|
Name |
Accession |
Description |
Interval |
E-value |
| AdoHcyase |
pfam05221 |
S-adenosyl-L-homocysteine hydrolase; |
10-459 |
0e+00 |
|
S-adenosyl-L-homocysteine hydrolase;
Pssm-ID: 461594 Cd Length: 429 Bit Score: 793.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 10 DYKVADISLADYGRKEIKLAEAEMPALIGLRKRYAASKPLAGAKILGCIHMTIQTAVLIETLVELGAEVRWTSCNIFSTQ 89
Cdd:pfam05221 1 DYKVADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 90 DHAAAAIAARGIPVFAWKGETEEEYVWCLEQQINVNGQPWDANMILDDGGDLTALVHEKYPALLERIHGITEETTTGVQR 169
Cdd:pfam05221 81 DHAAAAIAAAGVPVFAWKGETLEEYWWCTEQALTWPPDGGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 170 LIEMWKDGSLKVPAINVNDSVTKSKNDNKYGCRHSLNDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIVRVTE 249
Cdd:pfam05221 161 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 250 VDPICAMQACMDGYEVVSPYkngvqtgkkedinhDLLGNTDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTEIDTA 329
Cdd:pfam05221 241 IDPICALQAAMEGYEVVTME--------------DVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNIGHFDNEIDEI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 330 YL---RGYKWVEVKPQVHQVYRSEDenNYLILLSEGRLVNLGNATGHPSRVMDGSFANQVLGQIHLFQekfadlpaNEKA 406
Cdd:pfam05221 307 VLallKGVKWVNIKPQVDDITFPDG--KSIIVLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELWT--------NDKE 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 507075160 407 AKIRVEVLPKKLDEEVAAAMVAGFGGVLTQLTQEQADYLGVAVEGPFKSDAYK 459
Cdd:pfam05221 377 YENGVYVLPKKLDEKVARLHLEKLGAKLTELTKEQADYIGVPVEGPFKPDHYR 429
|
|
| AdoHcyase |
smart00996 |
S-adenosyl-L-homocysteine hydrolase; |
12-459 |
0e+00 |
|
S-adenosyl-L-homocysteine hydrolase;
Pssm-ID: 214963 [Multi-domain] Cd Length: 426 Bit Score: 785.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 12 KVADISLADYGRKEIKLAEAEMPALIGLRKRYAASKPLAGAKILGCIHMTIQTAVLIETLVELGAEVRWTSCNIFSTQDH 91
Cdd:smart00996 1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 92 AAAAIAARGIPVFAWKGETEEEYVWCLEQQINVNGqPWDANMILDDGGDLTALVHEKYPALLERIHGITEETTTGVQRLI 171
Cdd:smart00996 81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPD-GWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 172 EMWKDGSLKVPAINVNDSVTKSKNDNKYGCRHSLNDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIVRVTEVD 251
Cdd:smart00996 160 QMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 252 PICAMQACMDGYEVVSPykngvqtgkkedinHDLLGNTDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTEIDTAYL 331
Cdd:smart00996 240 PICALQAAMDGFEVVTM--------------EEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 332 RGY---KWVEVKPQVHQVYRSedENNYLILLSEGRLVNLGNATGHPSRVMDGSFANQVLGQIHLFQekfadlpaNEKAAK 408
Cdd:smart00996 306 RNNpglKWENIKPQVDHITFP--DGKRIILLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELFT--------KPGKYK 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 507075160 409 IRVEVLPKKLDEEVAAAMVAGFGGVLTQLTQEQADYLGVAVEGPFKSDAYK 459
Cdd:smart00996 376 NGVYVLPKKLDEKVARLHLEKLGAKLTKLTKEQADYIGVPVEGPFKPDHYR 426
|
|
| PRK05476 |
PRK05476 |
