|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02494 |
PLN02494 |
adenosylhomocysteinase |
8-482 |
0e+00 |
|
adenosylhomocysteinase
Pssm-ID: 178111 [Multi-domain] Cd Length: 477 Bit Score: 956.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 8 TAGREYKVRDMAQADFGRMEIELAQVEMPGLMSCIAEFGPAQPLAGANISGSLHMTIQTAVLIETLVALGANVRWCSCNI 87
Cdd:PLN02494 1 SSGREYKVKDMSQADFGRLEIELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 88 FSTQDHAAAAVARDSAAVFAWKGETLEEYWWCTDQMLNWG-EGSLDIIVDDGGDATLLIHEGYKAELEFAKSGAIPDPAS 166
Cdd:PLN02494 81 FSTQDHAAAAIARDSAAVFAWKGETLQEYWWCTERALDWGpGGGPDLIVDDGGDATLLIHEGVKAEEEFEKDGTLPDPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 167 TDNAEMKCVLKIIAENLKTNPKRWQKIVSTCVGVSEETTTGVKRLYEMQKAGELLFPAINVNDSVTKCKFDNLYGCRHSL 246
Cdd:PLN02494 161 TDNAEFKIVLTIIKDGLKVDPKKYHKMKERLVGVSEETTTGVKRLYQMQKNGTLLFPAINVNDSVTKSKFDNLYGCRHSL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 247 PDGIMRATDVMIASKTCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVDIFITTTGNK 326
Cdd:PLN02494 241 PDGLMRATDVMIAGKVAVICGYGDVGKGCAAAMKAAGARVIVTEIDPICALQALMEGYQVLTLEDVVSEADIFVTTTGNK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 327 DIIMVQHMEKMKNNAIVGNIGHFDNEIDMAGLESYPGIKRQNIKPQCDRFEFPD-GHGIIMLAEGRLLNLGCATGHPSFV 405
Cdd:PLN02494 321 DIIMVDHMRKMKNNAIVCNIGHFDNEIDMLGLETYPGVKRITIKPQTDRWVFPDtGSGIIVLAEGRLMNLGCATGHPSFV 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145350366 406 MSCSFTNQAIAQLELWNERKSGKYEKKVYVLPKHLDEKVAMLHLAKIGVKLTKLSTDQAQYINVPVEGPYKPAAYRY 482
Cdd:PLN02494 401 MSCSFTNQVIAQLELWNEKKSGKYEKKVYVLPKHLDEKVAALHLGKLGAKLTKLSKDQADYINVPVEGPYKPAHYRY 477
|
|
| AdoHcyase |
pfam05221 |
S-adenosyl-L-homocysteine hydrolase; |
12-481 |
0e+00 |
|
S-adenosyl-L-homocysteine hydrolase;
Pssm-ID: 461594 Cd Length: 429 Bit Score: 837.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 12 EYKVRDMAQADFGRMEIELAQVEMPGLMSCIAEFGPAQPLAGANISGSLHMTIQTAVLIETLVALGANVRWCSCNIFSTQ 91
Cdd:pfam05221 1 DYKVADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 92 DHAAAAVARDSAAVFAWKGETLEEYWWCTDQMLNW--GEGSLDIIVDDGGDATLLIHegykaelefaksgaipdpastdn 169
Cdd:pfam05221 81 DHAAAAIAAAGVPVFAWKGETLEEYWWCTEQALTWppDGGGPNMILDDGGDATLLVH----------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 170 aemkcvlkiiaenlktnpKRWQKIVSTCVGVSEETTTGVKRLYEMQKAGELLFPAINVNDSVTKCKFDNLYGCRHSLPDG 249
Cdd:pfam05221 138 ------------------KKYPRIAKGIKGVSEETTTGVHRLYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 250 IMRATDVMIASKTCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVDIFITTTGNKDII 329
Cdd:pfam05221 200 IKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 330 MVQHMEKMKNNAIVGNIGHFDNEIDMAGLESYPGIKRQNIKPQCDRFEFPDGHGIIMLAEGRLLNLGCATGHPSFVMSCS 409
Cdd:pfam05221 280 TVEHMDHMKMMAIVCNIGHFDNEIDEIVLALLKGVKWVNIKPQVDDITFPDGKSIIVLAEGRLVNLGCATGHPSFVMSNS 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145350366 410 FTNQAIAQLELWNERKsgKYEKKVYVLPKHLDEKVAMLHLAKIGVKLTKLSTDQAQYINVPVEGPYKPAAYR 481
Cdd:pfam05221 360 FTNQVLAQIELWTNDK--EYENGVYVLPKKLDEKVARLHLEKLGAKLTELTKEQADYIGVPVEGPFKPDHYR 429
|
|
| AdoHcyase |
smart00996 |
S-adenosyl-L-homocysteine hydrolase; |
14-481 |
0e+00 |
|
S-adenosyl-L-homocysteine hydrolase;
