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Conserved domains on  [gi|748803941|ref|WP_040051259|]
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NAD(+) synthase [Caballeronia concitans]

Protein Classification

glutamine-dependent NAD(+) synthetase( domain architecture ID 11479830)

glutamine-dependent NAD(+) synthetase catalyzes the ATP-dependent amidation of deamido-NAD to form NAD; uses L-glutamine as a nitrogen source

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nadE PRK02628
NAD synthetase; Reviewed
 3-683 0e+00

NAD synthetase; Reviewed


:

Pssm-ID: 235057 [Multi-domain]  Cd Length: 679  Bit Score: 1277.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941   3 RNFFNLYSHDFARVAVAIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDLFHQRALLDACEDALRSI 82
Cdd:PRK02628   2 MDFFSIYRHGFVRVAAATPKVRVADPAFNAARILALARRAADDGVALAVFPELSLSGYSCDDLFLQDTLLDAVEDALATL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  83 VEASKEAKIAMIVGLPVRAEHKLFNCAVVVADGAIRGVVPKSYLPNYGEFYEARQFSPADAATARTLSLCGQDVPFGASL 162
Cdd:PRK02628  82 VEASADLDPLLVVGAPLRVRHRLYNCAVVIHRGRILGVVPKSYLPNYREFYEKRWFAPGDGARGETIRLCGQEVPFGTDL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 163 LFQIKDLPLFRFHVEICEDVWVPIPPSSFAALAGATVLVNLSASNIVVGKSAYRHQLVGQQSARCVAAYLYTSAGEGEST 242
Cdd:PRK02628 162 LFEAEDLPGFVFGVEICEDLWVPIPPSSYAALAGATVLANLSASNITVGKADYRRLLVASQSARCLAAYVYAAAGVGEST 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 243 TDLAWDGQGLIYENGEMLAESERFAGESHVIFADVDLERLSRERMKQTTFGRStARHADEVAKFSVVEFALSAPTEDaLP 322
Cdd:PRK02628 242 TDLAWDGQTLIYENGELLAESERFPREEQLIVADVDLERLRQERLRNGSFDDN-ARHRDESAPFRTIPFALDPPAGD-LG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 323 LERRVARFPYVPADRTRRDARCNEVYNIQVQALLQRLRSSGISKVVIGVSGGLDSTHALLVCAKAMDRLGLPRSNILAYT 402
Cdd:PRK02628 320 LRRPVERFPFVPSDPARLDQRCYEAYNIQVSGLAQRLRATGLKKVVIGISGGLDSTHALLVAAKAMDRLGLPRKNILAYT 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 403 MPGFATSDRTLRQARELMQVIGCTAQEIDIRASCAQMLADIGHPHSEENTQYDITYENVQAGERTSHLFRLANLNNAIVI 482
Cdd:PRK02628 400 MPGFATTDRTKNNAVALMKALGVTAREIDIRPAALQMLKDIGHPFARGEPVYDVTFENVQAGERTQILFRLANQHGGIVI 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 483 GTGDLSELALGWCTYGVGDHMSHYNVNASVPKTLITHLVRWVAESGEIGDAGSDVLENVLSTDISPELIPGKESGALEQK 562
Cdd:PRK02628 480 GTGDLSELALGWCTYGVGDHMSHYNVNASVPKTLIQHLIRWVIASGQFDEAVSEVLLDILDTEISPELVPADKEGEIVQS 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 563 TESVIGPYELQDFNLYYTVRFGFAPSKVAFLAHAAWRDRDAGDWPEDPNVARNQYGLADIRKNLRIFLDRFFrTSQFKRS 642
Cdd:PRK02628 560 TEDIIGPYELQDFFLYYFLRYGFRPSKIAFLAWHAWKDAERGAWPGFPEDKRPAYDLATIKKWLEVFLRRFF-SSQFKRS 638

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 748803941 643 CIPNAPKVGSGGSLSPRGDWRAPSDSQATVWLNDLARIPET 683
Cdd:PRK02628 639 ALPNGPKVGSGGSLSPRGDWRAPSDASAAAWLDELERLVPE 679
 
Name Accession Description Interval E-value
nadE PRK02628
NAD synthetase; Reviewed
 3-683 0e+00

NAD synthetase; Reviewed


Pssm-ID: 235057 [Multi-domain]  Cd Length: 679  Bit Score: 1277.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941   3 RNFFNLYSHDFARVAVAIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDLFHQRALLDACEDALRSI 82
Cdd:PRK02628   2 MDFFSIYRHGFVRVAAATPKVRVADPAFNAARILALARRAADDGVALAVFPELSLSGYSCDDLFLQDTLLDAVEDALATL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  83 VEASKEAKIAMIVGLPVRAEHKLFNCAVVVADGAIRGVVPKSYLPNYGEFYEARQFSPADAATARTLSLCGQDVPFGASL 162
Cdd:PRK02628  82 VEASADLDPLLVVGAPLRVRHRLYNCAVVIHRGRILGVVPKSYLPNYREFYEKRWFAPGDGARGETIRLCGQEVPFGTDL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 163 LFQIKDLPLFRFHVEICEDVWVPIPPSSFAALAGATVLVNLSASNIVVGKSAYRHQLVGQQSARCVAAYLYTSAGEGEST 242
Cdd:PRK02628 162 LFEAEDLPGFVFGVEICEDLWVPIPPSSYAALAGATVLANLSASNITVGKADYRRLLVASQSARCLAAYVYAAAGVGEST 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 243 TDLAWDGQGLIYENGEMLAESERFAGESHVIFADVDLERLSRERMKQTTFGRStARHADEVAKFSVVEFALSAPTEDaLP 322
Cdd:PRK02628 242 TDLAWDGQTLIYENGELLAESERFPREEQLIVADVDLERLRQERLRNGSFDDN-ARHRDESAPFRTIPFALDPPAGD-LG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 323 LERRVARFPYVPADRTRRDARCNEVYNIQVQALLQRLRSSGISKVVIGVSGGLDSTHALLVCAKAMDRLGLPRSNILAYT 402
Cdd:PRK02628 320 LRRPVERFPFVPSDPARLDQRCYEAYNIQVSGLAQRLRATGLKKVVIGISGGLDSTHALLVAAKAMDRLGLPRKNILAYT 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 403 MPGFATSDRTLRQARELMQVIGCTAQEIDIRASCAQMLADIGHPHSEENTQYDITYENVQAGERTSHLFRLANLNNAIVI 482
Cdd:PRK02628 400 MPGFATTDRTKNNAVALMKALGVTAREIDIRPAALQMLKDIGHPFARGEPVYDVTFENVQAGERTQILFRLANQHGGIVI 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 483 GTGDLSELALGWCTYGVGDHMSHYNVNASVPKTLITHLVRWVAESGEIGDAGSDVLENVLSTDISPELIPGKESGALEQK 562
Cdd:PRK02628 480 GTGDLSELALGWCTYGVGDHMSHYNVNASVPKTLIQHLIRWVIASGQFDEAVSEVLLDILDTEISPELVPADKEGEIVQS 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 563 TESVIGPYELQDFNLYYTVRFGFAPSKVAFLAHAAWRDRDAGDWPEDPNVARNQYGLADIRKNLRIFLDRFFrTSQFKRS 642
Cdd:PRK02628 560 TEDIIGPYELQDFFLYYFLRYGFRPSKIAFLAWHAWKDAERGAWPGFPEDKRPAYDLATIKKWLEVFLRRFF-SSQFKRS 638

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 748803941 643 CIPNAPKVGSGGSLSPRGDWRAPSDSQATVWLNDLARIPET 683
Cdd:PRK02628 639 ALPNGPKVGSGGSLSPRGDWRAPSDASAAAWLDELERLVPE 679
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 59-670 3.08e-135

NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439941 [Multi-domain]  Cd Length: 542  Bit Score: 408.47  E-value: 3.08e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  59 AYTCDDLFHQRALLDACEDALRSIVEASKEAKIAMIVGLPVRAEHKLFNCAVVVADGAIRGVVPKSYLPNYGEFYEARQF 138
Cdd:COG0171    2 LLLLALLLLAAALLDAAAAAAAALAALAAAAAALLLLLLLLLLLLLLLLALLLLLAAARLLVAAAALLLLALAAGGGAAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 139 SPADAATARTLSLCGQDVPFGASLLFQIKDLPLFRFHVEICEDVWVPIPPSSFAALAGATVLVNLSASNIVVGKSAYRHQ 218
Cdd:COG0171   82 AGGGGGAGGGLLNGAALVLGGGDLLFFADDFLLLLLVVEEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVGAAAAAAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 219 LVGQQSARCVAAYLYTSAGEGESTTDLAWDGQGLIYENGEMLAESERFAGESHVIFADVDLERLSRERMKQTTFGRSTAR 298
Cdd:COG0171  162 LAAALLSSLSSAAYYAAAGGGESTTDLARGGGGGLLLVVLLLVGGGDDDFFDGGSAAVDDDDLLLLLRRRREEELLLARA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 299 HADEVAKFSVVEFALSAPTEDALPLErrvarfpyvpadrtrrdarcnEVYNIQVQALLQRLRSSGISKVVIGVSGGLDST 378
Cdd:COG0171  242 RDADGGRRVAAEAAPPPPEEEEMDLE---------------------EVYDALVLGLRDYVRKNGFKGVVLGLSGGIDSA 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 379 HALLVCAKAmdrlgLPRSNILAYTMPGFATSDRTLRQARELMQVIGCTAQEIDIRASCAQMLADIGHPhsEENTQYDITY 458
Cdd:COG0171  301 LVAALAVDA-----LGPENVLGVTMPSRYTSDESLEDAEELAENLGIEYEEIDITPAVEAFLEALPHA--FGGELDDVAE 373

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 459 ENVQAGERTSHLFRLANLNNAIVIGTGDLSELALGWCTYGvGDHMSHYNVNASVPKTLITHLVRWVAESGEIgdagsdVL 538
Cdd:COG0171  374 ENLQARIRMVILMALANKFGGLVLGTGNKSELAVGYFTKY-GDGAGDLAPIADLYKTQVYALARWLNRNGEV------IP 446

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 539 ENVLSTDISPELIPGkesgaleQKTESVIGPYELQDFNLYYTVRFGFAPSKVAflahAAWRDRDAgdwpedpnvarnqyg 618
Cdd:COG0171  447 EDIIDKPPSAELRPG-------QTDEDELGPYEVLDAILYAYVEEGLSPEEIA----AAGYDREW--------------- 500

                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|..
gi 748803941 619 ladirknLRIFLDRFFRtSQFKRSCIPNAPKVGSgGSLSPrgDWRAPSDSQA 670
Cdd:COG0171  501 -------VERVLRLVRR-NEYKRRQPPPGPKVSS-RAFGR--GRRYPIDSGR 541
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
 15-299 1.82e-114

Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases (class 7 and 8 nitrilases); Glutamine-dependent NAD synthetases are bifunctional enzymes, which have an N-terminal GAT domain and a C-terminal NAD+ synthetase domain. The GAT domain is a glutaminase (EC 3.5.1.2) which hydrolyses L-glutamine to L-glutamate and ammonia. The ammonia is used by the NAD+ synthetase domain in the ATP-dependent amidation of nicotinic acid adenine dinucleotide. Glutamine aminotransferases are categorized depending on their active site residues into different unrelated classes. This class of GAT domain belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to classes 7 and 8. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase forms a homooctamer.


Pssm-ID: 143594 [Multi-domain]  Cd Length: 261  Bit Score: 344.45  E-value: 1.82e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  15 RVAVAIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDLFHQRALLDACEDALRSIVEASKEAKIAMI 94
Cdd:cd07570    1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYPPEDLLLRPDFLEAAEEALEELAAATADLDIAVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  95 VGLPVRAEHKLFNCAVVVADGAIRGVVPKSYLPNYGEFYEARQFSPADAAtartlslcgqdvpfgasLLFQIKDlplFRF 174
Cdd:cd07570   81 VGLPLRHDGKLYNAAAVLQNGKILGVVPKQLLPNYGVFDEKRYFTPGDKP-----------------DVLFFKG---LRI 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 175 HVEICEDVWVPIPPSSFAALAGATVLVNLSASNIVVGKSAYRHQLVGQQSARCVAAYLYTSAGEGesTTDLAWDGQGLIY 254
Cdd:cd07570  141 GVEICEDLWVPDPPSAELALAGADLILNLSASPFHLGKQDYRRELVSSRSARTGLPYVYVNQVGG--QDDLVFDGGSFIA 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 748803941 255 EN-GEMLAESERFAgeshVIFADVDLERLSRERMKQTTFGRSTARH 299
Cdd:cd07570  219 DNdGELLAEAPRFE----EDLADVDLDRLRSERRRNSSFLDEEAEI 260
NAD_synthase pfam02540
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ...
 347-574 2.79e-19

NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.


Pssm-ID: 396888 [Multi-domain]  Cd Length: 241  Bit Score: 87.44  E-value: 2.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  347 VYNIQVQALLQRLRSSGISKVVIGVSGGLDSTHALLVCAKAmdrlgLPRSNILAYTMPGFATSDRTLRQARELMQVIGCT 426
Cdd:pfam02540   1 EINALVDFLRDYVQKAGFKGVVLGLSGGIDSSLVAYLAVKA-----LGKENVLALIMPSSQSSEEDVQDALALAENLGIE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  427 AQEIDIRASCAQMLADIGHphseenTQYDITYENVQAGERTSHLFRLANLNNAIVIGTGDLSELALGWCT-YgvGDHMSH 505
Cdd:pfam02540  76 YKTIDIKPIVRAFSQLFQD------ASEDFAKGNLKARIRMAILYYIANKFNYLVLGTGNKSELAVGYFTkY--GDGACD 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  506 YNVNASVPKTLITHLVRWVAesgeigdagsdVLENVLSTDISPELIPGkesgaleQKTESVIG-PYELQD 574
Cdd:pfam02540 148 IAPIGDLYKTQVYELARYLN-----------VPERIIKKPPSADLWPG-------QTDEEELGiPYDELD 199
nadE TIGR00552
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ...
 355-500 1.22e-14

NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273132 [Multi-domain]  Cd Length: 250  Bit Score: 74.35  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  355 LLQRLRSSGISKVVIGVSGGLDSTHALLVCAKAmdrlgLPRSNILAYTMPGFATSDRTLRQARELMQVIGCTAQEIDIR- 433
Cdd:TIGR00552  13 LRGYVQKSGAKGVVLGLSGGIDSAVVAALCVEA-----LGEQNHALLLPHSVQTPEQDVQDALALAEPLGINYKNIDIAp 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 748803941  434 -ASCAQMLADIGHPHSEEntqydITYENVQAGERTSHLFRLANLNNAIVIGTGDLSELALGWCT-YGVG 500
Cdd:TIGR00552  88 iAASFQAQTETGDELSDF-----LAKGNLKARLRMAALYAIANKHNLLVLGTGNKSELMLGYFTkYGDG 151
 
Name Accession Description Interval E-value
nadE PRK02628
NAD synthetase; Reviewed
 3-683 0e+00