S-adenosyl-L-homocysteine hydrolase; Provisional |
6-454 |
0e+00 |
|
S-adenosyl-L-homocysteine hydrolase; Provisional
Pssm-ID: 235488 [Multi-domain] Cd Length: 425 Bit Score: 715.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 6 ASFTDYKVADISLADYGRKEIKLAEAEMPALIGLRKRYAASKPLAGAKILGCIHMTIQTAVLIETLVELGAEVRWTSCNI 85
Cdd:PRK05476 3 ATGTDYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 86 FSTQDHAAAAIAARGIPVFAWKGETEEEYVWCLEQQInvngQPWDANMILDDGGDLTALVHEKYPALLERIHGITEETTT 165
Cdd:PRK05476 83 FSTQDDVAAALAAAGIPVFAWKGETLEEYWECIERAL----DGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 166 GVQRLIEMWKDGSLKVPAINVNDSVTKSKNDNKYGCRHSLNDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIV 245
Cdd:PRK05476 159 GVHRLYAMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 246 RVTEVDPICAMQACMDGYEVVSpykngvqtgkkediNHDLLGNTDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTE 325
Cdd:PRK05476 239 IVTEVDPICALQAAMDGFRVMT--------------MEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 326 IDTAYLRGY--KWVEVKPQVHQVYRseDENNYLILLSEGRLVNLGNATGHPSRVMDGSFANQVLGQIHLFQekfadlpaN 403
Cdd:PRK05476 305 IDVAALEELavKWREIKPQVDEYTL--PDGKRIILLAEGRLVNLGAATGHPSEVMDMSFANQALAQIELFT--------N 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 507075160 404 EKAAKIRVEVLPKKLDEEVAAAMVAGFGGVLTQLTQEQADYLGVAVEGPFK 454
Cdd:PRK05476 375 RGKLEPGVYVLPKELDEEVARLKLKALGVKLDELTEEQAEYIGVWVEGPFK 425
|
|
| SAM1 |
COG0499 |
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism]; |
6-452 |
0e+00 |
|
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
Pssm-ID: 440265 [Multi-domain] Cd Length: 420 Bit Score: 715.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 6 ASFTDYKVADISLADYGRKEIKLAEAEMPALIGLRKRYAASKPLAGAKILGCIHMTIQTAVLIETLVELGAEVRWTSCNI 85
Cdd:COG0499 1 TAPMDYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 86 FSTQDHAAAAIAARGIPVFAWKGETEEEYVWCLEQQINvngqpWDANMILDDGGDLTALVHEKYPALLERIHGITEETTT 165
Cdd:COG0499 81 LSTQDDVAAALAAAGIPVFAWKGETLEEYYWCIEQALD-----HGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 166 GVQRLIEMWKDGSLKVPAINVNDSVTKSKNDNKYGCRHSLNDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIV 245
Cdd:COG0499 156 GVHRLRAMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 246 RVTEVDPICAMQACMDGYEVVSPykngvqtgkkedinHDLLGNTDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTE 325
Cdd:COG0499 236 IVTEVDPICALEAAMDGFRVMPM--------------EEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 326 IDTAYLRGY--KWVEVKPQVHQvYRSEDeNNYLILLSEGRLVNLGNATGHPSRVMDGSFANQVLGQIHLFQekfadlpaN 403
Cdd:COG0499 302 IDVAALEKLavEKREIRPQVDE-YTLPD-GRRIYLLAEGRLVNLAAATGHPSEVMDMSFANQALAQIYLVK--------N 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 507075160 404 EKAAKIRVEVLPKKLDEEVAAAMVAGFGGVLTQLTQEQADYLGVAVEGP 452
Cdd:COG0499 372 GDKLEPGVYVLPKELDEEVARLKLEALGVKIDTLTEEQAEYLGSWVEGP 420
|
|
| SAHH |
cd00401 |
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ... |
20-447 |
0e+00 |
|
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.
