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Conserved domains on  [gi|1015218415|ref|NP_001309015|]
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adenosylhomocysteinase isoform 3 [Homo sapiens]

Protein Classification

adenosylhomocysteinase family protein( domain architecture ID 11278876)

adenosylhomocysteinase family protein such as adenosylhomocysteinase that catalyzes the hydrolysis of S-adenosyl-L-homocysteine to form L-homocysteine and adenosine and may play a key role in regulating the intracellular concentration of adenosylhomocysteine

CATH:  3.40.50.1480|3.40.50.720
Gene Ontology:  GO:0033353|GO:0070403
PubMed:  715439|11325033|30945211|25704928|31869345
SCOP:  4000098

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
10-433 0e+00

S-adenosyl-L-homocysteine hydrolase;


:

Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 886.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415   10 CEADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDH 89
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415   90 AAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYFKDG-PLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYK 168
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPDGwGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  169 MMANGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDP 248
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  249 INALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENA-VEKVNIKPQV 327
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNNPgLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  328 DRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVK 407
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELFTKPGKYKNGVYVLPKKLDEKVARLHLEKLGAK 400

                          410       420
                   ....*....|....*....|....*.
gi 1015218415  408 LTKLTEKQAQYLGMSCDGPFKPDHYR 433
Cdd:smart00996 401 LTKLTKEQADYIGVPVEGPFKPDHYR 426
 
Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
10-433 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 886.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415   10 CEADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDH 89
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415   90 AAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYFKDG-PLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYK 168
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPDGwGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  169 MMANGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDP 248
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  249 INALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENA-VEKVNIKPQV 327
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNNPgLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  328 DRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVK 407
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELFTKPGKYKNGVYVLPKKLDEKVARLHLEKLGAK 400

                          410       420
                   ....*....|....*....|....*.
gi 1015218415  408 LTKLTEKQAQYLGMSCDGPFKPDHYR 433
Cdd:smart00996 401 LTKLTKEQADYIGVPVEGPFKPDHYR 426
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
12-433 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 878.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  12 ADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAA 91
Cdd:pfam05221   5 ADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDHAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  92 AAIAKAGIPVYAWKGETDEEYLWCIEQTLYFKD--GPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKM 169
Cdd:pfam05221  85 AAIAAAGVPVFAWKGETLEEYWWCTEQALTWPPdgGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHRLYQM 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 170 MANGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPI 249
Cdd:pfam05221 165 AKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDPI 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 250 NALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDV-KWLNENAVEKVNIKPQVD 328
Cdd:pfam05221 245 CALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNIGHFDNEIDEiVLALLKGVKWVNIKPQVD 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 329 RYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKL 408
Cdd:pfam05221 325 DITFPDGKSIIVLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELWTNDKEYENGVYVLPKKLDEKVARLHLEKLGAKL 404

                         410       420
                  ....*....|....*....|....*
gi 1015218415 409 TKLTEKQAQYLGMSCDGPFKPDHYR 433
Cdd:pfam05221 405 TELTKEQADYIGVPVEGPFKPDHYR 429
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 18-420 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: 819.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  18 AWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKA 97
Cdd:cd00401     1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  98 GIPVYAWKGETDEEYLWCIEQTLyfkDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKV 177
Cdd:cd00401    81 GIPVFAWKGETEEEYWWCIEQAL---DHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 178 PAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAME 257
Cdd:cd00401   158 PAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMD 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 258 GYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRR 337
Cdd:cd00401   238 GFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 338 IILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQ 417
Cdd:cd00401   318 IILLAEGRLVNLACATGHPSFVMDMSFANQALAQIELWKNRDKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQAE 397


                  ...
gi 1015218415 418 YLG 420
Cdd:cd00401   398 YLG 400
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
12-426 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 818.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  12 ADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAA 91
Cdd:COG0499     9 KDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNPLSTQDDVA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  92 AAIAKAGIPVYAWKGETDEEYLWCIEQTLyfkDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMA 171
Cdd:COG0499    89 AALAAAGIPVFAWKGETLEEYYWCIEQAL---DHGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHRLRAMAK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 172 NGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINA 251
Cdd:COG0499   166 EGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVDPICA 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 252 LQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYR 331
Cdd:COG0499   246 LEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRPQVDEYT 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 332 LKNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKL 411
Cdd:COG0499   326 LPDGRRIYLLAEGRLVNLAAATGHPSEVMDMSFANQALAQIYLVKNGDKLEPGVYVLPKELDEEVARLKLEALGVKIDTL 405