NAD synthetase; Reviewed


Pssm-ID: 235057 [Multi-domain]  Cd Length: 679  Bit Score: 1277.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941   3 RNFFNLYSHDFARVAVAIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDLFHQRALLDACEDALRSI 82
Cdd:PRK02628   2 MDFFSIYRHGFVRVAAATPKVRVADPAFNAARILALARRAADDGVALAVFPELSLSGYSCDDLFLQDTLLDAVEDALATL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  83 VEASKEAKIAMIVGLPVRAEHKLFNCAVVVADGAIRGVVPKSYLPNYGEFYEARQFSPADAATARTLSLCGQDVPFGASL 162
Cdd:PRK02628  82 VEASADLDPLLVVGAPLRVRHRLYNCAVVIHRGRILGVVPKSYLPNYREFYEKRWFAPGDGARGETIRLCGQEVPFGTDL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 163 LFQIKDLPLFRFHVEICEDVWVPIPPSSFAALAGATVLVNLSASNIVVGKSAYRHQLVGQQSARCVAAYLYTSAGEGEST 242
Cdd:PRK02628 162 LFEAEDLPGFVFGVEICEDLWVPIPPSSYAALAGATVLANLSASNITVGKADYRRLLVASQSARCLAAYVYAAAGVGEST 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 243 TDLAWDGQGLIYENGEMLAESERFAGESHVIFADVDLERLSRERMKQTTFGRStARHADEVAKFSVVEFALSAPTEDaLP 322
Cdd:PRK02628 242 TDLAWDGQTLIYENGELLAESERFPREEQLIVADVDLERLRQERLRNGSFDDN-ARHRDESAPFRTIPFALDPPAGD-LG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 323 LERRVARFPYVPADRTRRDARCNEVYNIQVQALLQRLRSSGISKVVIGVSGGLDSTHALLVCAKAMDRLGLPRSNILAYT 402
Cdd:PRK02628 320 LRRPVERFPFVPSDPARLDQRCYEAYNIQVSGLAQRLRATGLKKVVIGISGGLDSTHALLVAAKAMDRLGLPRKNILAYT 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 403 MPGFATSDRTLRQARELMQVIGCTAQEIDIRASCAQMLADIGHPHSEENTQYDITYENVQAGERTSHLFRLANLNNAIVI 482
Cdd:PRK02628 400 MPGFATTDRTKNNAVALMKALGVTAREIDIRPAALQMLKDIGHPFARGEPVYDVTFENVQAGERTQILFRLANQHGGIVI 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 483 GTGDLSELALGWCTYGVGDHMSHYNVNASVPKTLITHLVRWVAESGEIGDAGSDVLENVLSTDISPELIPGKESGALEQK 562
Cdd:PRK02628 480 GTGDLSELALGWCTYGVGDHMSHYNVNASVPKTLIQHLIRWVIASGQFDEAVSEVLLDILDTEISPELVPADKEGEIVQS 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 563 TESVIGPYELQDFNLYYTVRFGFAPSKVAFLAHAAWRDRDAGDWPEDPNVARNQYGLADIRKNLRIFLDRFFrTSQFKRS 642
Cdd:PRK02628 560 TEDIIGPYELQDFFLYYFLRYGFRPSKIAFLAWHAWKDAERGAWPGFPEDKRPAYDLATIKKWLEVFLRRFF-SSQFKRS 638

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 748803941 643 CIPNAPKVGSGGSLSPRGDWRAPSDSQATVWLNDLARIPET 683
Cdd:PRK02628 639 ALPNGPKVGSGGSLSPRGDWRAPSDASAAAWLDELERLVPE 679
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 59-670 3.08e-135

NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439941 [Multi-domain]  Cd Length: 542  Bit Score: 408.47  E-value: 3.08e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  59 AYTCDDLFHQRALLDACEDALRSIVEASKEAKIAMIVGLPVRAEHKLFNCAVVVADGAIRGVVPKSYLPNYGEFYEARQF 138
Cdd:COG0171    2 LLLLALLLLAAALLDAAAAAAAALAALAAAAAALLLLLLLLLLLLLLLLALLLLLAAARLLVAAAALLLLALAAGGGAAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 139 SPADAATARTLSLCGQDVPFGASLLFQIKDLPLFRFHVEICEDVWVPIPPSSFAALAGATVLVNLSASNIVVGKSAYRHQ 218
Cdd:COG0171   82 AGGGGGAGGGLLNGAALVLGGGDLLFFADDFLLLLLVVEEEEEEFVGGPPPPPAALGGAGVLLILSSSSSAVGAAAAAAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 219 LVGQQSARCVAAYLYTSAGEGESTTDLAWDGQGLIYENGEMLAESERFAGESHVIFADVDLERLSRERMKQTTFGRSTAR 298
Cdd:COG0171  162 LAAALLSSLSSAAYYAAAGGGESTTDLARGGGGGLLLVVLLLVGGGDDDFFDGGSAAVDDDDLLLLLRRRREEELLLARA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 299 HADEVAKFSVVEFALSAPTEDALPLErrvarfpyvpadrtrrdarcnEVYNIQVQALLQRLRSSGISKVVIGVSGGLDST 378
Cdd:COG0171  242 RDADGGRRVAAEAAPPPPEEEEMDLE---------------------EVYDALVLGLRDYVRKNGFKGVVLGLSGGIDSA 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 379 HALLVCAKAmdrlgLPRSNILAYTMPGFATSDRTLRQARELMQVIGCTAQEIDIRASCAQMLADIGHPhsEENTQYDITY 458
Cdd:COG0171  301 LVAALAVDA-----LGPENVLGVTMPSRYTSDESLEDAEELAENLGIEYEEIDITPAVEAFLEALPHA--FGGELDDVAE 373

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 459 ENVQAGERTSHLFRLANLNNAIVIGTGDLSELALGWCTYGvGDHMSHYNVNASVPKTLITHLVRWVAESGEIgdagsdVL 538
Cdd:COG0171  374 ENLQARIRMVILMALANKFGGLVLGTGNKSELAVGYFTKY-GDGAGDLAPIADLYKTQVYALARWLNRNGEV------IP 446

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 539 ENVLSTDISPELIPGkesgaleQKTESVIGPYELQDFNLYYTVRFGFAPSKVAflahAAWRDRDAgdwpedpnvarnqyg 618
Cdd:COG0171  447 EDIIDKPPSAELRPG-------QTDEDELGPYEVLDAILYAYVEEGLSPEEIA----AAGYDREW--------------- 500

                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|..
gi 748803941 619 ladirknLRIFLDRFFRtSQFKRSCIPNAPKVGSgGSLSPrgDWRAPSDSQA 670
Cdd:COG0171  501 -------VERVLRLVRR-NEYKRRQPPPGPKVSS-RAFGR--GRRYPIDSGR 541
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
 15-299 1.82e-114

Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases (class 7 and 8 nitrilases); Glutamine-dependent NAD synthetases are bifunctional enzymes, which have an N-terminal GAT domain and a C-terminal NAD+ synthetase domain. The GAT domain is a glutaminase (EC 3.5.1.2) which hydrolyses L-glutamine to L-glutamate and ammonia. The ammonia is used by the NAD+ synthetase domain in the ATP-dependent amidation of nicotinic acid adenine dinucleotide. Glutamine aminotransferases are categorized depending on their active site residues into different unrelated classes. This class of GAT domain belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to classes 7 and 8. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase forms a homooctamer.