Pssm-ID: 214963 [Multi-domain] Cd Length: 426 Bit Score: 787.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 14 KVRDMAQADFGRMEIELAQVEMPGLMSCIAEFGPAQPLAGANISGSLHMTIQTAVLIETLVALGANVRWCSCNIFSTQDH 93
Cdd:smart00996 1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 94 AAAAVARDSAAVFAWKGETLEEYWWCTDQMLNWGEGS-LDIIVDDGGDATLLIHegykaelefaksgaipdpastdnaem 172
Cdd:smart00996 81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPDGWgPNMILDDGGDATLLVH-------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 173 kcvlkiiaenlktnpKRWQKIVSTCVGVSEETTTGVKRLYEMQKAGELLFPAINVNDSVTKCKFDNLYGCRHSLPDGIMR 252
Cdd:smart00996 135 ---------------KKYPRMLKKIRGVSEETTTGVHRLYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 253 ATDVMIASKTCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVDIFITTTGNKDIIMVQ 332
Cdd:smart00996 200 ATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDPICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITRE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 333 HMEKMKNNAIVGNIGHFDNEIDMAGLESYPGIKRQNIKPQCDRFEFPDGHGIIMLAEGRLLNLGCATGHPSFVMSCSFTN 412
Cdd:smart00996 280 HMRAMKDGAIVCNIGHFDNEIDVASLRNNPGLKWENIKPQVDHITFPDGKRIILLAEGRLVNLGCATGHPSFVMSNSFTN 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145350366 413 QAIAQLELWNerKSGKYEKKVYVLPKHLDEKVAMLHLAKIGVKLTKLSTDQAQYINVPVEGPYKPAAYR 481
Cdd:smart00996 360 QVLAQIELFT--KPGKYKNGVYVLPKKLDEKVARLHLEKLGAKLTKLTKEQADYIGVPVEGPFKPDHYR 426
|
|
| SAM1 |
COG0499 |
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism]; |
8-474 |
0e+00 |
|
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
Pssm-ID: 440265 [Multi-domain] Cd Length: 420 Bit Score: 724.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 8 TAGREYKVRDMAQADFGRMEIELAQVEMPGLMSCIAEFGPAQPLAGANISGSLHMTIQTAVLIETLVALGANVRWCSCNI 87
Cdd:COG0499 1 TAPMDYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 88 FSTQDHAAAAVARDSAAVFAWKGETLEEYWWCTDQMLNWGegsLDIIVDDGGDATLLIHegykaelefaksgaipdpast 167
Cdd:COG0499 81 LSTQDDVAAALAAAGIPVFAWKGETLEEYYWCIEQALDHG---PNIILDDGGDLTLLLH--------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 168 dnaemkcvlkiiaenlktnpKRWQKIVSTCVGVSEETTTGVKRLYEMQKAGELLFPAINVNDSVTKCKFDNLYGCRHSLP 247
Cdd:COG0499 137 --------------------KERPELLAGIIGGTEETTTGVHRLRAMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 248 DGIMRATDVMIASKTCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVDIFITTTGNKD 327
Cdd:COG0499 197 DGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVDPICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 328 IIMVQHMEKMKNNAIVGNIGHFDNEIDMAGLESYPGIKRqNIKPQCDRFEFPDGHGIIMLAEGRLLNLGCATGHPSFVMS 407
Cdd:COG0499 277 VITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKR-EIRPQVDEYTLPDGRRIYLLAEGRLVNLAAATGHPSEVMD 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145350366 408 CSFTNQAIAQLELWNERksGKYEKKVYVLPKHLDEKVAMLHLAKIGVKLTKLSTDQAQYINVPVEGP 474
Cdd:COG0499 356 MSFANQALAQIYLVKNG--DKLEPGVYVLPKELDEEVARLKLEALGVKIDTLTEEQAEYLGSWVEGP 420
|
|
| SAHH |
cd00401 |
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ... |
22-470 |