                         410
                  ....*....|....*
gi 1015218415 412 TEKQAQYLGMSCDGP 426
Cdd:COG0499   406 TEEQAEYLGSWVEGP 420
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 12-428 0e+00

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 811.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  12 ADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAA 91
Cdd:PRK05476   11 ADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNPFSTQDDVA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  92 AAIAKAGIPVYAWKGETDEEYLWCIEQTLyfKDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMA 171
Cdd:PRK05476   91 AALAAAGIPVFAWKGETLEEYWECIERAL--DGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGVHRLYAMAK 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 172 NGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINA 251
Cdd:PRK05476  169 DGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVDPICA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 252 LQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYR 331
Cdd:PRK05476  249 LQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKPQVDEYT 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 332 LKNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKL 411
Cdd:PRK05476  329 LPDGKRIILLAEGRLVNLGAATGHPSEVMDMSFANQALAQIELFTNRGKLEPGVYVLPKELDEEVARLKLKALGVKLDEL 408

                         410
                  ....*....|....*..
gi 1015218415 412 TEKQAQYLGMSCDGPFK 428
Cdd:PRK05476  409 TEEQAEYIGVWVEGPFK 425
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 18-426 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: 739.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  18 AWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAAA-AIAK 96
Cdd:TIGR00936   1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAaLAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  97 AGIPVYAWKGETDEEYLWCIEQTLyfkDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILK 176
Cdd:TIGR00936  81 AGIPVFAWRGETNEEYYWAIEQVL---DHEPNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 177 VPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAM 256
Cdd:TIGR00936 158 FPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 257 EGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGR 336
Cdd:TIGR00936 238 DGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 337 RIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQA 416
Cdd:TIGR00936 318 RIYLLAEGRLVNLAAAEGHPSEVMDMSFANQALAAEYLWKNHDKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQK 397

                         410
                  ....*....|
gi 1015218415 417 QYLGMSCDGP 426
Cdd:TIGR00936 398 EYLGSWEEGT 407
 
Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
10-433 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 886.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415   10 CEADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDH 89
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415   90 AAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYFKDG-PLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYK 168
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPDGwGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  169 MMANGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDP 248
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  249 INALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENA-VEKVNIKPQV 327
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNNPgLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  328 DRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVK 407
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELFTKPGKYKNGVYVLPKKLDEKVARLHLEKLGAK 400

                          410       420
                   ....*....|....*....|....*.
gi 1015218415  408 LTKLTEKQAQYLGMSCDGPFKPDHYR 433
Cdd:smart00996 401 LTKLTKEQADYIGVPVEGPFKPDHYR 426
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
12-433 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 878.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  12 ADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAA 91
Cdd:pfam05221   5 ADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDHAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  92 AAIAKAGIPVYAWKGETDEEYLWCIEQTLYFKD--GPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKM 169
Cdd:pfam05221  85 AAIAAAGVPVFAWKGETLEEYWWCTEQALTWPPdgGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHRLYQM 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 170 MANGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPI 249
Cdd:pfam05221 165 AKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDPI 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 250 NALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDV-KWLNENAVEKVNIKPQVD 328
Cdd:pfam05221 245 CALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNIGHFDNEIDEiVLALLKGVKWVNIKPQVD 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 329 RYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKL 408
Cdd:pfam05221 325 DITFPDGKSIIVLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELWTNDKEYENGVYVLPKKLDEKVARLHLEKLGAKL 404

                         410       420
                  ....*....|....*....|....*
gi 1015218415 409 TKLTEKQAQYLGMSCDGPFKPDHYR 433
Cdd:pfam05221 405 TELTKEQADYIGVPVEGPFKPDHYR 429
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 18-420 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: 819.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  18 AWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKA 97
Cdd:cd00401     1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  98 GIPVYAWKGETDEEYLWCIEQTLyfkDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKV 177
Cdd:cd00401    81 GIPVFAWKGETEEEYWWCIEQAL---DHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 178 PAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAME 257
Cdd:cd00401   158 PAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMD 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 258 GYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRR 337
Cdd:cd00401   238 GFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 338 IILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQ 417
Cdd:cd00401   318 IILLAEGRLVNLACATGHPSFVMDMSFANQALAQIELWKNRDKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQAE 397