Pssm-ID: 143594 [Multi-domain]  Cd Length: 261  Bit Score: 344.45  E-value: 1.82e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  15 RVAVAIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDLFHQRALLDACEDALRSIVEASKEAKIAMI 94
Cdd:cd07570    1 RIALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYPPEDLLLRPDFLEAAEEALEELAAATADLDIAVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  95 VGLPVRAEHKLFNCAVVVADGAIRGVVPKSYLPNYGEFYEARQFSPADAAtartlslcgqdvpfgasLLFQIKDlplFRF 174
Cdd:cd07570   81 VGLPLRHDGKLYNAAAVLQNGKILGVVPKQLLPNYGVFDEKRYFTPGDKP-----------------DVLFFKG---LRI 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 175 HVEICEDVWVPIPPSSFAALAGATVLVNLSASNIVVGKSAYRHQLVGQQSARCVAAYLYTSAGEGesTTDLAWDGQGLIY 254
Cdd:cd07570  141 GVEICEDLWVPDPPSAELALAGADLILNLSASPFHLGKQDYRRELVSSRSARTGLPYVYVNQVGG--QDDLVFDGGSFIA 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 748803941 255 EN-GEMLAESERFAgeshVIFADVDLERLSRERMKQTTFGRSTARH 299
Cdd:cd07570  219 DNdGELLAEAPRFE----EDLADVDLDRLRSERRRNSSFLDEEAEI 260
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 343-641 7.13e-64

NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.


Pssm-ID: 467484 [Multi-domain]  Cd Length: 248  Bit Score: 212.03  E-value: 7.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 343 RCNEVYNIQVQALLQRLRSSGISKVVIGVSGGLDSTHALLVCAKAMDRlglprSNILAYTMPGFATSDRTLRQARELMQV 422
Cdd:cd00553    2 DPEEIIEALVCFLRDYLRKSGAKGFVLGLSGGIDSAVVAALAVRALGA-----ENVLALIMPSRYSSKETRDDAKALAEN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 423 IGCTAQEIDIRASCAQMLADIGHPHSEENTqyDITYENVQAGERTSHLFRLANLNNAIVIGTGDLSELALGWCTYGvGDH 502
Cdd:cd00553   77 LGIEYRTIDIDPIVDAFLKALEHAGGSEAE--DLALGNIQARLRMVLLYALANLLGGLVLGTGNKSELLLGYFTKY-GDG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 503 MSHYNVNASVPKTLITHLVRWVAesgeigdagsdVLENVLSTDISPELIPGkesgaleQKTESVIG-PYELQDFNLYYTV 581
Cdd:cd00553  154 AADINPIGDLYKTQVRELARYLG-----------VPEEIIEKPPSAELWPG-------QTDEDELGmPYEELDLILYGLV 215

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 582 RFGFAPskvaflahaawrdrdagdwpedpnvaRNQYGLADIRKNLRIFLDRFFRtSQFKR 641
Cdd:cd00553  216 DGKLGP--------------------------EEILSPGEDEEKVKRIFRLYRR-NEHKR 248
PRK13981 PRK13981
NAD synthetase; Provisional
 15-574 2.84e-63

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 219.64  E-value: 2.84e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  15 RVAVAIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDLFHQRALLDACEDALRSIVEASKeAKIAMI 94
Cdd:PRK13981   2 RIALAQLNPTVGDIAGNAAKILAAAAEAADAGADLLLFPELFLSGYPPEDLLLRPAFLAACEAALERLAAATA-GGPAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  95 VGLPVRAEHKLFNCAVVVADGAIRGVVPKSYLPNYGEFYEARQFSPADaatartlslcgqdvpfgASLLFQIKDLplfRF 174
Cdd:PRK13981  81 VGHPWREGGKLYNAAALLDGGEVLATYRKQDLPNYGVFDEKRYFAPGP-----------------EPGVVELKGV---RI 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 175 HVEICEDVWVPIPPSSFAAlAGATVLVNLSASNIVVGKSAYRHQLVgqqSARCVaaylytsagegESttdlawdGQGLIY 254
Cdd:PRK13981 141 GVPICEDIWNPEPAETLAE-AGAELLLVPNASPYHRGKPDLREAVL---RARVR-----------ET-------GLPLVY 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 255 EN--G---EMLaeserFAGESHVIFADVDLerlsRERMKQttFgrstarhADEVAkfsVVEFalsaptedalplERRVAR 329
Cdd:PRK13981 199 LNqvGgqdELV-----FDGASFVLNADGEL----AARLPA--F-------EEQIA---VVDF------------DRGEDG 245

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 330 FPYVPADRTRRDARCNEVYNIQVQALLQRLRSSGISKVVIGVSGGLDSThalLVCAKAMDRLGlpRSNILAYTMPGFATS 409
Cdd:PRK13981 246 WRPLPGPIAPPPEGEAEDYRALVLGLRDYVRKNGFPGVVLGLSGGIDSA---LVAAIAVDALG--AERVRAVMMPSRYTS 320

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 410 DRTLRQARELMQVIGCTAQEIDI---RASCAQMLADIghphsEENTQYDITYENVQAGERTSHLFRLANLNNAIVIGTGD 486
Cdd:PRK13981 321 EESLDDAAALAKNLGVRYDIIPIepaFEAFEAALAPL-----FAGTEPDITEENLQSRIRGTLLMALSNKFGSLVLTTGN 395

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 487 LSELALGWCT-YgvGDHMSHYNVNASVPKTLITHLVRWVAESGEigdaGSDVLENVLSTDISPELIPGkesgaleQKTES 565
Cdd:PRK13981 396 KSEMAVGYATlY--GDMAGGFAPIKDVYKTLVYRLCRWRNTVSP----GEVIPERIITKPPSAELRPN-------QTDQD 462


                 ....*....
gi 748803941 566 VIGPYELQD 574
Cdd:PRK13981 463 SLPPYDVLD 471
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
15-293 7.18e-58

Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 196.62  E-value: 7.18e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  15 RVAVAIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDLFHQRALLDACEDALRSIVEASKEAKIAMI 94
Cdd:COG0388    3 RIALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPALAALAELARELGIAVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  95 VGLPVRAEH-KLFNCAVVV-ADGAIRGVVPKSYLPNYGEFYEARQFSPADAatartlslcgqdvpfgasllFQIKDLPLF 172
Cdd:COG0388   83 VGLPERDEGgRLYNTALVIdPDGEILGRYRKIHLPNYGVFDEKRYFTPGDE--------------------LVVFDTDGG 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 173 RFHVEICEDVWVPiPPSSFAALAGATVLVNLSASNIVVGKsAYRHQLVGQQSARCVAAYLYtsAGEGESTTDLAWDGQGL 252
Cdd:COG0388  143 RIGVLICYDLWFP-ELARALALAGADLLLVPSASPFGRGK-DHWELLLRARAIENGCYVVA--ANQVGGEDGLVFDGGSM 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 748803941 253 IYE-NGEMLAESErfaGESHVIFADVDLERLSRERMKQTTFG 293
Cdd:COG0388  219 IVDpDGEVLAEAG---DEEGLLVADIDLDRLREARRRFPVLR 257
PLN02339 PLN02339
NAD+ synthase (glutamine-hydrolysing)
 31-378 1.46e-27

NAD+ synthase (glutamine-hydrolysing)