Pssm-ID: 240619 [Multi-domain] Cd Length: 402 Bit Score: 646.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 20 DYGRKEIKLAEAEMPALIGLRKRYAASKPLAGAKILGCIHMTIQTAVLIETLVELGAEVRWTSCNIFSTQDHAAAAIAAR 99
Cdd:cd00401 1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 100 GIPVFAWKGETEEEYVWCLEQQINvngqpWDANMILDDGGDLTALVHEKYPALLERIHGITEETTTGVQRLIEMWKDGSL 179
Cdd:cd00401 81 GIPVFAWKGETEEEYWWCIEQALD-----HGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 180 KVPAINVNDSVTKSKNDNKYGCRHSLNDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIVRVTEVDPICAMQAC 259
Cdd:cd00401 156 LFPAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 260 MDGYEVVsPYKNGVQTGkkedinhdllgntDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTEIDTAYLR--GYKWV 337
Cdd:cd00401 236 MDGFEVM-PMEEAAKIG-------------DIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEelAVEKR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 338 EVKPQVHQvYRSEDeNNYLILLSEGRLVNLGNATGHPSRVMDGSFANQVLGQIHLFQEKfadlpaneKAAKIRVEVLPKK 417
Cdd:cd00401 302 EIRPQVDE-YTLPD-GRRIILLAEGRLVNLACATGHPSFVMDMSFANQALAQIELWKNR--------DKLEPGVYVLPKE 371
|
410 420 430
....*....|....*....|....*....|
gi 507075160 418 LDEEVAAAMVAGFGGVLTQLTQEQADYLGV 447
Cdd:cd00401 372 LDEEVARLKLEALGIKLDKLTEEQAEYLGS 401
|
|
| ahcY |
TIGR00936 |
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ... |
20-452 |
1.03e-180 |
|
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the regeneration of the methyl donor S-adenosylmethionine. Species that lack this enzyme are likely to have adenosylhomocysteine nucleosidase (EC 3.2.2.9), an enzyme which also acts as 5'-methyladenosine nucleosidase (see TIGR01704). [Energy metabolism, Amino acids and amines]
Pssm-ID: 213572 Cd Length: 407 Bit Score: 510.79 E-value: 1.03e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 20 DYGRKEIKLAEAEMPALIGLRKRYAASKPLAGAKILGCIHMTIQTAVLIETLVELGAEVRWTSCNIFSTQDHAAAA-IAA 98
Cdd:TIGR00936 1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAAlAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 99 RGIPVFAWKGETEEEYVWCLEQQINVngqpwDANMILDDGGDLTALVHEKYPALLERIHGITEETTTGVQRLIEMWKDGS 178
Cdd:TIGR00936 81 AGIPVFAWRGETNEEYYWAIEQVLDH-----EPNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 179 LKVPAINVNDSVTKSKNDNKYGCRHSLNDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIVRVTEVDPICAMQA 258
Cdd:TIGR00936 156 LKFPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 259 CMDGYEVVspykngvqtgKKEDINHDllgnTDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTEIDTAYLR--GYKW 336
Cdd:TIGR00936 236 AMDGFRVM----------TMEEAAKI----GDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEelAVEK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 337 VEVKPQVHQvYRSEDENNyLILLSEGRLVNLGNATGHPSRVMDGSFANQVLGQIHLFQEkfadlpaNEKAAKiRVEVLPK 416
Cdd:TIGR00936 302 VNVRPQVDE-YILKDGRR-IYLLAEGRLVNLAAAEGHPSEVMDMSFANQALAAEYLWKN-------HDKLEP-GVYRLPK 371
|
410 420 430
....*....|....*....|....*....|....*.
gi 507075160 417 KLDEEVAAAMVAGFGGVLTQLTQEQADYLGVAVEGP 452
Cdd:TIGR00936 372 ELDEMVARLKLEAMGIEIDELTEEQKEYLGSWEEGT 407
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AdoHcyase |
pfam05221 |
S-adenosyl-L-homocysteine hydrolase; |
10-459 |
0e+00 |
|
S-adenosyl-L-homocysteine hydrolase;
Pssm-ID: 461594 Cd Length: 429 Bit Score: 793.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 10 DYKVADISLADYGRKEIKLAEAEMPALIGLRKRYAASKPLAGAKILGCIHMTIQTAVLIETLVELGAEVRWTSCNIFSTQ 89
Cdd:pfam05221 1 DYKVADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 90 DHAAAAIAARGIPVFAWKGETEEEYVWCLEQQINVNGQPWDANMILDDGGDLTALVHEKYPALLERIHGITEETTTGVQR 169
Cdd:pfam05221 81 DHAAAAIAAAGVPVFAWKGETLEEYWWCTEQALTWPPDGGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 170 LIEMWKDGSLKVPAINVNDSVTKSKNDNKYGCRHSLNDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIVRVTE 249
Cdd:pfam05221 161 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 250 VDPICAMQACMDGYEVVSPYkngvqtgkkedinhDLLGNTDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTEIDTA 329
Cdd:pfam05221 241 IDPICALQAAMEGYEVVTME--------------DVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNIGHFDNEIDEI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 330 YL---RGYKWVEVKPQVHQVYRSEDenNYLILLSEGRLVNLGNATGHPSRVMDGSFANQVLGQIHLFQekfadlpaNEKA 406
Cdd:pfam05221 307 VLallKGVKWVNIKPQVDDITFPDG--KSIIVLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELWT--------NDKE 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 507075160 407 AKIRVEVLPKKLDEEVAAAMVAGFGGVLTQLTQEQADYLGVAVEGPFKSDAYK 459