                  ...
gi 1015218415 418 YLG 420
Cdd:cd00401   398 YLG 400
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
12-426 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 818.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  12 ADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAA 91
Cdd:COG0499     9 KDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNPLSTQDDVA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  92 AAIAKAGIPVYAWKGETDEEYLWCIEQTLyfkDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMA 171
Cdd:COG0499    89 AALAAAGIPVFAWKGETLEEYYWCIEQAL---DHGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHRLRAMAK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 172 NGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINA 251
Cdd:COG0499   166 EGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVDPICA 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 252 LQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYR 331
Cdd:COG0499   246 LEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRPQVDEYT 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 332 LKNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKL 411
Cdd:COG0499   326 LPDGRRIYLLAEGRLVNLAAATGHPSEVMDMSFANQALAQIYLVKNGDKLEPGVYVLPKELDEEVARLKLEALGVKIDTL 405

                         410
                  ....*....|....*
gi 1015218415 412 TEKQAQYLGMSCDGP 426
Cdd:COG0499   406 TEEQAEYLGSWVEGP 420
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 12-428 0e+00

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 811.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  12 ADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAA 91
Cdd:PRK05476   11 ADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNPFSTQDDVA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  92 AAIAKAGIPVYAWKGETDEEYLWCIEQTLyfKDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMA 171
Cdd:PRK05476   91 AALAAAGIPVFAWKGETLEEYWECIERAL--DGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGVHRLYAMAK 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 172 NGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINA 251
Cdd:PRK05476  169 DGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVDPICA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 252 LQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYR 331
Cdd:PRK05476  249 LQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKPQVDEYT 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 332 LKNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKL 411
Cdd:PRK05476  329 LPDGKRIILLAEGRLVNLGAATGHPSEVMDMSFANQALAQIELFTNRGKLEPGVYVLPKELDEEVARLKLKALGVKLDEL 408

                         410
                  ....*....|....*..
gi 1015218415 412 TEKQAQYLGMSCDGPFK 428
Cdd:PRK05476  409 TEEQAEYIGVWVEGPFK 425
PTZ00075 PTZ00075
Adenosylhomocysteinase; Provisional
 12-434 0e+00

Adenosylhomocysteinase; Provisional


Pssm-ID: 240258  Cd Length: 476  Bit Score: 769.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  12 ADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAA 91
Cdd:PTZ00075    8 KDISLAEFGRKEIELAENEMPGLMALREEYGPSKPLKGARITGCLHMTVQTAVLIETLKALGAEVRWCSCNIFSTQDHAA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  92 AAIAKAG-IPVYAWKGETDEEYLWCIEQTLYFKDG-PLNMILDDGGDLTNLIHT-------------------------- 143
Cdd:PTZ00075   88 AAIAKAGsVPVFAWKGETLEEYWWCTEQALKWPNGdGPNLIVDDGGDATLLVHEgvkaeklyeekgilpdpldpsnedek 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 144 ---------------KYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRA 208
Cdd:PTZ00075  168 clltvlkklltknpdKWTNLVKKIVGVSEETTTGVHRLYKMLKKGELLFPAINVNDSVTKSKFDNIYGCRHSLIDGIFRA 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 209 TDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRH 288
Cdd:PTZ00075  248 TDVMIAGKTVVVCGYGDVGKGCAQALRGFGARVVVTEIDPICALQAAMEGYQVVTLEDVVETADIFVTATGNKDIITLEH 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 289 FEQMKDDAIVCNIGHFDVEIDVKWL-NENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQ 367
Cdd:PTZ00075  328 MRRMKNNAIVGNIGHFDNEIQVAELeAYPGIEIVEIKPQVDRYTFPDGKGIILLAEGRLVNLGCATGHPSFVMSNSFTNQ 407

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015218415 368 VMAQIELWTHPD--KYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMSCDGPFKPDHYRY 434
Cdd:PTZ00075  408 VLAQIELWENRDtgKYPNGVYKLPKELDEKVARLHLKKLGAKLTKLTDKQAEYIGVPVDGPYKSDHYRY 476
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 18-426 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: 739.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  18 AWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAAA-AIAK 96
Cdd:TIGR00936   1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAaLAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  97 AGIPVYAWKGETDEEYLWCIEQTLyfkDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILK 176
Cdd:TIGR00936  81 AGIPVFAWRGETNEEYYWAIEQVL---DHEPNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 177 VPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAM 256
Cdd:TIGR00936 158 FPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 257 EGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGR 336
Cdd:TIGR00936 238 DGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 337 RIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQA 416
Cdd:TIGR00936 318 RIYLLAEGRLVNLAAAEGHPSEVMDMSFANQALAAEYLWKNHDKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQK 397