Pssm-ID: 177973 [Multi-domain]  Cd Length: 700  Bit Score: 118.63  E-value: 1.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  31 NAQETIKLAKQAaarGAVLVAFPELGLSAYTCDDLFHQRALLDACEDALRSIVEASKEAKIAMIVGLPVRAEHKLFNCAV 110
Cdd:PLN02339  24 RIKESIAEAKAA---GAVYRVGPELEITGYGCEDHFLELDTVTHSWECLAEILVGDLTDGILCDIGMPVIHGGVRYNCRV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 111 VVADGAIRGVVPKSYLPNYGEFYEARQFSP---ADAATARTLSLC-----GQ-DVPFG-ASLLFQIKDLPlfrfhVEICE 180
Cdd:PLN02339 101 FCLNRKILLIRPKMWLANDGNYRELRWFTAwkhKKKVEDFQLPEEiaeatSQkSVPFGdGYLQFLDTAVA-----AETCE 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 181 DVWVPIPPSSFAALAGATVLVNLSASNIVVGKSAYRHQLVGQQSARCVAAYLYtSAGEGESTTDLAWDGQGLIYENGEML 260
Cdd:PLN02339 176 ELFTPQAPHIDLALNGVEIISNGSGSHHQLRKLNTRLDLIRSATHKCGGVYLY-ANQRGCDGGRLYYDGCACIVVNGEVV 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 261 AESERFA-GESHVIFADVDLERLSRERMKQTTFgRSTARHADEVAKFSvVEFALSAPTEDALPLERRVARFPYVPADRTR 339
Cdd:PLN02339 255 AQGSQFSlQDVEVVTACVDLDAVVSFRGSISSF-REQASSKKRVPSVA-VPFKLCPPFSLSLVPSSPLKIRYHSPEEEIA 332

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 748803941 340 RDARCnevyniqvqALLQRLRSSGISKVVIGVSGGLDST 378
Cdd:PLN02339 333 LGPAC---------WLWDYLRRSGASGFLLPLSGGADSS 362
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 15-292 4.73e-26

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143610  Cd Length: 269  Bit Score: 108.14  E-value: 4.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  15 RVAVAIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDLFHQRALLDAcEDALRSIVEASKEakIAMI 94
Cdd:cd07586    1 RVAIAQIDPVLGDVEENLEKHLEIIETARERGADLVVFPELSLTGYNLGDLVYEVAMHAD-DPRLQALAEASGG--ICVV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  95 VGLPVRAEH-KLFNCAVVVADGAIRGVVPKSYLPNYGEFYEARQFSPADAATArtlslcgqdvpfgasllFQIKDLplfR 173
Cdd:cd07586   78 FGFVEEGRDgRFYNSAAYLEDGRVVHVHRKVYLPTYGLFEEGRYFAPGSHLRA-----------------FDTRFG---R 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 174 FHVEICEDVWVPIPPsSFAALAGATVLVNLSASNIVVGKSAYRHQLVGQQSARCVAAyLYT-------SAG-EGESTTdl 245
Cdd:cd07586  138 AGVLICEDAWHPSLP-YLLALDGADVIFIPANSPARGVGGDFDNEENWETLLKFYAM-MNGvyvvfanRVGvEDGVYF-- 213

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 748803941 246 aWDGQGLIYENGEMLAESERFagESHVIFADVDLERLSRERMKQTTF 292
Cdd:cd07586  214 -WGGSRVVDPDGEVVAEAPLF--EEDLLVAELDRSAIRRARFFSPTF 257
NAD_synthase pfam02540
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ...
 347-574 2.79e-19

NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.


Pssm-ID: 396888 [Multi-domain]  Cd Length: 241  Bit Score: 87.44  E-value: 2.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  347 VYNIQVQALLQRLRSSGISKVVIGVSGGLDSTHALLVCAKAmdrlgLPRSNILAYTMPGFATSDRTLRQARELMQVIGCT 426
Cdd:pfam02540   1 EINALVDFLRDYVQKAGFKGVVLGLSGGIDSSLVAYLAVKA-----LGKENVLALIMPSSQSSEEDVQDALALAENLGIE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  427 AQEIDIRASCAQMLADIGHphseenTQYDITYENVQAGERTSHLFRLANLNNAIVIGTGDLSELALGWCT-YgvGDHMSH 505
Cdd:pfam02540  76 YKTIDIKPIVRAFSQLFQD------ASEDFAKGNLKARIRMAILYYIANKFNYLVLGTGNKSELAVGYFTkY--GDGACD 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  506 YNVNASVPKTLITHLVRWVAesgeigdagsdVLENVLSTDISPELIPGkesgaleQKTESVIG-PYELQD 574
Cdd:pfam02540 148 IAPIGDLYKTQVYELARYLN-----------VPERIIKKPPSADLWPG-------QTDEEELGiPYDELD 199
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 15-282 3.33e-19

Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. The family includes: Nitrilase EC:3.5.5.1, Aliphatic amidase EC:3.5.1.4, Biotidinase EC:3.5.1.12, Beta-ureidopropionase EC:3.5.1.6. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins.


Pssm-ID: 425873 [Multi-domain]  Cd Length: 257  Bit Score: 87.80  E-value: 3.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941   15 RVAVAIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDLFHQRALLDACEdALRSIVEASKEAKIAMI 94
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAHFLEAAEVGDGE-TLAGLAALARKNGIAIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941   95 VGLPVRAEH--KLFNCAVVV-ADGAIRGVVPKSYL---PNYGEFYEARQFSPADAATartlslcgqdvpfgasllfqIKD 168
Cdd:pfam00795  80 IGLIERWLTggRLYNTAVLLdPDGKLVGKYRKLHLfpePRPPGFRERVLFEPGDGGT--------------------VFD 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  169 LPLFRFHVEICEDVWVPIpPSSFAALAGATVLVNLSASNIVVGK-SAYRHQLVGQQSARCVAAYLYTSAGEGESTTDLAW 247
Cdd:pfam00795 140 TPLGKIGAAICYEIRFPE-LLRALALKGAEILINPSARAPFPGSlGPPQWLLLARARALENGCFVIAANQVGGEEDAPWP 218

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 748803941  248 DGQGLIY-ENGEMLAESERFAGEshVIFADVDLERL 282
Cdd:pfam00795 219 YGHSMIIdPDGRILAGAGEWEEG--VLIADIDLALV 252
PRK13980 PRK13980
NAD synthetase; Provisional
 336-498 7.28e-18

NAD synthetase; Provisional


Pssm-ID: 184435 [Multi-domain]  Cd Length: 265  Bit Score: 84.11  E-value: 7.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 336 DRTRRDARCNEVYNIQVQALLQRLRSSGISKVVIGVSGGLDSTHALLVCAKAmdrlgLPRSNILAYTMPGFATSDRTLRQ 415
Cdd:PRK13980   2 DLRVLALDYEKVREIIVDFIREEVEKAGAKGVVLGLSGGIDSAVVAYLAVKA-----LGKENVLALLMPSSVSPPEDLED 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 416 ARELMQVIGCTAQEIDIrascaqmlADIGHPHSEENTQYDITYE-NVQAGERTSHLFRLANLNNAIVIGTGDLSELALGW 494
Cdd:PRK13980  77 AELVAEDLGIEYKVIEI--------TPIVDAFFSAIPDADRLRVgNIMARTRMVLLYDYANRENRLVLGTGNKSELLLGY 148


                 ....*
gi 748803941 495 CT-YG 498
Cdd:PRK13980 149 FTkYG 153
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
 15-143 9.51e-15

Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); Pseudomonas sp. MCI3434 R-amidase hydrolyzes (R,S)-piperazine-2-tert-butylcarboxamide to form (R)-piperazine-2-carboxylic acid. It does so with strict R-stereoselectively. Its preferred substrates are carboxamide compounds which have the amino or imino group connected to their beta- or gamma-carbon. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group. It has been suggested that this subgroup represents a new class. Members of the nitrilase superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Native R-amidase however appears to be a monomer.