Cdd:pfam05221 377 YENGVYVLPKKLDEKVARLHLEKLGAKLTELTKEQADYIGVPVEGPFKPDHYR 429
|
|
| AdoHcyase |
smart00996 |
S-adenosyl-L-homocysteine hydrolase; |
12-459 |
0e+00 |
|
S-adenosyl-L-homocysteine hydrolase;
Pssm-ID: 214963 [Multi-domain] Cd Length: 426 Bit Score: 785.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 12 KVADISLADYGRKEIKLAEAEMPALIGLRKRYAASKPLAGAKILGCIHMTIQTAVLIETLVELGAEVRWTSCNIFSTQDH 91
Cdd:smart00996 1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 92 AAAAIAARGIPVFAWKGETEEEYVWCLEQQINVNGqPWDANMILDDGGDLTALVHEKYPALLERIHGITEETTTGVQRLI 171
Cdd:smart00996 81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPD-GWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 172 EMWKDGSLKVPAINVNDSVTKSKNDNKYGCRHSLNDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIVRVTEVD 251
Cdd:smart00996 160 QMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 252 PICAMQACMDGYEVVSPykngvqtgkkedinHDLLGNTDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTEIDTAYL 331
Cdd:smart00996 240 PICALQAAMDGFEVVTM--------------EEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 332 RGY---KWVEVKPQVHQVYRSedENNYLILLSEGRLVNLGNATGHPSRVMDGSFANQVLGQIHLFQekfadlpaNEKAAK 408
Cdd:smart00996 306 RNNpglKWENIKPQVDHITFP--DGKRIILLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELFT--------KPGKYK 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 507075160 409 IRVEVLPKKLDEEVAAAMVAGFGGVLTQLTQEQADYLGVAVEGPFKSDAYK 459
Cdd:smart00996 376 NGVYVLPKKLDEKVARLHLEKLGAKLTKLTKEQADYIGVPVEGPFKPDHYR 426
|
|
| PRK05476 |
PRK05476 |
S-adenosyl-L-homocysteine hydrolase; Provisional |
6-454 |
0e+00 |
|
S-adenosyl-L-homocysteine hydrolase; Provisional
Pssm-ID: 235488 [Multi-domain] Cd Length: 425 Bit Score: 715.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 6 ASFTDYKVADISLADYGRKEIKLAEAEMPALIGLRKRYAASKPLAGAKILGCIHMTIQTAVLIETLVELGAEVRWTSCNI 85
Cdd:PRK05476 3 ATGTDYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 86 FSTQDHAAAAIAARGIPVFAWKGETEEEYVWCLEQQInvngQPWDANMILDDGGDLTALVHEKYPALLERIHGITEETTT 165
Cdd:PRK05476 83 FSTQDDVAAALAAAGIPVFAWKGETLEEYWECIERAL----DGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 166 GVQRLIEMWKDGSLKVPAINVNDSVTKSKNDNKYGCRHSLNDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIV 245
Cdd:PRK05476 159 GVHRLYAMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 246 RVTEVDPICAMQACMDGYEVVSpykngvqtgkkediNHDLLGNTDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTE 325
Cdd:PRK05476 239 IVTEVDPICALQAAMDGFRVMT--------------MEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 326 IDTAYLRGY--KWVEVKPQVHQVYRseDENNYLILLSEGRLVNLGNATGHPSRVMDGSFANQVLGQIHLFQekfadlpaN 403
Cdd:PRK05476 305 IDVAALEELavKWREIKPQVDEYTL--PDGKRIILLAEGRLVNLGAATGHPSEVMDMSFANQALAQIELFT--------N 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 507075160 404 EKAAKIRVEVLPKKLDEEVAAAMVAGFGGVLTQLTQEQADYLGVAVEGPFK 454
Cdd:PRK05476 375 RGKLEPGVYVLPKELDEEVARLKLKALGVKLDELTEEQAEYIGVWVEGPFK 425
|
|
| SAM1 |
COG0499 |
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism]; |
6-452 |
0e+00 |
|
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
Pssm-ID: 440265 [Multi-domain] Cd Length: 420 Bit Score: 715.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 6 ASFTDYKVADISLADYGRKEIKLAEAEMPALIGLRKRYAASKPLAGAKILGCIHMTIQTAVLIETLVELGAEVRWTSCNI 85
Cdd:COG0499 1 TAPMDYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 86 FSTQDHAAAAIAARGIPVFAWKGETEEEYVWCLEQQINvngqpWDANMILDDGGDLTALVHEKYPALLERIHGITEETTT 165
Cdd:COG0499 81 LSTQDDVAAALAAAGIPVFAWKGETLEEYYWCIEQALD-----HGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 166 GVQRLIEMWKDGSLKVPAINVNDSVTKSKNDNKYGCRHSLNDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIV 245
Cdd:COG0499 156 GVHRLRAMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 246 RVTEVDPICAMQACMDGYEVVSPykngvqtgkkedinHDLLGNTDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTE 325
Cdd:COG0499 236 IVTEVDPICALEAAMDGFRVMPM--------------EEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 326 IDTAYLRGY--KWVEVKPQVHQvYRSEDeNNYLILLSEGRLVNLGNATGHPSRVMDGSFANQVLGQIHLFQekfadlpaN 403
Cdd:COG0499 302 IDVAALEKLavEKREIRPQVDE-YTLPD-GRRIYLLAEGRLVNLAAATGHPSEVMDMSFANQALAQIYLVK--------N 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 507075160 404 EKAAKIRVEVLPKKLDEEVAAAMVAGFGGVLTQLTQEQADYLGVAVEGP 452
Cdd:COG0499 372 GDKLEPGVYVLPKELDEEVARLKLEALGVKIDTLTEEQAEYLGSWVEGP 420
|
|
| SAHH |
cd00401 |
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ... |
20-447 |
0e+00 |
|
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.