                         410
                  ....*....|
gi 1015218415 417 QYLGMSCDGP 426
Cdd:TIGR00936 398 EYLGSWEEGT 407
PLN02494 PLN02494
adenosylhomocysteinase
 12-434 0e+00

adenosylhomocysteinase


Pssm-ID: 178111 [Multi-domain]  Cd Length: 477  Bit Score: 600.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  12 ADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAA 91
Cdd:PLN02494    9 KDMSQADFGRLEIELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNIFSTQDHAA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  92 AAIAKAGIPVYAWKGETDEEYLWCIEQTL-YFKDGPLNMILDDGGDLTNLIH---------------------------- 142
Cdd:PLN02494   89 AAIARDSAAVFAWKGETLQEYWWCTERALdWGPGGGPDLIVDDGGDATLLIHegvkaeeefekdgtlpdptstdnaefki 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 143 -------------TKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRAT 209
Cdd:PLN02494  169 vltiikdglkvdpKKYHKMKERLVGVSEETTTGVKRLYQMQKNGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDGLMRAT 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 210 DVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHF 289
Cdd:PLN02494  249 DVMIAGKVAVICGYGDVGKGCAAAMKAAGARVIVTEIDPICALQALMEGYQVLTLEDVVSEADIFVTTTGNKDIIMVDHM 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 290 EQMKDDAIVCNIGHFDVEIDVKWLNE-NAVEKVNIKPQVDRYRLKN-GRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQ 367
Cdd:PLN02494  329 RKMKNNAIVCNIGHFDNEIDMLGLETyPGVKRITIKPQTDRWVFPDtGSGIIVLAEGRLMNLGCATGHPSFVMSCSFTNQ 408

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015218415 368 VMAQIELWTHPD--KYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMSCDGPFKPDHYRY 434
Cdd:PLN02494  409 VIAQLELWNEKKsgKYEKKVYVLPKHLDEKVAALHLGKLGAKLTKLSKDQADYINVPVEGPYKPAHYRY 477
AdoHcyase_NAD pfam00670
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
193-354 4.72e-112

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 395543 [Multi-domain]  Cd Length: 162  Bit Score: 325.85  E-value: 4.72e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 193 NLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACQEGN 272
Cdd:pfam00670   1 NLYGCRESLIDGIKRATDVMIAGKVAVVCGYGDVGKGCAASLKGQGARVIVTEIDPICALQAAMEGFQVVTLEEVVDKAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 273 IFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCA 352
Cdd:pfam00670  81 IFVTTTGNKDIITGEHMAKMKNDAIVCNIGHFDNEIDVAWLEANGKKKENIKPQVDRYTLPDGKHIILLAEGRLVNLGCA 160


                  ..
gi 1015218415 353 MG 354
Cdd:pfam00670 161 TG 162
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
193-354 2.80e-108

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 316.31  E-value: 2.80e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  193 NLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACQEGN 272
Cdd:smart00997   1 NRYGTGESLLDGILRATNVLLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPIRALEAAMDGFEVMKMEEAAKRAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  273 IFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCA 352
Cdd:smart00997  81 IFVTATGNKDVITREHFRAMKDGAILANAGHFDVEIDVAALEELAVEKREVRPQVDEYTLPDGKRIYLLAEGRLVNLAAA 160


                   ..
gi 1015218415  353 MG 354
Cdd:smart00997 161 TG 162
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 52-374 1.21e-101