Pssm-ID: 143600  Cd Length: 254  Bit Score: 74.54  E-value: 9.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  15 RVAVAIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDLFHQRALLDAcEDALRSIVEASKEAKIAMI 94
Cdd:cd07576    1 RLALYQGPARDGDVAANLARLDEAAARAAAAGADLLVFPELFLTGYNIGDAVARLAEPAD-GPALQALRAIARRHGIAIV 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 748803941  95 VGLPVRAEHKLFNCAVVV-ADGAIRGVVPKSYLpnYGEfYEARQFSPADA 143
Cdd:cd07576   80 VGYPERAGGAVYNAAVLIdEDGTVLANYRKTHL--FGD-SERAAFTPGDR 126
nadE TIGR00552
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ...
 355-500 1.22e-14

NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273132 [Multi-domain]  Cd Length: 250  Bit Score: 74.35  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  355 LLQRLRSSGISKVVIGVSGGLDSTHALLVCAKAmdrlgLPRSNILAYTMPGFATSDRTLRQARELMQVIGCTAQEIDIR- 433
Cdd:TIGR00552  13 LRGYVQKSGAKGVVLGLSGGIDSAVVAALCVEA-----LGEQNHALLLPHSVQTPEQDVQDALALAEPLGINYKNIDIAp 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 748803941  434 -ASCAQMLADIGHPHSEEntqydITYENVQAGERTSHLFRLANLNNAIVIGTGDLSELALGWCT-YGVG 500
Cdd:TIGR00552  88 iAASFQAQTETGDELSDF-----LAKGNLKARLRMAALYAIANKHNLLVLGTGNKSELMLGYFTkYGDG 151
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 15-286 2.59e-14

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143604  Cd Length: 268  Bit Score: 73.53  E-value: 2.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  15 RVAVAIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDLFHQRALLDACEDAL--RSIVEASKEAKIA 92
Cdd:cd07580    1 RVACVQFDPRVGDLDANLARSIELIREAADAGANLVVLPELANTGYVFESRDEAFALAEEVPDGAstRAWAELAAELGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  93 MIVGLPVRAEHKLFNCAVVVADGAIRGVVPKSYLPNygefYEARQFSPADAAtartlslcgqdvpfgasllFQIKDLPLF 172
Cdd:cd07580   81 IVAGFAERDGDRLYNSAVLVGPDGVIGTYRKAHLWN----EEKLLFEPGDLG-------------------LPVFDTPFG 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 173 RFHVEICEDVWVPIPPSSfAALAGATVLVnlsasnIVVGKSAYRHQLVGQqsaRCVAAYLYTSAGegeSTTDLA------ 246
Cdd:cd07580  138 RIGVAICYDGWFPETFRL-LALQGADIVC------VPTNWVPMPRPPEGG---PPMANILAMAAA---HSNGLFiacadr 204

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 748803941 247 --------WDGQGLIYE-NGEMLAESERfAGESHVIFADVDLERLSRER 286
Cdd:cd07580  205 vgtergqpFIGQSLIVGpDGWPLAGPAS-GDEEEILLADIDLTAARRKR 252
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 15-295 8.51e-13

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143609  Cd Length: 261  Bit Score: 68.88  E-value: 8.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  15 RVAVAIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDLFHQRALLDACEdALRSIVEASKEAKIAMI 94
Cdd:cd07585    1 RIALVQFEARVGDKARNLAVIARWTRKAAAQGAELVCFPEMCITGYTHVRALSREAEVPDGP-STQALSDLARRYGLTIL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  95 VGLPVRAEHKLFNCAVVVADGAIRGVVPKSYLPNygefYEARQFSPADAatartlslcgqdvpfgasllFQIKDLPLFRF 174
Cdd:cd07585   80 AGLIEKAGDRPYNTYLVCLPDGLVHRYRKLHLFR----REHPYIAAGDE--------------------YPVFATPGVRF 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 175 HVEICEDVWVPiPPSSFAALAGATVLVNLSASNIVVGKSAyRHQLVGQQSARCVAAYLYTSAgegestTDLAWDGQGLIY 254
Cdd:cd07585  136 GILICYDNHFP-ENVRATALLGAEILFAPHATPGTTSPKG-REWWMRWLPARAYDNGVFVAA------CNGVGRDGGEVF 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 748803941 255 ENGEML------AESERFAGESHVIFADVDLERL--SRERmKQTTFGRS 295
Cdd:cd07585  208 PGGAMIldpygrVLAETTSGGDGMVVADLDLDLIntVRGR-RWISFLRA 255
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 15-288 5.46e-12

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143608  Cd Length: 258  Bit Score: 66.62  E-value: 5.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  15 RVAVAIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDL-FHQRALLDAC-EDALRSIVEASKEAKIA 92
Cdd:cd07584    1 KVALIQMDSVLGDVKANLKKAAELCKEAAAEGADLICFPELATTGYRPDLLgPKLWELSEPIdGPTVRLFSELAKELGVY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  93 MIVGLPVRAE--HKLFNCAVVVA-DGAIRGVVPKSYLpnYGEfyEARQFSPadaatartlslcGQDVPfgasllfqIKDL 169
Cdd:cd07584   81 IVCGFVEKGGvpGKVYNSAVVIDpEGESLGVYRKIHL--WGL--EKQYFRE------------GEQYP--------VFDT 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 170 PLFRFHVEICEDVWVPIPPSSFaALAGATVLVNLSASNIvvgKSAYRHQLvgQQSARCVAAYLYTSA-----GEGESTTd 244
Cdd:cd07584  137 PFGKIGVMICYDMGFPEVARIL-TLKGAEVIFCPSAWRE---QDADIWDI--NLPARALENTVFVAAvnrvgNEGDLVL- 209

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 748803941 245 laWDGQGLIYENGEMLAESERFAGEshVIFADVDLERLSRERMK 288
Cdd:cd07584  210 --FGKSKILNPRGQVLAEASEEAEE--ILYAEIDLDAIADYRMT 249
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
 26-286 1.45e-11

N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known as N-carbamoylputrescine amidase and carbamoylputrescine hydrolase) converts N-carbamoylputrescine to putrescine, a step in polyamine biosynthesis in plants and bacteria. This subgroup includes Arabidopsis thaliana CPA, also known as nitrilase-like 1 (NLP1), and Pseudomonas aeruginosa AguB. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 11. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer; P. aeruginosa AugB is a homohexamer, Arabidopsis thaliana NLP1 is a homooctomer.


Pssm-ID: 143597  Cd Length: 284  Bit Score: 65.66  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  26 ADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCD----DLFhQRALLDACEDALRSIVEASKEAKIAMIVGL-PVR 100
Cdd:cd07573   12 EDPEANLAKAEELVREAAAQGAQIVCLQELFETPYFCQeedeDYF-DLAEPPIPGPTTARFQALAKELGVVIPVSLfEKR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 101 AEHKLFNCAVVV-ADGAIRGVVPKSYLPNYGEFYEARQFSPADAAtartlslcgqdvpfgasllFQIKDLPLFRFHVEIC 179
Cdd:cd07573   91 GNGLYYNSAVVIdADGSLLGVYRKMHIPDDPGYYEKFYFTPGDTG-------------------FKVFDTRYGRIGVLIC 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 180 EDVWVPiPPSSFAALAGATVLVNLSA-----SNIVVGKSAYRH-QLVGQQSArcVAAYLYTSA-----GEGESTTDLAWD 248
Cdd:cd07573  152 WDQWFP-EAARLMALQGAEILFYPTAigsepQEPPEGLDQRDAwQRVQRGHA--IANGVPVAAvnrvgVEGDPGSGITFY 228