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: 708.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 22 DFGRMEIELAQVEMPGLMSCIAEFGPAQPLAGANISGSLHMTIQTAVLIETLVALGANVRWCSCNIFSTQDHAAAAVARD 101
Cdd:cd00401 1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 102 SAAVFAWKGETLEEYWWCTDQMLNWGegsLDIIVDDGGDATLLIHEGYKAELEfaksgaipdpastdnaemkcvlkiiae 181
Cdd:cd00401 81 GIPVFAWKGETEEEYWWCIEQALDHG---PNLIIDDGGDLTHLLHTKRPDLLK--------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 182 nlktnpkrwqkivsTCVGVSEETTTGVKRLYEMQKAGELLFPAINVNDSVTKCKFDNLYGCRHSLPDGIMRATDVMIASK 261
Cdd:cd00401 131 --------------KIIGGSEETTTGVHRLRAMEKEGKLLFPAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 262 TCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVDIFITTTGNKDIIMVQHMEKMKNNA 341
Cdd:cd00401 197 VVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMDGFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 342 IVGNIGHFDNEIDMAGLESYpGIKRQNIKPQCDRFEFPDGHGIIMLAEGRLLNLGCATGHPSFVMSCSFTNQAIAQLELW 421
Cdd:cd00401 277 ILCNAGHFDVEIDVAALEEL-AVEKREIRPQVDEYTLPDGRRIILLAEGRLVNLACATGHPSFVMDMSFANQALAQIELW 355
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 145350366 422 NERksGKYEKKVYVLPKHLDEKVAMLHLAKIGVKLTKLSTDQAQYINVP 470
Cdd:cd00401 356 KNR--DKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQAEYLGSW 402
|
|
| ahcY |
TIGR00936 |
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ... |
22-474 |
0e+00 |
|
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: 558.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 22 DFGRMEIELAQVEMPGLMSCIAEFGPAQPLAGANISGSLHMTIQTAVLIETLVALGANVRWCSCNIFSTQDHAAAAVARD 101
Cdd:TIGR00936 1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAALAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 102 S-AAVFAWKGETLEEYWWCTDQMLnwgEGSLDIIVDDGGDATLLIHEgykaelefaksgaipdpastdnaemkcvlkiia 180
Cdd:TIGR00936 81 AgIPVFAWRGETNEEYYWAIEQVL---DHEPNIIIDDGADLIFLLHT--------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 181 enlktnpkRWQKIVSTCVGVSEETTTGVKRLYEMQKAGELLFPAINVNDSVTKCKFDNLYGCRHSLPDGIMRATDVMIAS 260
Cdd:TIGR00936 125 --------ERPELLEKIIGGSEETTTGVIRLRAMEAEGVLKFPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 261 KTCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVDIFITTTGNKDIIMVQHMEKMKNN 340
Cdd:TIGR00936 197 KTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAMDGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 341 AIVGNIGHFDNEIDMAGLESYpGIKRQNIKPQCDRFEFPDGHGIIMLAEGRLLNLGCATGHPSFVMSCSFTNQAIAQLEL 420
Cdd:TIGR00936 277 AIVANIGHFDVEIDVKALEEL-AVEKVNVRPQVDEYILKDGRRIYLLAEGRLVNLAAAEGHPSEVMDMSFANQALAAEYL 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 145350366 421 WNERksGKYEKKVYVLPKHLDEKVAMLHLAKIGVKLTKLSTDQAQYINVPVEGP 474
Cdd:TIGR00936 356 WKNH--DKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQKEYLGSWEEGT 407
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02494 |
PLN02494 |
adenosylhomocysteinase |
8-482 |
0e+00 |
|
adenosylhomocysteinase
Pssm-ID: 178111 [Multi-domain] Cd Length: 477 Bit Score: 956.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 8 TAGREYKVRDMAQADFGRMEIELAQVEMPGLMSCIAEFGPAQPLAGANISGSLHMTIQTAVLIETLVALGANVRWCSCNI 87