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: 305.31  E-value: 1.21e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415  52 IAGCLHMTVETA------VLIETLVTLGAEVQWSSCNIFSTQDHaaaaiakagipvyawkgETDEEYLWCIEQTLYFKDG 125
Cdd:cd12154     1 IAGPKEIKNEEFrvglspSVVATLVEAGHEVRVETGAGIGAGFA-----------------DQAYVQAGAIVVTLAKALW 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 126 PLNMILDDGGDLTNlIHTKYPQLLPgIRGISEETTTGVHNLYKMmANGILKVPAINVNDSVTKSKFDNLYGCRESLIDGI 205
Cdd:cd12154    64 SLDVVLKVKEPLTN-AEYALIQKLG-DRLLFTYTIGADHRDLTE-ALARAGLTAIAVEGVELPLLTSNSIGAGELSVQFI 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 206 KRATDV----------MIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEG-YEVTTMDEACQEGNIF 274
Cdd:cd12154   141 ARFLEVqqpgrlggapDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGgKNVEELEEALAEADVI 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 275 VTTTGCIDIILGR-----HFEQMKDDAIVCNIGHFDVEIDVKWLnenavekvnikpqvdRYRLKNGRRIILLAEGRLVNL 349
Cdd:cd12154   221 VTTTLLPGKRAGIlvpeeLVEQMKPGSVIVNVAVGAVGCVQALH---------------TQLLEEGHGVVHYGDVNMPGP 285

                         330       340
                  ....*....|....*....|....*
gi 1015218415 350 GCAMGHPSFVMSNSFTNQVMAQIEL 374
Cdd:cd12154   286 GCAMGVPWDATLRLAANTLPALVKL 310
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 212-300 2.50e-09

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: 240648 [Multi-domain]  Cd Length: 310  Bit Score: 58.32  E-value: 2.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 212 MIAGKVAVVAGYGDVGKGCAQALRGFGARVIITeiDP-INALQAAMEGYEVTTMDEACQEGNIfVT--------TTGCID 282
Cdd:cd12171   144 ELRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVY--DPyVDPEKIEADGVKKVSLEELLKRSDV-VSlharltpeTRGMIG 220

                          90
                  ....*....|....*...
gi 1015218415 283 iilGRHFEQMKDDAIVCN 300
Cdd:cd12171   221 ---AEEFALMKPTAYFIN 235
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 211-302 7.20e-09

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: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 56.87  E-value: 7.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 211 VMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPiNALQAAMEGYEVTTMDEACQEGNIFV-------TTTGCIDi 283
Cdd:cd12165   133 KELRGKTVGILGYGHIGREIARLLKAFGMRVIGVSRSP-KEDEGADFVGTLSDLDEALEQADVVVvalpltkQTRGLIG- 210

                          90
                  ....*....|....*....
gi 1015218415 284 ilGRHFEQMKDDAIVCNIG 302
Cdd:cd12165   211 --AAELAAMKPGAILVNVG 227
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 213-302 9.60e-09

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439881 [Multi-domain]  Cd Length: 314  Bit Score: 56.36  E-value: 9.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 213 IAGKVAVVAGYGDVGKGCAQALRGFGARVIITeiDP-INALQAAMEGYE-VTTMDEACQEGNIFV-------TTTGCIDi 283
Cdd:COG0111   138 LRGKTVGIVGLGRIGRAVARRLRAFGMRVLAY--DPsPKPEEAADLGVGlVDSLDELLAEADVVSlhlpltpETRGLIG- 214

                          90
                  ....*....|....*....
gi 1015218415 284 ilGRHFEQMKDDAIVCNIG 302
Cdd:COG0111   215 --AEELAAMKPGAILINTA 231
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 211-302 1.61e-07

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 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: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 52.58  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 211 VMIAGK-VAVVaGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACQEGNIFV-------TTTGCID 282
Cdd:cd12175   138 RELSGKtVGIV-GLGNIGRAVARRLRGFGVEVIYYDRFRDPEAEEKDLGVRYVELDELLAESDVVSlhvpltpETRHLIG 216

                          90       100
                  ....*....|....*....|
gi 1015218415 283 iilGRHFEQMKDDAIVCNIG 302
Cdd:cd12175   217 ---AEELAAMKPGAILINTA 233
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 213-302 1.68e-07

Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 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. 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. 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 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. 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, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240622 [Multi-domain]  Cd Length: 302  Bit Score: 52.63  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 213 IAGKVAVVAGYGDVGKGCAQALRGFGARVIITeiDPINAL-QAAMEGYEVTTMDEACQEGNIFV-------TTTGCIDii 284
Cdd:cd05198   138 LEGKTVGIVGLGRIGQRVAKRLQAFGMKVLYY--DRTRKPePEEDLGFRVVSLDELLAQSDVVVlhlpltpETRHLIN-- 213