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 748803941 249 GQGLIY-ENGEMLAESERFAGEshVIFADVDLERLSRER 286
Cdd:cd07573  229 GSSFIAdPFGEILAQASRDEEE--ILVAEFDLDEIEEVR 265
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
 15-286 2.44e-10

Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup of the nitrilase superfamily. This superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. Pyrococcus horikoshii Ph0642 is a hypothetical protein belonging to this subgroup. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). This subgroup was classified as belonging to class 13, which represents proteins that at the time were difficult to place in a distinct similarity group. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143601  Cd Length: 259  Bit Score: 61.55  E-value: 2.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  15 RVAVAIPNCKVADPAFNAQETIKLAKQAAARgavLVAFPELGLSAYtcddLF--HQRALLDACED----ALRSIVEASKE 88
Cdd:cd07577    1 KVGYVQFNPKFGEVEKNLKKVESLIKGVEAD---LIVLPELFNTGY----AFtsKEEVASLAESIpdgpTTRFLQELARE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  89 AKIAMIVGLPVRAEHKLFNCAVVVADGAIRGVVPKSYLpnygeFYEARQ-FSPADaatartlslcgqdvpfgasLLFQIK 167
Cdd:cd07577   74 TGAYIVAGLPERDGDKFYNSAVVVGPEGYIGIYRKTHL-----FYEEKLfFEPGD-------------------TGFRVF 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 168 DLPLFRFHVEICEDvWVpIPPSSFA-ALAGATVLVNlsASNIVVGksayrhqlVGQQS--ARCVAAYLYTSA----GE-- 238
Cdd:cd07577  130 DIGDIRIGVMICFD-WY-FPEAARTlALKGADIIAH--PANLVLP--------YCPKAmpIRALENRVFTITanriGTee 197

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 748803941 239 -GESTtdLAWDGQGLIYE-NGEMLAEserfAGES--HVIFADVDLeRLSRER 286
Cdd:cd07577  198 rGGET--LRFIGKSQITSpKGEVLAR----APEDgeEVLVAEIDP-RLARDK 242
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 26-205 6.17e-08

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143605  Cd Length: 255  Bit Score: 54.12  E-value: 6.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  26 ADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDLFHQRALLDACEDALRSIVEASKEAKIAMIVGLPVRAE-HK 104
Cdd:cd07581   10 GDKEENLEKVRRLLAEAAAAGADLVVFPEYTMARFGDGLDDYARVAEPLDGPFVSALARLARELGITVVAGMFEPAGdGR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 105 LFNCAVVV-ADGAIRGVVPKSYLPN-YGeFYEARQFSPADAATARTLSLCGqdvpfgasllfqikdlplFRFHVEICEDV 182
Cdd:cd07581   90 VYNTLVVVgPDGEIIAVYRKIHLYDaFG-FRESDTVAPGDELPPVVFVVGG------------------VKVGLATCYDL 150

                        170       180
                 ....*....|....*....|...
gi 748803941 183 WVPIPPSSFaALAGATVLVNLSA 205
Cdd:cd07581  151 RFPELARAL-ALAGADVIVVPAA 172
PLN02747 PLN02747
N-carbamolyputrescine amidase
 26-205 7.46e-08

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 54.39  E-value: 7.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  26 ADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYTCDDlfhQRALLDACEDALRSIVEASKEAKIAMIVG--LPV---- 99
Cdd:PLN02747  18 DDRAANVDKAERLVREAHAKGANIILIQELFEGYYFCQA---QREDFFQRAKPYEGHPTIARMQKLAKELGvvIPVsffe 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 100 RAEHKLFN-CAVVVADGAIRGVVPKSYLPNYGEFYEARQFSPADAAtartlslcgqdvpfgasllFQIKDLPLFRFHVEI 178
Cdd:PLN02747  95 EANNAHYNsIAIIDADGTDLGLYRKSHIPDGPGYQEKFYFNPGDTG-------------------FKVFDTKFAKIGVAI 155

                        170       180
                 ....*....|....*....|....*..
gi 748803941 179 CEDVWVPIPPSSFaALAGATVLVNLSA 205
Cdd:PLN02747 156 CWDQWFPEAARAM-VLQGAEVLLYPTA 181
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
 36-299 1.65e-07

N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses N-carbamyl-D-amino acids to produce D-amino acids. It is an important biocatalyst in the pharmaceutical industry, producing useful D-amino acids for example in the preparation of beta-lactam antibiotics. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 6. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Agrobacterium radiobacter DCase forms a tetramer (dimer of dimers). Some DCases may form trimers.


Pssm-ID: 143593  Cd Length: 302  Bit Score: 53.47  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  36 IKLAKQAAARGAVLVAFPELGLSAYTCDDLFHQRALLDAC------EDALRSIVEASKEAKIAMIVGLPVRAEH----KL 105
Cdd:cd07569   28 IALLEEAASRGAQLVVFPELALTTFFPRWYFPDEAELDSFfetempNPETQPLFDRAKELGIGFYLGYAELTEDggvkRR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 106 FNCAVVV-ADGAIRGVVPKSYLPNYGEFY--------EARQFSPADaatartlslcgqdvpfgasLLFQIKDLPLFRFHV 176
Cdd:cd07569  108 FNTSILVdKSGKIVGKYRKVHLPGHKEPEpyrpfqhlEKRYFEPGD-------------------LGFPVFRVPGGIMGM 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 177 EICED-VWvpipPSSF--AALAGATVLV---NLSASNIVVGK----SAYRHQLVGQQSARCVAAYLYTSAGEGESttdla 246
Cdd:cd07569  169 CICNDrRW----PETWrvMGLQGVELVLlgyNTPTHNPPAPEhdhlRLFHNLLSMQAGAYQNGTWVVAAAKAGME----- 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 748803941 247 wDGQGLI------YENGEMLAESERFAGEshVIFADVDLERlsRERMKQTTFgrSTARH 299
Cdd:cd07569  240 -DGCDLIggscivAPTGEIVAQATTLEDE--VIVADCDLDL--CREGRETVF--NFARH 291
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
 15-212 2.77e-07

Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); This subgroup includes mammalian Nit1 and Nit2, the Nit1-like domain of the invertebrate NitFhit, and various uncharacterized bacterial and archaeal Nit-like proteins. Nit1 and Nit2 are candidate tumor suppressor proteins. In NitFhit, the Nit1-like domain is encoded as a fusion protein with the non-homologous tumor suppressor, fragile histidine triad (Fhit). Mammalian Nit1 and Fhit may affect distinct signal pathways, and both may participate in DNA damage-induced apoptosis. Nit1 is a negative regulator in T cells. Overexpression of Nit2 in HeLa cells leads to a suppression of cell growth through cell cycle arrest in G2. These Nit proteins and the Nit1-like domain of NitFhit belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 10.