Cdd:PLN02494 1 SSGREYKVKDMSQADFGRLEIELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 88 FSTQDHAAAAVARDSAAVFAWKGETLEEYWWCTDQMLNWG-EGSLDIIVDDGGDATLLIHEGYKAELEFAKSGAIPDPAS 166
Cdd:PLN02494 81 FSTQDHAAAAIARDSAAVFAWKGETLQEYWWCTERALDWGpGGGPDLIVDDGGDATLLIHEGVKAEEEFEKDGTLPDPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 167 TDNAEMKCVLKIIAENLKTNPKRWQKIVSTCVGVSEETTTGVKRLYEMQKAGELLFPAINVNDSVTKCKFDNLYGCRHSL 246
Cdd:PLN02494 161 TDNAEFKIVLTIIKDGLKVDPKKYHKMKERLVGVSEETTTGVKRLYQMQKNGTLLFPAINVNDSVTKSKFDNLYGCRHSL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 247 PDGIMRATDVMIASKTCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVDIFITTTGNK 326
Cdd:PLN02494 241 PDGLMRATDVMIAGKVAVICGYGDVGKGCAAAMKAAGARVIVTEIDPICALQALMEGYQVLTLEDVVSEADIFVTTTGNK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 327 DIIMVQHMEKMKNNAIVGNIGHFDNEIDMAGLESYPGIKRQNIKPQCDRFEFPD-GHGIIMLAEGRLLNLGCATGHPSFV 405
Cdd:PLN02494 321 DIIMVDHMRKMKNNAIVCNIGHFDNEIDMLGLETYPGVKRITIKPQTDRWVFPDtGSGIIVLAEGRLMNLGCATGHPSFV 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145350366 406 MSCSFTNQAIAQLELWNERKSGKYEKKVYVLPKHLDEKVAMLHLAKIGVKLTKLSTDQAQYINVPVEGPYKPAAYRY 482
Cdd:PLN02494 401 MSCSFTNQVIAQLELWNEKKSGKYEKKVYVLPKHLDEKVAALHLGKLGAKLTKLSKDQADYINVPVEGPYKPAHYRY 477
|
|
| AdoHcyase |
pfam05221 |
S-adenosyl-L-homocysteine hydrolase; |
12-481 |
0e+00 |
|
S-adenosyl-L-homocysteine hydrolase;
Pssm-ID: 461594 Cd Length: 429 Bit Score: 837.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 12 EYKVRDMAQADFGRMEIELAQVEMPGLMSCIAEFGPAQPLAGANISGSLHMTIQTAVLIETLVALGANVRWCSCNIFSTQ 91
Cdd:pfam05221 1 DYKVADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 92 DHAAAAVARDSAAVFAWKGETLEEYWWCTDQMLNW--GEGSLDIIVDDGGDATLLIHegykaelefaksgaipdpastdn 169
Cdd:pfam05221 81 DHAAAAIAAAGVPVFAWKGETLEEYWWCTEQALTWppDGGGPNMILDDGGDATLLVH----------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 170 aemkcvlkiiaenlktnpKRWQKIVSTCVGVSEETTTGVKRLYEMQKAGELLFPAINVNDSVTKCKFDNLYGCRHSLPDG 249
Cdd:pfam05221 138 ------------------KKYPRIAKGIKGVSEETTTGVHRLYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 250 IMRATDVMIASKTCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVDIFITTTGNKDII 329
Cdd:pfam05221 200 IKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 330 MVQHMEKMKNNAIVGNIGHFDNEIDMAGLESYPGIKRQNIKPQCDRFEFPDGHGIIMLAEGRLLNLGCATGHPSFVMSCS 409
Cdd:pfam05221 280 TVEHMDHMKMMAIVCNIGHFDNEIDEIVLALLKGVKWVNIKPQVDDITFPDGKSIIVLAEGRLVNLGCATGHPSFVMSNS 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145350366 410 FTNQAIAQLELWNERKsgKYEKKVYVLPKHLDEKVAMLHLAKIGVKLTKLSTDQAQYINVPVEGPYKPAAYR 481
Cdd:pfam05221 360 FTNQVLAQIELWTNDK--EYENGVYVLPKKLDEKVARLHLEKLGAKLTELTKEQADYIGVPVEGPFKPDHYR 429
|
|
| PTZ00075 |
PTZ00075 |
Adenosylhomocysteinase; Provisional |
12-482 |
0e+00 |
|
Adenosylhomocysteinase; Provisional
Pssm-ID: 240258 Cd Length: 476 Bit Score: 828.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 12 EYKVRDMAQADFGRMEIELAQVEMPGLMSCIAEFGPAQPLAGANISGSLHMTIQTAVLIETLVALGANVRWCSCNIFSTQ 91
Cdd:PTZ00075 4 DYKVKDISLAEFGRKEIELAENEMPGLMALREEYGPSKPLKGARITGCLHMTVQTAVLIETLKALGAEVRWCSCNIFSTQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 92 DHAAAAVARD-SAAVFAWKGETLEEYWWCTDQMLNWGEGS-LDIIVDDGGDATLLIHEGYKAELEFAKSGAIPDPASTDN 169