Pssm-ID: 240619 [Multi-domain] Cd Length: 402 Bit Score: 646.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 20 DYGRKEIKLAEAEMPALIGLRKRYAASKPLAGAKILGCIHMTIQTAVLIETLVELGAEVRWTSCNIFSTQDHAAAAIAAR 99
Cdd:cd00401 1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 100 GIPVFAWKGETEEEYVWCLEQQINvngqpWDANMILDDGGDLTALVHEKYPALLERIHGITEETTTGVQRLIEMWKDGSL 179
Cdd:cd00401 81 GIPVFAWKGETEEEYWWCIEQALD-----HGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 180 KVPAINVNDSVTKSKNDNKYGCRHSLNDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIVRVTEVDPICAMQAC 259
Cdd:cd00401 156 LFPAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 260 MDGYEVVsPYKNGVQTGkkedinhdllgntDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTEIDTAYLR--GYKWV 337
Cdd:cd00401 236 MDGFEVM-PMEEAAKIG-------------DIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEelAVEKR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 338 EVKPQVHQvYRSEDeNNYLILLSEGRLVNLGNATGHPSRVMDGSFANQVLGQIHLFQEKfadlpaneKAAKIRVEVLPKK 417
Cdd:cd00401 302 EIRPQVDE-YTLPD-GRRIILLAEGRLVNLACATGHPSFVMDMSFANQALAQIELWKNR--------DKLEPGVYVLPKE 371
|
410 420 430
....*....|....*....|....*....|
gi 507075160 418 LDEEVAAAMVAGFGGVLTQLTQEQADYLGV 447
Cdd:cd00401 372 LDEEVARLKLEALGIKLDKLTEEQAEYLGS 401
|
|
| PTZ00075 |
PTZ00075 |
Adenosylhomocysteinase; Provisional |
9-460 |
0e+00 |
|
Adenosylhomocysteinase; Provisional
Pssm-ID: 240258 Cd Length: 476 Bit Score: 579.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 9 TDYKVADISLADYGRKEIKLAEAEMPALIGLRKRYAASKPLAGAKILGCIHMTIQTAVLIETLVELGAEVRWTSCNIFST 88
Cdd:PTZ00075 3 TDYKVKDISLAEFGRKEIELAENEMPGLMALREEYGPSKPLKGARITGCLHMTVQTAVLIETLKALGAEVRWCSCNIFST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 89 QDHAAAAIAARG-IPVFAWKGETEEEYVWCLEQQIN-VNGQPwdANMILDDGGDLTALVHE------------------- 147
Cdd:PTZ00075 83 QDHAAAAIAKAGsVPVFAWKGETLEEYWWCTEQALKwPNGDG--PNLIVDDGGDATLLVHEgvkaeklyeekgilpdpld 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 148 ----------------------KYPALLERIHGITEETTTGVQRLIEMWKDGSLKVPAINVNDSVTKSKNDNKYGCRHSL 205
Cdd:PTZ00075 161 psnedekclltvlkklltknpdKWTNLVKKIVGVSEETTTGVHRLYKMLKKGELLFPAINVNDSVTKSKFDNIYGCRHSL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 206 NDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIVRVTEVDPICAMQACMDGYEVVSpykngvqtgkKEDINHDl 285
Cdd:PTZ00075 241 IDGIFRATDVMIAGKTVVVCGYGDVGKGCAQALRGFGARVVVTEIDPICALQAAMEGYQVVT----------LEDVVET- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 286 lgnTDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTEIDTAYLRGY---KWVEVKPQVHQvYRSEDeNNYLILLSEG 362
Cdd:PTZ00075 310 ---ADIFVTATGNKDIITLEHMRRMKNNAIVGNIGHFDNEIQVAELEAYpgiEIVEIKPQVDR-YTFPD-GKGIILLAEG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 363 RLVNLGNATGHPSRVMDGSFANQVLGQIHLFQEKFADLPANEkaakirVEVLPKKLDEEVAAAMVAGFGGVLTQLTQEQA 442
Cdd:PTZ00075 385 RLVNLGCATGHPSFVMSNSFTNQVLAQIELWENRDTGKYPNG------VYKLPKELDEKVARLHLKKLGAKLTKLTDKQA 458
|
490
....*....|....*...