Pssm-ID: 143596  Cd Length: 265  Bit Score: 52.43  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  15 RVAVaIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPElgLSAYTCDDLFHQRALLDACED--ALRSIVEASKEAKIA 92
Cdd:cd07572    1 RVAL-IQMTSTADKEANLARAKELIEEAAAQGAKLVVLPE--CFNYPGGTDAFKLALAEEEGDgpTLQALSELAKEHGIW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  93 MIVG-LPVRAEH--KLFNCAVVV-ADGAIRGVVPKSYL-----PNYGEFYEARQFSPADAAtartlslcgqdVPFgasll 163
Cdd:cd07572   78 LVGGsIPERDDDdgKVYNTSLVFdPDGELVARYRKIHLfdvdvPGGISYRESDTLTPGDEV-----------VVV----- 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 748803941 164 fqikDLPLFRFHVEICEDVwvpippsSFAALA------GATVLVNLSASNIVVGK 212
Cdd:cd07572  142 ----DTPFGKIGLGICYDL-------RFPELAralarqGADILTVPAAFTMTTGP 185
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
 15-117 1.35e-06

Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases (nitrile aminohydrolases, EC:3.5.5.1) hydrolyze nitriles (RCN) to ammonia and the corresponding carboxylic acid. Most nitrilases prefer aromatic nitriles, some prefer arylacetonitriles and others aliphatic nitriles. This group includes the nitrilase cyanide dihydratase (CDH), which hydrolyzes inorganic cyanide (HCN) to produce formate. It also includes cyanide hydratase (CH), which hydrolyzes HCN to formamide. This group includes four Arabidopsis thaliana nitrilases (Ath)NIT1-4. AthNIT1-3 have a strong substrate preference for phenylpropionitrile (PPN) and other nitriles which may originate from the breakdown of glucosinolates. The product of PPN hydrolysis, phenylacetic acid has auxin activity. AthNIT1-3 can also convert indoacetonitrile to indole-3-acetic acid (IAA, auxin), but with a lower affinity and velocity. From their expression patterns, it has been speculated that NIT3 may produce IAA during the early stages of germination, and that NIT3 may produce IAA during embryo development and maturation. AthNIT4 has a strong substrate specificity for the nitrile, beta-cyano-L-alanine (Ala(CN)), an intermediate of cyanide detoxification. AthNIT4 has both a nitrilase activity and a nitrile hydratase (NHase) activity, which generate aspartic acid and asparagine respectively from Ala(CN). NHase catalyzes the hydration of nitriles to their corresponding amides. This subgroup belongs to a larger nitrilase superfamily comprised of belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 1.


Pssm-ID: 143588  Cd Length: 297  Bit Score: 50.56  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  15 RVAVaipnCKVADPAFNAQETI----KLAKQAAARGAVLVAFPELGLSAY----TCDDLFHQRAL--------LDACEDA 78
Cdd:cd07564    2 KVAA----VQAAPVFLDLAATVekacRLIEEAAANGAQLVVFPEAFIPGYpywiWFGAPAEGRELfaryyensVEVDGPE 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 748803941  79 LRSIVEASKEAKIAMIVGLPVRAEHKLFNCAVVV-ADGAI 117
Cdd:cd07564   78 LERLAEAARENGIYVVLGVSERDGGTLYNTQLLIdPDGEL 117
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
 33-286 1.00e-04

mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This family includes mammalian-like beta-AS (EC 3.5.1.6, also known as beta-ureidopropionase or N-carbamoyl-beta-alanine amidohydrolase). This enzyme catalyzes the third and final step in the catabolic pyrimidine catabolic pathway responsible for the degradation of uracil and thymine, the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate to the beta-amino acids, beta-alanine and beta-aminoisobutyrate respectively. This family belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 5. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Beta-ASs from this subgroup are found in various oligomeric states, dimer (human), hexamer (calf liver), decamer (Arabidopsis and Zea mays), and in the case of Drosophila melanogaster beta-AS, as a homooctamer assembled as a left-handed helical turn, with the possibility of higher order oligomers formed by adding dimers at either end. Rat beta-AS changes its oligomeric state (hexamer, trimer, dodecamer) in response to allosteric effectors. Eukaryotic Saccharomyces kluyveri beta-AS belongs to a different superfamily.


Pssm-ID: 143592  Cd Length: 287  Bit Score: 44.79  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  33 QETIKLAKQAAARGAVLVAFPELGLSAYTCDDlfHQRALLDACEDA-----LRSIVEASKEAKIAMIVglPVRAEHK--- 104
Cdd:cd07568   30 QKHVTMIREAAEAGAQIVCLQEIFYGPYFCAE--QDTKWYEFAEEIpngptTKRFAALAKEYNMVLIL--PIYEKEQggt 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 105 LFNCAVVV-ADGAIRGVVPKSYLPNYGEFYEARQFSPADaatartlslcgqdvpfgasLLFQIKDLPLFRFHVEICEDVW 183
Cdd:cd07568  106 LYNTAAVIdADGTYLGKYRKNHIPHVGGFWEKFYFRPGN-------------------LGYPVFDTAFGKIGVYICYDRH 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 184 VPIPPSSFaALAGATVLVNLSASniVVGKSAYRHQLvgQQSARCVAAYLYTSA----GEGESTTDLAWDGQG-LIYENGE 258
Cdd:cd07568  167 FPEGWRAL-GLNGAEIVFNPSAT--VAGLSEYLWKL--EQPAAAVANGYFVGAinrvGTEAPWNIGEFYGSSyFVDPRGQ 241

                        250       260
                 ....*....|....*....|....*...
gi 748803941 259 MLAESERfaGESHVIFADVDLERLSRER 286
Cdd:cd07568  242 FVASASR--DKDELLVAELDLDLIREVR 267
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 15-119 1.27e-04

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143607  Cd Length: 253  Bit Score: 44.07  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941  15 RVAVAIPNCKVADPAFNAQETIKLAKQAAARGAVLVAFPELGLSAYtcdDLFHQRALLDACEDALRSIV-EASKEAKIAM 93
Cdd:cd07583    1 KIALIQLDIVWGDPEANIERVESLIEEAAAAGADLIVLPEMWNTGY---FLDDLYELADEDGGETVSFLsELAKKHGVNI 77

                         90       100
                 ....*....|....*....|....*...
gi 748803941  94 IVG-LPVRAEHKLFNCAVVVA-DGAIRG 119
Cdd:cd07583   78 VAGsVAEKEGGKLYNTAYVIDpDGELIA 105
PTZ00323 PTZ00323
NAD+ synthase; Provisional
 351-489 4.55e-04

NAD+ synthase; Provisional


Pssm-ID: 185554 [Multi-domain]  Cd Length: 294  Bit Score: 42.84  E-value: 4.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 351 QVQALLQRLRSSGISKVVIGVSGGLDSTHALLVCAKAMDRLGLPRSNILAYTMPgFATSDRTLRQARELMQVIGCTAQEI 430
Cdd:PTZ00323  33 KCAKLNEYMRRCGLKGCVTSVSGGIDSAVVLALCARAMRMPNSPIQKNVGLCQP-IHSSAWALNRGRENIQACGATEVTV 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 748803941 431 DIRASCAQMladighpHSEENTQYDITYENVQAGE-----RTSHLFRLANL-----NNAIVIGTGDLSE 489
Cdd:PTZ00323 112 DQTEIHTQL-------SSLVEKAVGIKGGAFARGQlrsymRTPVAFYVAQLlsqegTPAVVMGTGNFDE 173
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
353-433 9.01e-04

ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 41.63  E-value: 9.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748803941 353 QALLQRLRSSGisKVVIGVSGGLDSThalLVCAKAMDRLGlprSNILAYTMPGFATSDRTLRQARELmqvigctAQEIDI 432
Cdd:COG1606    6 ERLKAILKELG--SVLVAFSGGVDST---LLAKVAHDVLG---DRVLAVTADSPSLPERELEEAKEL-------AKEIGI 70


                 .
gi 748803941 433 R 433
Cdd:COG1606   71 R 71
nadE PRK00768
ammonia-dependent NAD(+) synthetase;
352-391 1.00e-02

ammonia-dependent NAD(+) synthetase;


Pssm-ID: 234831 [Multi-domain]  Cd Length: 268  Bit Score: 38.58  E-value: 1.00e-02
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 748803941 352 VQALLQRLRSSGISKVVIGVSGGLDSTHALLVCAKAMDRL 391
Cdd:PRK00768  26 VDFLKDYLKKSGLKSLVLGISGGQDSTLAGRLAQLAVEEL 65
 
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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