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Conserved domains on  [gi|505003523|ref|WP_015190625|]
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adenosylhomocysteinase [Gloeocapsa sp. PCC 7428]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
5-425 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


:

Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 746.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   5 STKPKYEIKDLALAATGRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADAILIASNP 84
Cdd:COG0499    1 TAPMDYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  85 LSTQDDVAASLVADhDIPVFAIKGEDNETYHRHVQIALDHRPNVIIDDGSDVVATLIQQRQHQIADIIGTTEETTTGIVR 164
Cdd:COG0499   81 LSTQDDVAAALAAA-GIPVFAWKGETLEEYYWCIEQALDHGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 165 LKAMFRDGVLTFPAMNVNDADTKHFFDNRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTE 244
Cdd:COG0499  160 LRAMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 245 IDPVRAIEAVMDGFRVLPMSEAAPEGDLFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSLGATATEVKQVRN 324
Cdd:COG0499  240 VDPICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRP 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 325 FTQEYRMPNGKSVVVLGEGRLINLAAAEGHPSAVMDMSFANQALACEYLVKNKGSLEPGIHSIPTEVDQEIARLKLQAMG 404
Cdd:COG0499  320 QVDEYTLPDGRRIYLLAEGRLVNLAAATGHPSEVMDMSFANQALAQIYLVKNGDKLEPGVYVLPKELDEEVARLKLEALG 399

                        410       420
                 ....*....|....*....|.
gi 505003523 405 INIDSLTAEQEEYINSWTAGT 425
Cdd:COG0499  400 VKIDTLTEEQAEYLGSWVEGP 420
 
Name Accession Description Interval E-value
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
5-425 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 746.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   5 STKPKYEIKDLALAATGRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADAILIASNP 84
Cdd:COG0499    1 TAPMDYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  85 LSTQDDVAASLVADhDIPVFAIKGEDNETYHRHVQIALDHRPNVIIDDGSDVVATLIQQRQHQIADIIGTTEETTTGIVR 164
Cdd:COG0499   81 LSTQDDVAAALAAA-GIPVFAWKGETLEEYYWCIEQALDHGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 165 LKAMFRDGVLTFPAMNVNDADTKHFFDNRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTE 244
Cdd:COG0499  160 LRAMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 245 IDPVRAIEAVMDGFRVLPMSEAAPEGDLFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSLGATATEVKQVRN 324
Cdd:COG0499  240 VDPICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRP 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 325 FTQEYRMPNGKSVVVLGEGRLINLAAAEGHPSAVMDMSFANQALACEYLVKNKGSLEPGIHSIPTEVDQEIARLKLQAMG 404
Cdd:COG0499  320 QVDEYTLPDGRRIYLLAEGRLVNLAAATGHPSEVMDMSFANQALAQIYLVKNGDKLEPGVYVLPKELDEEVARLKLEALG 399

                        410       420
                 ....*....|....*....|.
gi 505003523 405 INIDSLTAEQEEYINSWTAGT 425
Cdd:COG0499  400 VKIDTLTEEQAEYLGSWVEGP 420
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 3-425 0e+00

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 706.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   3 ATSTKPKYEIKDLALAATGRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADAILIAS 82
Cdd:PRK05476   1 TTATGTDYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  83 NPLSTQDDVAASLVADhDIPVFAIKGEDNETYHRHVQIALD-HRPNVIIDDGSDVVATLIQQRQHQIADIIGTTEETTTG 161
Cdd:PRK05476  81 NPFSTQDDVAAALAAA-GIPVFAWKGETLEEYWECIERALDgHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 162 IVRLKAMFRDGVLTFPAMNVNDADTKHFFDNRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVI 241
Cdd:PRK05476 160 VHRLYAMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 242 VTEIDPVRAIEAVMDGFRVLPMSEAAPEGDLFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSLGATATEVKQ 321
Cdd:PRK05476 240 VTEVDPICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWRE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 322 VRNFTQEYRMPNGKSVVVLGEGRLINLAAAEGHPSAVMDMSFANQALACEYLVKNKGSLEPGIHSIPTEVDQEIARLKLQ 401
Cdd:PRK05476 320 IKPQVDEYTLPDGKRIILLAEGRLVNLGAATGHPSEVMDMSFANQALAQIELFTNRGKLEPGVYVLPKELDEEVARLKLK 399

                        410       420
                 ....*....|....*....|....
gi 505003523 402 AMGINIDSLTAEQEEYINSWTAGT 425
Cdd:PRK05476 400 ALGVKLDELTEEQAEYIGVWVEGP 423
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 19-421 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: 686.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  19 ATGRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADAILIASNPLSTQDDVAASLVAD 98
Cdd:cd00401    1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  99 hDIPVFAIKGEDNETYHRHVQIALDHRPNVIIDDGSDVVATLIQQRQHQIADIIGTTEETTTGIVRLKAMFRDGVLTFPA 178
Cdd:cd00401   81 -GIPVFAWKGETEEEYWWCIEQALDHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLFPA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 179 MNVNDADTKHFFDNRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMDGF 258
Cdd:cd00401  160 IAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMDGF 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 259 RVLPMSEAAPEGDLFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSLGATATEVKQVRNFTQEYRMPNGKSVV 338
Cdd:cd00401  240 EVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRRII 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 339 VLGEGRLINLAAAEGHPSAVMDMSFANQALACEYLVKNKGSLEPGIHSIPTEVDQEIARLKLQAMGINIDSLTAEQEEYI 418
Cdd:cd00401  320 LLAEGRLVNLACATGHPSFVMDMSFANQALAQIELWKNRDKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQAEYL 399