Cdd:PTZ00075 84 DHAAAAIAKAgSVPVFAWKGETLEEYWWCTEQALKWPNGDgPNLIVDDGGDATLLVHEGVKAEKLYEEKGILPDPLDPSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 170 AEMKCVLKIIAENLKTNPKRWQKIVSTCVGVSEETTTGVKRLYEMQKAGELLFPAINVNDSVTKCKFDNLYGCRHSLPDG 249
Cdd:PTZ00075 164 EDEKCLLTVLKKLLTKNPDKWTNLVKKIVGVSEETTTGVHRLYKMLKKGELLFPAINVNDSVTKSKFDNIYGCRHSLIDG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 250 IMRATDVMIASKTCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVDIFITTTGNKDII 329
Cdd:PTZ00075 244 IFRATDVMIAGKTVVVCGYGDVGKGCAQALRGFGARVVVTEIDPICALQAAMEGYQVVTLEDVVETADIFVTATGNKDII 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 330 MVQHMEKMKNNAIVGNIGHFDNEIDMAGLESYPGIKRQNIKPQCDRFEFPDGHGIIMLAEGRLLNLGCATGHPSFVMSCS 409
Cdd:PTZ00075 324 TLEHMRRMKNNAIVGNIGHFDNEIQVAELEAYPGIEIVEIKPQVDRYTFPDGKGIILLAEGRLVNLGCATGHPSFVMSNS 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145350366 410 FTNQAIAQLELWNERKSGKYEKKVYVLPKHLDEKVAMLHLAKIGVKLTKLSTDQAQYINVPVEGPYKPAAYRY 482
Cdd:PTZ00075 404 FTNQVLAQIELWENRDTGKYPNGVYKLPKELDEKVARLHLKKLGAKLTKLTDKQAEYIGVPVDGPYKSDHYRY 476
|
|
| AdoHcyase |
smart00996 |
S-adenosyl-L-homocysteine hydrolase; |
14-481 |
0e+00 |
|
S-adenosyl-L-homocysteine hydrolase;
Pssm-ID: 214963 [Multi-domain] Cd Length: 426 Bit Score: 787.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 14 KVRDMAQADFGRMEIELAQVEMPGLMSCIAEFGPAQPLAGANISGSLHMTIQTAVLIETLVALGANVRWCSCNIFSTQDH 93
Cdd:smart00996 1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 94 AAAAVARDSAAVFAWKGETLEEYWWCTDQMLNWGEGS-LDIIVDDGGDATLLIHegykaelefaksgaipdpastdnaem 172
Cdd:smart00996 81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPDGWgPNMILDDGGDATLLVH-------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 173 kcvlkiiaenlktnpKRWQKIVSTCVGVSEETTTGVKRLYEMQKAGELLFPAINVNDSVTKCKFDNLYGCRHSLPDGIMR 252
Cdd:smart00996 135 ---------------KKYPRMLKKIRGVSEETTTGVHRLYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 253 ATDVMIASKTCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVDIFITTTGNKDIIMVQ 332
Cdd:smart00996 200 ATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDPICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITRE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 333 HMEKMKNNAIVGNIGHFDNEIDMAGLESYPGIKRQNIKPQCDRFEFPDGHGIIMLAEGRLLNLGCATGHPSFVMSCSFTN 412
Cdd:smart00996 280 HMRAMKDGAIVCNIGHFDNEIDVASLRNNPGLKWENIKPQVDHITFPDGKRIILLAEGRLVNLGCATGHPSFVMSNSFTN 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145350366 413 QAIAQLELWNerKSGKYEKKVYVLPKHLDEKVAMLHLAKIGVKLTKLSTDQAQYINVPVEGPYKPAAYR 481
Cdd:smart00996 360 QVLAQIELFT--KPGKYKNGVYVLPKKLDEKVARLHLEKLGAKLTKLTKEQADYIGVPVEGPFKPDHYR 426
|
|
| PRK05476 |
PRK05476 |
S-adenosyl-L-homocysteine hydrolase; Provisional |
6-476 |
0e+00 |
|
S-adenosyl-L-homocysteine hydrolase; Provisional
Pssm-ID: 235488 [Multi-domain] Cd Length: 425 Bit Score: 724.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 6 TSTAGREYKVRDMAQADFGRMEIELAQVEMPGLMSCIAEFGPAQPLAGANISGSLHMTIQTAVLIETLVALGANVRWCSC 85
Cdd:PRK05476 1 TTATGTDYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 86 NIFSTQDHAAAAVARDSAAVFAWKGETLEEYWWCTDQMLnwGEGSLDIIVDDGGDATLLIHEgykaelefaksgaipdpa 165