                          90
                  ....*....|....*...
gi 1015218415 285 lGRHFEQMKDDAIVCNIG 302
Cdd:cd05198   214 -EEELALMKPGAVLVNTA 230
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 213-302 2.19e-07

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: 52.14  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 213 IAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACQEGNIFV-------TTTGCIDiil 285
Cdd:cd05300   132 LAGKTVLIVGLGDIGREIARRAKAFGMRVIGVRRSGRPAPPVVDEVYTPDELDELLPEADYVVnalpltpETRGLFN--- 208

                          90
                  ....*....|....*..
gi 1015218415 286 GRHFEQMKDDAIVCNIG 302
Cdd:cd05300   209 AERFAAMKPGAVLINVG 225
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 213-302 3.15e-07

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: 50.19  E-value: 3.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 213 IAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACQEGNIFV-------TTTGCIDiil 285
Cdd:pfam02826  34 LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSLDELLAESDVVSlhlpltpETRHLIN--- 110

                          90
                  ....*....|....*..
gi 1015218415 286 GRHFEQMKDDAIVCNIG 302
Cdd:pfam02826 111 AERLALMKPGAILINTA 127
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
 213-300 3.35e-07

Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. 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.


Pssm-ID: 240650 [Multi-domain]  Cd Length: 304  Bit Score: 51.65  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 213 IAGKVAVVAGYGDVGKGCAQALRGFGARVIITeiDP-INALQAAMEGYEVTTMDEACQEGNiFVT--------TTGCIDi 283
Cdd:cd12173   136 LRGKTLGIVGLGRIGREVARRARAFGMKVLAY--DPyISAERAAAGGVELVSLDELLAEAD-FISlhtpltpeTRGLIN- 211

                          90
                  ....*....|....*..
gi 1015218415 284 ilGRHFEQMKDDAIVCN 300
Cdd:cd12173   212 --AEELAKMKPGAILIN 226
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 213-300 1.18e-06

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as 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. Many, not all, members of this family are dimeric.


Pssm-ID: 240649 [Multi-domain]  Cd Length: 306  Bit Score: 50.18  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 213 IAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPiNALQAAMEGYEVTTMDEACQEGNiFVT--------TTGCIDii 284
Cdd:cd12172   140 LYGKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPYP-DEEFAKEHGVEFVSLEELLKESD-FISlhlpltpeTRHLIN-- 215

                          90
                  ....*....|....*.
gi 1015218415 285 lGRHFEQMKDDAIVCN 300
Cdd:cd12172   216 -AAELALMKPGAILIN 230
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 216-300 1.69e-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: 240644 [Multi-domain]  Cd Length: 330  Bit Score: 49.48  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 216 KVAVVaGYGDVGKGCAQALRGFGARVIITeiDP-INALQAAMEGYEVTTMDEACQEGNIFVT-------TTGCIDiilGR 287
Cdd:cd12167   152 TVGIV-GFGRIGRAVVELLRPFGLRVLVY--DPyLPAAEAAALGVELVSLDELLARSDVVSLhapltpeTRGMID---AR 225

                          90
                  ....*....|...
gi 1015218415 288 HFEQMKDDAIVCN 300
Cdd:cd12167   226 LLALMRDGATFIN 238
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
 213-302 2.59e-05

Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, Coenzyme transport and metabolism, General function prediction only]; Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440672 [Multi-domain]  Cd Length: 316  Bit Score: 45.85  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 213 IAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAmeGYEVTTMDEACQEGNIFV-------TTTGCIDiil 285
Cdd:COG1052   141 LSGKTLGIIGLGRIGQAVARRAKGFGMKVLYYDRSPKPEVAEL--GAEYVSLDELLAESDIVSlhcpltpETRHLIN--- 215

                          90
                  ....*....|....*..
gi 1015218415 286 GRHFEQMKDDAIVCNIG 302
Cdd:COG1052   216 AEELALMKPGAILINTA 232
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
 216-300 5.82e-05

D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenases family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. 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.


