLNGiNGEKMDIFIRDGKIV----ESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
AdeC cd01295
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ...
 51-91 3.44e-04

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: 43.37  E-value: 3.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1211981011  51 DASGCWVTPGFLDTHTHYDAELLVAPSLSESV-RHGVTTVLI 91
Cdd:cd01295     1 DAEGKYIVPGFIDAHLHIESSMLTPSEFAKAVlPHGTTTVIA 42
Amidohydro_3 pfam07969
Amidohydrolase family;
48-557 4.60e-04

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 42.90  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011  48 RTIDASGCWVTPGFLDTHTHydaellvapslsesvrhgvttvLIGSCSLSMVCSDPEDASDIFTRVETVPREKVLPILkq 127
Cdd:pfam07969   1 EVIDAKGRLVLPGFVDPHTH----------------------LDGGGLNLRELRLPDVLPNAVVKGQAGRTPKGRWLV-- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 128 HKSWQTPK-EWVAF----------MDQHPlgPNVISFLGHSDLRAAVMgLHRATDRNVTPTPEeqqkMEALLEEALQEGF 196
Cdd:pfam07969  57 GEGWDEAQfAETRFpyaladldevAPDGP--VLLRALHTHAAVANSAA-LDLAGITKATEDPP----GGEIARDANGEGL 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 197 LGLStmclkwdkvdgdREWSKSLPSTYARWREVSRLNALLRRYGR-VHQGAPNAANPlqvTQYLKETLGWLRKPLKTTLI 275
Cdd:pfam07969 130 TGLL------------REGAYALPPLLAREAEAAAVAAALAALPGfGITSVDGGGGN---VHSLDDYEPLRELTAAEKLK 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 276 AMID-LKGNPTVKPMASL----VGWLANSFGGNFRWQLLPTPFTVYADGMDIVLFEEFG-----AGEMALDIRdqLERND 345
Cdd:pfam07969 195 ELLDaPERLGLPHSIYELrigaMKLFADGVLGSRTAALTEPYFDAPGTGWPDFEDEALAelvaaARERGLDVA--IHAIG 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 346 llkDEQYRRKFRKFykEKLSPRVWQRDFGDAV---ILDCPDKSVVGRnFAELAADRGIHVVdffldMVVAHGRSLRWFTT 422
Cdd:pfam07969 273 ---DATIDTALDAF--EAVAEKLGNQGRVRIEhaqGVVPYTYSQIER-VAALGGAAGVQPV-----FDPLWGDWLQDRLG 341

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 423 VGNHRK-DRLRKMVTNPGALITFSDAGAHIRNMAFY---NLPLRFLKLVNESHDEGEpiMSLERAVHRLTGEQADWLG-- 496
Cdd:pfam07969 342 AERARGlTPVKELLNAGVKVALGSDAPVGPFDPWPRigaAVMRQTAGGGEVLGPDEE--LSLEEALALYTSGPAKALGle 419

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1211981011 497 VNAGHIRVGDRADITVldprgLDQDLEQVEwgEMENFGLErmvnrvpgcVREVLINGRPAV 557
Cdd:pfam07969 420 DRKGTLGVGKDADLVV-----LDDDPLTVD--PPAIADIR---------VRLTVVDGRVVY 464
pyrC PRK00369
dihydroorotase; Provisional
 477-564 5.19e-04

dihydroorotase; Provisional


Pssm-ID: 234738 [Multi-domain]  Cd Length: 392  Bit Score: 42.83  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 477 IMSLERAVHRLTGEQADWLGVNAGHIRVGDRADITVL--DPRGLDQDLEQVEWGEMENFGLErmvnrvpGCVREVLINGR 554
Cdd:PRK00369  297 ILSIDRAVELISTNPARILGIPYGEIKEGYRANFTVIqfEDWRYSTKYSKVIETPLDGFELK-------ASVYATIVQGK 369

                          90
                  ....*....|
gi 1211981011 555 PAVTNGEVQP 564
Cdd:PRK00369  370 LAYLEGEVFP 379
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
478-559 5.24e-04

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 42.53  E-value: 5.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 478 MSLERAVHRLTGEQADWLGVNA-GHIRVGDRADITVLdprgldqDLEQVEWGEMENFGLERMVNR--VP-GCVR--EVLI 551
Cdd:PRK09237  296 MPLEEVIAAVTKNAADALRLPElGRLQVGSDADLTLF-------TLKDGPFTLTDSEGDSLIGERllTPlATVRggKVVL 368


                  ....*...
gi 1211981011 552 NGRPAVTN 559
Cdd:PRK09237  369 TEQGSAEH 376
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 48-89 8.13e-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: 41.90  E-value: 8.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1211981011  48 RTIDASGCWVTPGFLDTHTHYDAE----------------LLVAPSLSESVRHGVTTV 89
Cdd:cd01299     2 QVIDLGGKTLMPGLIDAHTHLGSDpgdlpldlalpveyrtIRATRQARAALRAGFTTV 59
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 25-105 8.33e-04