Cdd:PRK05476 81 NPFSTQDDVAAALAAAGIPVFAWKGETLEEYWECIERAL--DGHGPNMILDDGGDLTLLVHT------------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 166 stdnaemkcvlkiiaenlktnpkRWQKIVSTCVGVSEETTTGVKRLYEMQKAGELLFPAINVNDSVTKCKFDNLYGCRHS 245
Cdd:PRK05476 141 -----------------------ERPELLANIKGVTEETTTGVHRLYAMAKDGALKFPAINVNDSVTKSKFDNRYGTGES 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 246 LPDGIMRATDVMIASKTCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVDIFITTTGN 325
Cdd:PRK05476 198 LLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVDPICALQAAMDGFRVMTMEEAAELGDIFVTATGN 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 326 KDIIMVQHMEKMKNNAIVGNIGHFDNEIDMAGLESYPgIKRQNIKPQCDRFEFPDGHGIIMLAEGRLLNLGCATGHPSFV 405
Cdd:PRK05476 278 KDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELA-VKWREIKPQVDEYTLPDGKRIILLAEGRLVNLGAATGHPSEV 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145350366 406 MSCSFTNQAIAQLELWNERksGKYEKKVYVLPKHLDEKVAMLHLAKIGVKLTKLSTDQAQYINVPVEGPYK 476
Cdd:PRK05476 357 MDMSFANQALAQIELFTNR--GKLEPGVYVLPKELDEEVARLKLKALGVKLDELTEEQAEYIGVWVEGPFK 425
|
|
| SAM1 |
COG0499 |
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism]; |
8-474 |
0e+00 |
|
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
Pssm-ID: 440265 [Multi-domain] Cd Length: 420 Bit Score: 724.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 8 TAGREYKVRDMAQADFGRMEIELAQVEMPGLMSCIAEFGPAQPLAGANISGSLHMTIQTAVLIETLVALGANVRWCSCNI 87
Cdd:COG0499 1 TAPMDYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 88 FSTQDHAAAAVARDSAAVFAWKGETLEEYWWCTDQMLNWGegsLDIIVDDGGDATLLIHegykaelefaksgaipdpast 167
Cdd:COG0499 81 LSTQDDVAAALAAAGIPVFAWKGETLEEYYWCIEQALDHG---PNIILDDGGDLTLLLH--------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 168 dnaemkcvlkiiaenlktnpKRWQKIVSTCVGVSEETTTGVKRLYEMQKAGELLFPAINVNDSVTKCKFDNLYGCRHSLP 247
Cdd:COG0499 137 --------------------KERPELLAGIIGGTEETTTGVHRLRAMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 248 DGIMRATDVMIASKTCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVDIFITTTGNKD 327
Cdd:COG0499 197 DGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVDPICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 328 IIMVQHMEKMKNNAIVGNIGHFDNEIDMAGLESYPGIKRqNIKPQCDRFEFPDGHGIIMLAEGRLLNLGCATGHPSFVMS 407
Cdd:COG0499 277 VITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKR-EIRPQVDEYTLPDGRRIYLLAEGRLVNLAAATGHPSEVMD 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145350366 408 CSFTNQAIAQLELWNERksGKYEKKVYVLPKHLDEKVAMLHLAKIGVKLTKLSTDQAQYINVPVEGP 474
Cdd:COG0499 356 MSFANQALAQIYLVKNG--DKLEPGVYVLPKELDEEVARLKLEALGVKIDTLTEEQAEYLGSWVEGP 420
|
|
| SAHH |
cd00401 |
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ... |
22-470 |
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: 708.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 22 DFGRMEIELAQVEMPGLMSCIAEFGPAQPLAGANISGSLHMTIQTAVLIETLVALGANVRWCSCNIFSTQDHAAAAVARD 101
Cdd:cd00401 1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 102 SAAVFAWKGETLEEYWWCTDQMLNWGegsLDIIVDDGGDATLLIHEGYKAELEfaksgaipdpastdnaemkcvlkiiae 181