gi 507075160 443 DYLGVAVEGPFKSDAYKY 460
Cdd:PTZ00075 459 EYIGVPVDGPYKSDHYRY 476
|
|
| PLN02494 |
PLN02494 |
adenosylhomocysteinase |
10-460 |
0e+00 |
|
adenosylhomocysteinase
Pssm-ID: 178111 [Multi-domain] Cd Length: 477 Bit Score: 515.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 10 DYKVADISLADYGRKEIKLAEAEMPALIGLRKRYAASKPLAGAKILGCIHMTIQTAVLIETLVELGAEVRWTSCNIFSTQ 89
Cdd:PLN02494 5 EYKVKDMSQADFGRLEIELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNIFSTQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 90 DHAAAAIAARGIPVFAWKGETEEEYVWCLEQQINVnGQPWDANMILDDGGDLTALVHE---------------------- 147
Cdd:PLN02494 85 DHAAAAIARDSAAVFAWKGETLQEYWWCTERALDW-GPGGGPDLIVDDGGDATLLIHEgvkaeeefekdgtlpdptstdn 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 148 -------------------KYPALLERIHGITEETTTGVQRLIEMWKDGSLKVPAINVNDSVTKSKNDNKYGCRHSLNDA 208
Cdd:PLN02494 164 aefkivltiikdglkvdpkKYHKMKERLVGVSEETTTGVKRLYQMQKNGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 209 IKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIVRVTEVDPICAMQACMDGYEVVSPykngvqtgkkedinHDLLGN 288
Cdd:PLN02494 244 LMRATDVMIAGKVAVICGYGDVGKGCAAAMKAAGARVIVTEIDPICALQALMEGYQVLTL--------------EDVVSE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 289 TDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTEIDTAYLRGY---KWVEVKPQVHQvYRSEDENNYLILLSEGRLV 365
Cdd:PLN02494 310 ADIFVTTTGNKDIIMVDHMRKMKNNAIVCNIGHFDNEIDMLGLETYpgvKRITIKPQTDR-WVFPDTGSGIIVLAEGRLM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 366 NLGNATGHPSRVMDGSFANQVLGQIHLFQEKfadlpANEKAAKiRVEVLPKKLDEEVAAAMVAGFGGVLTQLTQEQADYL 445
Cdd:PLN02494 389 NLGCATGHPSFVMSCSFTNQVIAQLELWNEK-----KSGKYEK-KVYVLPKHLDEKVAALHLGKLGAKLTKLSKDQADYI 462
|
490
....*....|....*
gi 507075160 446 GVAVEGPFKSDAYKY 460
Cdd:PLN02494 463 NVPVEGPYKPAHYRY 477
|
|
| ahcY |
TIGR00936 |
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ... |
20-452 |
1.03e-180 |
|
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the regeneration of the methyl donor S-adenosylmethionine. Species that lack this enzyme are likely to have adenosylhomocysteine nucleosidase (EC 3.2.2.9), an enzyme which also acts as 5'-methyladenosine nucleosidase (see TIGR01704). [Energy metabolism, Amino acids and amines]
Pssm-ID: 213572 Cd Length: 407 Bit Score: 510.79 E-value: 1.03e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 20 DYGRKEIKLAEAEMPALIGLRKRYAASKPLAGAKILGCIHMTIQTAVLIETLVELGAEVRWTSCNIFSTQDHAAAA-IAA 98
Cdd:TIGR00936 1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAAlAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 99 RGIPVFAWKGETEEEYVWCLEQQINVngqpwDANMILDDGGDLTALVHEKYPALLERIHGITEETTTGVQRLIEMWKDGS 178
Cdd:TIGR00936 81 AGIPVFAWRGETNEEYYWAIEQVLDH-----EPNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 179 LKVPAINVNDSVTKSKNDNKYGCRHSLNDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIVRVTEVDPICAMQA 258
Cdd:TIGR00936 156 LKFPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 259 CMDGYEVVspykngvqtgKKEDINHDllgnTDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTEIDTAYLR--GYKW 336
Cdd:TIGR00936 236 AMDGFRVM----------TMEEAAKI----GDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEelAVEK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 337 VEVKPQVHQvYRSEDENNyLILLSEGRLVNLGNATGHPSRVMDGSFANQVLGQIHLFQEkfadlpaNEKAAKiRVEVLPK 416
Cdd:TIGR00936 302 VNVRPQVDE-YILKDGRR-IYLLAEGRLVNLAAAEGHPSEVMDMSFANQALAAEYLWKN-------HDKLEP-GVYRLPK 371
|
410 420 430
....*....|....*....|....*....|....*.