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: 41.99  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011  25 HVGVKD-----GRVAGVLDQPPEPGLATRT-IDASGCWVTPGFLDTHTHY------------DAELlvapSLSESVRHGV 86
Cdd:cd01308    14 YLGKKDiliagGKILAIEDQLNLPGYENVTvVDLHGKILVPGFIDQHVHIiggggeggpstrTPEV----TLSDLTTAGV 89

                          90       100
                  ....*....|....*....|.
gi 1211981011  87 TTV--LIGSCSlsmVCSDPED 105
Cdd:cd01308    90 TTVvgCLGTDG---ISRSMED 107
guan_deamin TIGR02967
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ...
 26-90 1.89e-03

guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 132012 [Multi-domain]  Cd Length: 401  Bit Score: 40.70  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011  26 VGVKDGRVAGV---LDQPPEPGLATRTIDASGCWVTPGFLDTHTHY---------DAELL-------------------- 73
Cdd:TIGR02967   9 LVVENGRIVAVgdyAELKETLPAGVEIDDYRGHLIMPGFIDTHIHYpqtemiasyGEQLLewlekytfptearfadpdha 88

                          90       100
                  ....*....|....*....|
gi 1211981011  74 --VAPS-LSESVRHGVTTVL 90
Cdd:TIGR02967  89 eeVAEFfLDELLRNGTTTAL 108
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 30-67 2.13e-03

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: 40.76  E-value: 2.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1211981011  30 DGRVAGVL--DQPPEpglATRTIDASGCWVTPGFLDTHTH 67
Cdd:cd01309     1 DGKIVAVGaeITTPA---DAEVIDAKGKHVTPGLIDAHSH 37
Urease_alpha cd00375
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ...
 5-92 2.68e-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: 40.78  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011   5 DTLIVGGRYFDGTGgpSRIAHVGVKDGRVAGV-----------LDQPPEPGLATRTIDASGCWVTPGFLDTHTHYdaell 73
Cdd:cd00375    66 DLVITNALIIDYTG--IYKADIGIKDGRIVAIgkagnpdimdgVTPNMIVGPSTEVIAGEGKIVTAGGIDTHVHF----- 138

                          90       100
                  ....*....|....*....|
gi 1211981011  74 VAPSL-SESVRHGVTTVLIG 92
Cdd:cd00375   139 ICPQQiEEALASGITTMIGG 158
hutI TIGR01224
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ...
 26-67 5.17e-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: 39.32  E-value: 5.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1211981011  26 VGVKDGRVAGVLDQPPEPGL-ATRTIDASGCWVTPGFLDTHTH 67
Cdd:TIGR01224   6 ILIHGGKIVWIGQLAALPGEeATEIIDCGGGLVTPGLVDPHTH 48
PRK09236 PRK09236
dihydroorotase; Reviewed
 19-68 5.48e-03

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 39.47  E-value: 5.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1211981011  19 GPSRIAHVGVKDGRVAGVLDQ-PPEPglATRTIDASGCWVTPGFLDTHTHY 68
Cdd:PRK09236   15 GKIFEGDVLIENGRIAKIASSiSAKS--ADTVIDAAGRYLLPGMIDDQVHF 63
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 394-554 5.88e-03

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: 39.02  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 394 LAADRGIHVVDFFLDMVVAHGRSLRWFTTVGNHRK-----DRLRKMVTNpGALITF-SDAGAHIRNMAFynlpLRFLKLV 467
Cdd:pfam01979 185 LILAHGVHLSPTEANLLAEHLKGAGVAHCPFSNSKlrsgrIALRKALED-GVKVGLgTDGAGSGNSLNM----LEELRLA 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011 468 NESHDEGEPIMSLERAVHRLTGEQADWLGV--NAGHIRVGDRADITVLDPRGLDqdleqvewgemENFGLERmvnrvPGC 545
Cdd:pfam01979 260 LELQFDPEGGLSPLEALRMATINPAKALGLddKVGSIEVGKDADLVVVDLDPLA-----------AFFGLKP-----DGN 323


                  ....*....
gi 1211981011 546 VREVLINGR 554
Cdd:pfam01979 324 VKKVIVKGK 332
ureC PRK13207
urease subunit alpha; Reviewed
 24-92 6.22e-03

urease subunit alpha; Reviewed


Pssm-ID: 237305 [Multi-domain]  Cd Length: 568  Bit Score: 39.39  E-value: 6.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1211981011  24 AHVGVKDGRVAGV------LDQPP---EPGLATRTIDASGCWVTPGFLDTHTHYdaellVAPSLSE-SVRHGVTTvLIG 92
Cdd:PRK13207   85 ADIGIKDGRIVAIgkagnpDIQDGvdiIIGPGTEVIAGEGLIVTAGGIDTHIHF-----ICPQQIEeALASGVTT-MIG 157
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 24-90 9.49e-03

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 38.62  E-value: 9.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211981011  24 AHVGVKDGRVAGVlDQPPEPglATRTIDASGCWVTPGFLDTHThyDA-ELLVAP----------SLSES----VRHGVTT 88
Cdd:PRK15446   20 GSLLIEDGRIAAI-DPGASA--LPGAIDAEGDYLLPGLVDLHT--DNlEKHLAPrpgvdwpadaALAAHdaqlAAAGITT 94


                  ..
gi 1211981011  89 VL 90
Cdd:PRK15446   95 VF 96
 
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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