Cdd:cd00401 81 GIPVFAWKGETEEEYWWCIEQALDHG---PNLIIDDGGDLTHLLHTKRPDLLK--------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 182 nlktnpkrwqkivsTCVGVSEETTTGVKRLYEMQKAGELLFPAINVNDSVTKCKFDNLYGCRHSLPDGIMRATDVMIASK 261
Cdd:cd00401 131 --------------KIIGGSEETTTGVHRLRAMEKEGKLLFPAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 262 TCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVDIFITTTGNKDIIMVQHMEKMKNNA 341
Cdd:cd00401 197 VVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMDGFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 342 IVGNIGHFDNEIDMAGLESYpGIKRQNIKPQCDRFEFPDGHGIIMLAEGRLLNLGCATGHPSFVMSCSFTNQAIAQLELW 421
Cdd:cd00401 277 ILCNAGHFDVEIDVAALEEL-AVEKREIRPQVDEYTLPDGRRIILLAEGRLVNLACATGHPSFVMDMSFANQALAQIELW 355
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 145350366 422 NERksGKYEKKVYVLPKHLDEKVAMLHLAKIGVKLTKLSTDQAQYINVP 470
Cdd:cd00401 356 KNR--DKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQAEYLGSW 402
|
|
| ahcY |
TIGR00936 |
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ... |
22-474 |
0e+00 |
|
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: 558.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 22 DFGRMEIELAQVEMPGLMSCIAEFGPAQPLAGANISGSLHMTIQTAVLIETLVALGANVRWCSCNIFSTQDHAAAAVARD 101
Cdd:TIGR00936 1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAALAKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 102 S-AAVFAWKGETLEEYWWCTDQMLnwgEGSLDIIVDDGGDATLLIHEgykaelefaksgaipdpastdnaemkcvlkiia 180
Cdd:TIGR00936 81 AgIPVFAWRGETNEEYYWAIEQVL---DHEPNIIIDDGADLIFLLHT--------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 181 enlktnpkRWQKIVSTCVGVSEETTTGVKRLYEMQKAGELLFPAINVNDSVTKCKFDNLYGCRHSLPDGIMRATDVMIAS 260
Cdd:TIGR00936 125 --------ERPELLEKIIGGSEETTTGVIRLRAMEAEGVLKFPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 261 KTCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVDIFITTTGNKDIIMVQHMEKMKNN 340
Cdd:TIGR00936 197 KTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAMDGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 341 AIVGNIGHFDNEIDMAGLESYpGIKRQNIKPQCDRFEFPDGHGIIMLAEGRLLNLGCATGHPSFVMSCSFTNQAIAQLEL 420
Cdd:TIGR00936 277 AIVANIGHFDVEIDVKALEEL-AVEKVNVRPQVDEYILKDGRRIYLLAEGRLVNLAAAEGHPSEVMDMSFANQALAAEYL 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 145350366 421 WNERksGKYEKKVYVLPKHLDEKVAMLHLAKIGVKLTKLSTDQAQYINVPVEGP 474
Cdd:TIGR00936 356 WKNH--DKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQKEYLGSWEEGT 407
|
|
| AdoHcyase_NAD |
pfam00670 |
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
238-400 |
2.91e-95 |
|
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
Pssm-ID: 395543 [Multi-domain] Cd Length: 162 Bit Score: 285.01 E-value: 2.91e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 238 NLYGCRHSLPDGIMRATDVMIASKTCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVD 317
Cdd:pfam00670 1 NLYGCRESLIDGIKRATDVMIAGKVAVVCGYGDVGKGCAASLKGQGARVIVTEIDPICALQAAMEGFQVVTLEEVVDKAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 318 IFITTTGNKDIIMVQHMEKMKNNAIVGNIGHFDNEIDMAGLESYpGIKRQNIKPQCDRFEFPDGHGIIMLAEGRLLNLGC 397
Cdd:pfam00670 81 IFVTTTGNKDIITGEHMAKMKNDAIVCNIGHFDNEIDVAWLEAN-GKKKENIKPQVDRYTLPDGKHIILLAEGRLVNLGC 159
|
...