gi 507075160 417 KLDEEVAAAMVAGFGGVLTQLTQEQADYLGVAVEGP 452
Cdd:TIGR00936 372 ELDEMVARLKLEAMGIEIDELTEEQKEYLGSWEEGT 407
|
|
| AdoHcyase_NAD |
smart00997 |
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
197-372 |
2.31e-78 |
|
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
Pssm-ID: 198065 [Multi-domain] Cd Length: 162 Bit Score: 240.82 E-value: 2.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 197 NKYGCRHSLNDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIVRVTEVDPICAMQACMDGYEVVSPykngvqtg 276
Cdd:smart00997 1 NRYGTGESLLDGILRATNVLLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPIRALEAAMDGFEVMKM-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 277 kkedinHDLLGNTDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTEIDTAYLRGY--KWVEVKPQVHQvYRSEDeNN 354
Cdd:smart00997 73 ------EEAAKRADIFVTATGNKDVITREHFRAMKDGAILANAGHFDVEIDVAALEELavEKREVRPQVDE-YTLPD-GK 144
|
170
....*....|....*...
gi 507075160 355 YLILLSEGRLVNLGNATG 372
Cdd:smart00997 145 RIYLLAEGRLVNLAAATG 162
|
|
| AdoHcyase_NAD |
pfam00670 |
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
197-372 |
2.90e-69 |
|
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
Pssm-ID: 395543 [Multi-domain] Cd Length: 162 Bit Score: 217.60 E-value: 2.90e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 197 NKYGCRHSLNDAIKRATDMLLSGRRALVVGYGDVGKGSAQSLRQEGMIVRVTEVDPICAMQACMDGYEVVspykngvqtg 276
Cdd:pfam00670 1 NLYGCRESLIDGIKRATDVMIAGKVAVVCGYGDVGKGCAASLKGQGARVIVTEIDPICALQAAMEGFQVV---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 277 KKEDINHDllgnTDLVVTTTGNYHVCDAAMLDSLKAGAVVCNIGHFDTEIDTAYLRGY--KWVEVKPQVHQvYRSEDeNN 354
Cdd:pfam00670 71 TLEEVVDK----ADIFVTTTGNKDIITGEHMAKMKNDAIVCNIGHFDNEIDVAWLEANgkKKENIKPQVDR-YTLPD-GK 144
|
170
....*....|....*...
gi 507075160 355 YLILLSEGRLVNLGNATG 372
Cdd:pfam00670 145 HIILLAEGRLVNLGCATG 162
|
|
| FDH_GDH_like |
cd12154 |
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ... |
54-392 |
5.20e-42 |
|
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases.