Pssm-ID: 240662  Cd Length: 329  Bit Score: 44.83  E-value: 5.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 216 KVAVVaGYGDVGKGCAQALRGFGARVIITEIDPINALQAamEGYEVTTMDEACQEGNI-------FVTTTGCIDIILgrh 288
Cdd:cd12186   147 TVGII-GTGRIGSAAAKIFKGFGAKVIAYDPYPNPELEK--FLLYYDSLEDLLKQADIislhvplTKENHHLINAEA--- 220

                          90
                  ....*....|..
gi 1015218415 289 FEQMKDDAIVCN 300
Cdd:cd12186   221 FAKMKDGAILVN 232
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
 206-317 2.31e-04

Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate dehydrogenase (PGDH) catalyzes the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDH comes in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. 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.


Pssm-ID: 240628 [Multi-domain]  Cd Length: 301  Bit Score: 42.91  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 206 KRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINAlQAAMEGYEVTTMDEACQEGN---IFVTTTGCID 282
Cdd:cd05303   130 KKYKGIELRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDE-QAVELGVKTVSLEELLKNSDfisLHVPLTPETK 208

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1015218415 283 IILGR-HFEQMKDDAIVCNIGHFDVeidvkwLNENA 317
Cdd:cd05303   209 HMINKkELELMKDGAIIINTSRGGV------IDEEA 238
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
 213-302 8.15e-04

Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate Dehydrogenase (PGDH) catalyzes the NAD-dependent conversion of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first step in serine biosynthesis. Over-expression of PGDH has been implicated as supporting proliferation of certain breast cancers, while PGDH deficiency is linked to defects in mammalian central nervous system development. PGDH is a member of the 2-hydroxyacid dehydrogenase family, 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/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: 240632 [Multi-domain]  Cd Length: 314  Bit Score: 41.03  E-value: 8.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 213 IAGKVAVVAGYGDVGKGCAQALRGFGARVIiteidPINALQAAMEG----YEVTTMDEACQEGNIFV-------TTTGCI 281
Cdd:cd12155   133 LYGKTILFLGTGSIGQEIAKRLKAFGMKVI-----GVNTSGRDVEYfdkcYPLEELDEVLKEADIVVnvlplteETHHLF 207

                          90       100
                  ....*....|....*....|.
gi 1015218415 282 DiilGRHFEQMKDDAIVCNIG 302
Cdd:cd12155   208 D---EAFFEQMKKGALFINVG 225
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
215-352 9.49e-04

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 40.78  E-value: 9.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 215 GKVAVVAG-YGDVGKGCAQALRGFGARVIITEIDPINALQAAME-GYEV--TTMDEACQEG-----NIFVTTTGCIDIil 285
Cdd:PRK07067    6 GKVALLTGaASGIGEAVAERYLAEGARVVIADIKPARARLAALEiGPAAiaVSLDVTRQDSidrivAAAVERFGGIDI-- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 286 grhfeqmkddaIVCNIGHFDVE--IDVKWLNENAVEKVNIK------PQVDRYRLKNGR--RIILLAE--GR----LVNL 349
Cdd:PRK07067   84 -----------LFNNAALFDMApiLDISRDSYDRLFAVNVKglfflmQAVARHMVEQGRggKIINMASqaGRrgeaLVSH 152


                  ...
gi 1015218415 350 GCA 352
Cdd:PRK07067  153 YCA 155
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
214-284 9.70e-04

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 41.37  E-value: 9.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 214 AGKVAVVAG-YGDVGKGCAQALRGFGARVIITEIDPINALQAAME-----GYEVTTMD----EACQEG-NIFVTTTGCID 282
Cdd:PRK08324  421 AGKVALVTGaAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAElggpdRALGVACDvtdeAAVQAAfEEAALAFGGVD 500


                  ..
gi 1015218415 283 II 284
Cdd:PRK08324  501 IV 502
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 212-300 1.10e-03

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as 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. Many, not all, members of this family are dimeric.


Pssm-ID: 240651 [Multi-domain]  Cd Length: 305  Bit Score: 40.62  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 212 MIAGKVAVVAGYGDVGKGCAQALRGFGARVII--TEIDPINALQAAMEGYEVTTMDEACQEGNIF-------VTTTGCID 282
Cdd:cd12174   132 ELRGKTLGVIGLGNIGRLVANAALALGMKVIGydPYLSVEAAWKLSVEVQRVTSLEELLATADYItlhvpltDETRGLIN 211

                          90
                  ....*....|....*...
gi 1015218415 283 iilGRHFEQMKDDAIVCN 300
Cdd:cd12174   212 ---AELLAKMKPGAILLN 226
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
215-302 1.54e-03