gi 145350366 398 ATG 400
Cdd:pfam00670 160 ATG 162
|
|
| AdoHcyase_NAD |
smart00997 |
S-adenosyl-L-homocysteine hydrolase, NAD binding domain; |
238-400 |
4.18e-85 |
|
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
Pssm-ID: 198065 [Multi-domain] Cd Length: 162 Bit Score: 258.92 E-value: 4.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 238 NLYGCRHSLPDGIMRATDVMIASKTCWVAGYGDVGKGSAAALKAAGARVIVSEIDPICALQAAMEGYQVAPIEDVVDQVD 317
Cdd:smart00997 1 NRYGTGESLLDGILRATNVLLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPIRALEAAMDGFEVMKMEEAAKRAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 318 IFITTTGNKDIIMVQHMEKMKNNAIVGNIGHFDNEIDMAGLESYPgIKRQNIKPQCDRFEFPDGHGIIMLAEGRLLNLGC 397
Cdd:smart00997 81 IFVTATGNKDVITREHFRAMKDGAILANAGHFDVEIDVAALEELA-VEKREVRPQVDEYTLPDGKRIYLLAEGRLVNLAA 159
|
...
gi 145350366 398 ATG 400
Cdd:smart00997 160 ATG 162
|
|
| FDH_GDH_like |
cd12154 |
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ... |
56-420 |
1.73e-40 |
|
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: 147.76 E-value: 1.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 56 ISGSLHMTIQTA------VLIETLVALGANVRWCSCNIFSTQDHAAAAVardsaavfawkgetleeYWWCTDQMLNWGEG 129
Cdd:cd12154 1 IAGPKEIKNEEFrvglspSVVATLVEAGHEVRVETGAGIGAGFADQAYV-----------------QAGAIVVTLAKALW 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 130 SLDIIVDDGGDATllihegykaelefaksgaipdpastdnaemkcvlKIIAENLKTNPKRwqkivstcvGVSEETTTGVK 209
Cdd:cd12154 64 SLDVVLKVKEPLT----------------------------------NAEYALIQKLGDR---------LLFTYTIGADH 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 210 RLYEMQkAGELLFPAINVNDSVTKCKFDNLYGCRHSLPDGIMRATDV----------MIASKTCWVAGYGDVGKGSAAAL 279
Cdd:cd12154 101 RDLTEA-LARAGLTAIAVEGVELPLLTSNSIGAGELSVQFIARFLEVqqpgrlggapDVAGKTVVVVGAGVVGKEAAQML 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145350366 280 KAAGARVIVSEIDPICALQAAMEG-YQVAPIEDVVDQVDIFITTTGNKDIIM-----VQHMEKMKNNAIVGNIGHFDNEI 353
Cdd:cd12154 180 RGLGAQVLITDINVEALEQLEELGgKNVEELEEALAEADVIVTTTLLPGKRAgilvpEELVEQMKPGSVIVNVAVGAVGC 259
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145350366 354 DMAgLESYPgikrqnikpqcdrfeFPDGHGIIMLAEGRLLNLGCATGHPSFVMSCSFTNQAIAQLEL 420
Cdd:cd12154 260 VQA-LHTQL---------------LEEGHGVVHYGDVNMPGPGCAMGVPWDATLRLAANTLPALVKL 310
|
|
| |