Pssm-ID: 240631 [Multi-domain] Cd Length: 310 Bit Score: 151.23 E-value: 5.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 54 ILGCIHMTIQTA------VLIETLVELGAEVRWTSCNIFSTQDHAAAAIaargipvfawkgeteeeYVWCLEQQINVngQ 127
Cdd:cd12154 1 IAGPKEIKNEEFrvglspSVVATLVEAGHEVRVETGAGIGAGFADQAYV-----------------QAGAIVVTLAK--A 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 128 PWDANMILDDGGDLTAlVHEKYPALLErIHGITEETTTGVQRLIEMwKDGSLKVPAINVNDSVTKSKNDNKYGCRHSLND 207
Cdd:cd12154 62 LWSLDVVLKVKEPLTN-AEYALIQKLG-DRLLFTYTIGADHRDLTE-ALARAGLTAIAVEGVELPLLTSNSIGAGELSVQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 208 AIKRATDML----------LSGRRALVVGYGDVGKGSAQSLRQEGMIVRVTEVDPICAMQACMDGYEVVspykngvqtgk 277
Cdd:cd12154 139 FIARFLEVQqpgrlggapdVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKNV----------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 278 kEDINhDLLGNTDLVVTTTG-----NYHVCDAAMLDSLKAGAVVCNIGHFDTEIDTAYLRGYkwVEVKpqvHQVyrsede 352
Cdd:cd12154 208 -EELE-EALAEADVIVTTTLlpgkrAGILVPEELVEQMKPGSVIVNVAVGAVGCVQALHTQL--LEEG---HGV------ 274
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 507075160 353 nnylILLSEGRLVNLGNATGHPSRVMDGSFANQVLGQIHL 392
Cdd:cd12154 275 ----VHYGDVNMPGPGCAMGVPWDATLRLAANTLPALVKL 310
|
|
| 2-Hacid_dh_1 |
cd05300 |
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ... |
217-320 |
1.63e-06 |
|
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomains but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants.
Pssm-ID: 240625 [Multi-domain] Cd Length: 313 Bit Score: 49.83 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 217 LSGRRALVVGYGDVGKGSAQSLRQEGMIV-----RVTEVDPicamqaCMDgyEVVSPykngvqtgkkEDInHDLLGNTDL 291
Cdd:cd05300 132 LAGKTVLIVGLGDIGREIARRAKAFGMRVigvrrSGRPAPP------VVD--EVYTP----------DEL-DELLPEADY 192
|
90 100 110
....*....|....*....|....*....|...
gi 507075160 292 VVT----TTGNYHVCDAAMLDSLKAGAVVCNIG 320
Cdd:cd05300 193 VVNalplTPETRGLFNAERFAAMKPGAVLINVG 225
|
|
| 2-Hacid_dh_7 |
cd12166 |
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ... |
217-325 |
4.03e-06 |
|
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240643 [Multi-domain] Cd Length: 300 Bit Score: 48.36 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 217 LSGRRALVVGYGDVGKGSAQSLRQEGmiVRVTEVdpicAMQAcMDGYEVVSPykngvqtgkkEDInHDLLGNTDLVVT-- 294
Cdd:cd12166 130 LADRRVLIVGYGSIGRAIERRLAPFE--VRVTRV----ARTA-RPGEQVHGI----------DEL-PALLPEADVVVLiv 191
|
90 100 110
....*....|....*....|....*....|....*.
gi 507075160 295 --TTGNYHVCDAAMLDSLKAGAVVCNIG---HFDTE 325
Cdd:cd12166 192 plTDETRGLVDAEFLARMPDGALLVNVArgpVVDTD 227
|
|
| NAD_binding_7 |
pfam13241 |
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria. |
217-319 |
5.32e-04 |
|
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
Pssm-ID: 433055 [Multi-domain] Cd Length: 104 Bit Score: 39.38 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 217 LSGRRALVVGYGDVGKGSAQSLRQEGmiVRVTEVDPicamqacmdgyEVVSPYKNGVQTgKKEDINHDLLGnTDLVVTTT 296
Cdd:pfam13241 5 LRGKRVLVVGGGEVAARKARKLLEAG--AKVTVVSP-----------EITPFLEGLLDL-IRREFEGDLDG-ADLVIAAT 69
|
90 100
....*....|....*....|....*..
gi 507075160 297 G----NYHVCDAAmldslKAGAVVCNI 319
Cdd:pfam13241 70 DdpelNERIAALA-----RARGILVNV 91
|
|
| 2-Hacid_dh_C |
pfam02826 |
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ... |
217-320 |
3.17e-03 |
|
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.
Pssm-ID: 427007 [Multi-domain] Cd Length: 178 Bit Score: 38.63 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507075160 217 LSGRRALVVGYGDVGKGSAQSLRQEGMIVRVTEVDPICAMQACMDGYEVVSPykngvqtgkkedinHDLLGNTDLVV--- 293
Cdd:pfam02826 34 LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSL--------------DELLAESDVVSlhl 99
|
90 100
....*....|....*....|....*...
gi 507075160 294 -TTTGNYHVCDAAMLDSLKAGAVVCNIG 320
Cdd:pfam02826 100 pLTPETRHLINAERLALMKPGAILINTA 127
|
|
| |