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 40.59  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 215 GKVAVVAGYGDVGKGCAQALRGFGARVIIT--EIDPINALQAAMEGY-----EVTT-MDEACQEGNIFVTTTGCIDIILG 286
Cdd:COG5322   152 ATVAVVGATGSIGSVCARLLAREVKRLTLVarNLERLEELAEEILRNpggkvTITTdIDEALREADIVVTVTSAVGAIID 231

                          90
                  ....*....|....*.
gi 1015218415 287 rhFEQMKDDAIVCNIG 302
Cdd:COG5322   232 --PEDLKPGAVVCDVA 245
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
218-261 1.66e-03

Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];


Pssm-ID: 440839 [Multi-domain]  Cd Length: 279  Bit Score: 40.10  E-value: 1.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1015218415 218 AVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEGYEV 261
Cdd:COG1226   127 VIIAGFGRVGQIVARLLRAEGIPFVVIDLDPERVEELRRFGIKV 170
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 213-255 2.22e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 39.61  E-value: 2.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1015218415 213 IAGKVAVVAGYGD-VGKGCAQALRGFGARVIITEIDPINALQAA 255
Cdd:PRK08265    4 LAGKVAIVTGGATlIGAAVARALVAAGARVAIVDIDADNGAAVA 47
PRK06196 PRK06196
oxidoreductase; Provisional
 208-265 2.61e-03

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 39.67  E-value: 2.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015218415 208 ATDVM----IAGKVAVVAG-YGDVGKGCAQALRGFGARVIITEIDPINALQAA--MEGYEVTTMD 265
Cdd:PRK06196   15 AEEVLaghdLSGKTAIVTGgYSGLGLETTRALAQAGAHVIVPARRPDVAREALagIDGVEVVMLD 79
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 213-300 3.81e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 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: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 39.23  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 213 IAGKVAVVAGYGDVGKGCAQALR-GFGARVIITeiDP-INALQAAMEGYEVTTMDEACQEGNIFV----TTTGCIDIILG 286
Cdd:cd12177   145 LSGKTVGIIGYGNIGSRVAEILKeGFNAKVLAY--DPyVSEEVIKKKGAKPVSLEELLAESDIISlhapLTEETYHMINE 222

                          90
                  ....*....|....
gi 1015218415 287 RHFEQMKDDAIVCN 300
Cdd:cd12177   223 KAFSKMKKGVILVN 236
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 213-302 3.98e-03

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: 240639 [Multi-domain]  Cd Length: 307  Bit Score: 38.97  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 213 IAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPinalqAAMEGYEVTTMDEACQEGNIfVT--------TTGCIDIi 284
Cdd:cd12162   145 LAGKTLGIIGYGNIGQAVARIARAFGMKVLFAERKG-----APPLREGYVSLDELLAQSDV-ISlhcpltpeTRNLINA- 217

                          90
                  ....*....|....*...
gi 1015218415 285 lgRHFEQMKDDAIVCNIG 302
Cdd:cd12162   218 --EELAKMKPGAILINTA 233
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 213-302 6.42e-03

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. D-HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. Similar to the structurally distinct L-HicDH, D-HicDH exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. 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.


Pssm-ID: 240620 [Multi-domain]  Cd Length: 323  Bit Score: 38.44  E-value: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 213 IAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAamEGYEVTTMDEACQEGNIFvtTTGCIDIILGRH---- 288
Cdd:cd01619   141 LEDQTVGVVGTGKIGRAVAQRAKGFGMKVIAYDPFRNPELED--KGVKYVSLEELFKNSDII--SLHVPLTPENHHmine 216

                          90
                  ....*....|....*.
gi 1015218415 289 --FEQMKDDAIVCNIG 302
Cdd:cd01619   217 eaFKLMKKGVIIINTA 232
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
 214-300 6.86e-03

D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. 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.


Pssm-ID: 240663 [Multi-domain]  Cd Length: 329  Bit Score: 38.41  E-value: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015218415 214 AGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALqAAMEGYEVTTMDEACQEGNIfVT-----TTGCIDIILGRH 288
Cdd:cd12187   138 AGKTLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEEL-AERLGFRYVSLEELLQESDI-ISlhvpyTPQTHHLINREN 215

                          90
                  ....*....|..
gi 1015218415 289 FEQMKDDAIVCN 300
Cdd:cd12187   216 FALMKPGAVLIN 227
 
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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