                 ...
gi 505003523 419 NSW 421
Cdd:cd00401  400 GSW 402
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 21-425 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: 673.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   21 GRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADAILIASNPLSTQDDVAASLVADHD 100
Cdd:TIGR00936   3 GRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAALAKGAG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  101 IPVFAIKGEDNETYHRHVQIALDHRPNVIIDDGSDVVATLIQQRQHQIADIIGTTEETTTGIVRLKAMFRDGVLTFPAMN 180
Cdd:TIGR00936  83 IPVFAWRGETNEEYYWAIEQVLDHEPNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLKFPAIN 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  181 VNDADTKHFFDNRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMDGFRV 260
Cdd:TIGR00936 163 VNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAMDGFRV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  261 LPMSEAAPEGDLFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSLGATATEVKQVRNFTQEYRMPNGKSVVVL 340
Cdd:TIGR00936 243 MTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGRRIYLL 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  341 GEGRLINLAAAEGHPSAVMDMSFANQALACEYLVKNKGSLEPGIHSIPTEVDQEIARLKLQAMGINIDSLTAEQEEYINS 420
Cdd:TIGR00936 323 AEGRLVNLAAAEGHPSEVMDMSFANQALAAEYLWKNHDKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQKEYLGS 402


                  ....*
gi 505003523  421 WTAGT 425
Cdd:TIGR00936 403 WEEGT 407
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
12-419 1.71e-147

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 425.80  E-value: 1.71e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523    12 IKDLALAATGRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADAILIASNPLSTQDDV 91
Cdd:smart00996   2 VADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDHA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523    92 AASLVADhDIPVFAIKGEDNETY----HRHVQIALDHRPNVIIDDGSDvvAT-LIQQRQHQIADIIGTTEETTTGIV-RL 165
Cdd:smart00996  82 AAAIAAA-GVPVFAWKGETLEEYwwciEQTLTWPDGWGPNMILDDGGD--ATlLVHKKYPRMLKKIRGVSEETTTGVhRL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   166 KAMFRDGVLTFPAMNVNDADTKHFFDNRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTEI 245
Cdd:smart00996 159 YQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   246 DPVRAIEAVMDGFRVLPMSEAAPEGDLFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSL----GATATEVK- 320
Cdd:smart00996 239 DPICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLrnnpGLKWENIKp 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   321 QVrnftQEYRMPNGKSVVVLGEGRLINLAAAEGHPSAVMDMSFANQALACEYLVKNKGSLEPGIHSIPTEVDQEIARLKL 400
Cdd:smart00996 319 QV----DHITFPDGKRIILLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELFTKPGKYKNGVYVLPKKLDEKVARLHL 394

                          410
                   ....*....|....*....
gi 505003523   401 QAMGINIDSLTAEQEEYIN 419
Cdd:smart00996 395 EKLGAKLTKLTKEQADYIG 413
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
10-419 5.85e-138

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 401.82  E-value: 5.85e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   10 YEIKDLALAATGRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADaILIAS-NPLSTQ 88
Cdd:pfam05221   2 YKVADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAE-VRWAScNIFSTQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   89 DDVAASLVADhDIPVFAIKGEDNETYHRHVQIALDH-----RPNVIIDDGSDvvAT-LIQQRQHQIADIIGTTEETTTGI 162
Cdd:pfam05221  81 DHAAAAIAAA-GVPVFAWKGETLEEYWWCTEQALTWppdggGPNMILDDGGD--ATlLVHKKYPRIAKGIKGVSEETTTG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  163 V-RLKAMFRDGVLTFPAMNVNDADTKHFFDNRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVI 241
Cdd:pfam05221 158 VhRLYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  242 VTEIDPVRAIEAVMDGFRVLPMSEAAPEGDLFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSLGATATEVKQ 321
Cdd:pfam05221 238 VTEIDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNIGHFDNEIDEIVLALLKGVKWV 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  322 VRNFTQ-EYRMPNGKSVVVLGEGRLINLAAAEGHPSAVMDMSFANQALACEYLVKNKGSLEPGIHSIPTEVDQEIARLKL 400
Cdd:pfam05221 318 NIKPQVdDITFPDGKSIIVLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELWTNDKEYENGVYVLPKKLDEKVARLHL 397

                         410
                  ....*....|....*....
gi 505003523  401 QAMGINIDSLTAEQEEYIN 419
Cdd:pfam05221 398 EKLGAKLTELTKEQADYIG 416
 
Name Accession Description Interval E-value
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
5-425 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 746.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   5 STKPKYEIKDLALAATGRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADAILIASNP 84
Cdd:COG0499    1 TAPMDYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  85 LSTQDDVAASLVADhDIPVFAIKGEDNETYHRHVQIALDHRPNVIIDDGSDVVATLIQQRQHQIADIIGTTEETTTGIVR 164
Cdd:COG0499   81 LSTQDDVAAALAAA-GIPVFAWKGETLEEYYWCIEQALDHGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 165 LKAMFRDGVLTFPAMNVNDADTKHFFDNRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTE 244
Cdd:COG0499  160 LRAMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 245 IDPVRAIEAVMDGFRVLPMSEAAPEGDLFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSLGATATEVKQVRN 324
Cdd:COG0499  240 VDPICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRP 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 325 FTQEYRMPNGKSVVVLGEGRLINLAAAEGHPSAVMDMSFANQALACEYLVKNKGSLEPGIHSIPTEVDQEIARLKLQAMG 404
Cdd:COG0499  320 QVDEYTLPDGRRIYLLAEGRLVNLAAATGHPSEVMDMSFANQALAQIYLVKNGDKLEPGVYVLPKELDEEVARLKLEALG 399

                        410       420
                 ....*....|....*....|.
gi 505003523 405 INIDSLTAEQEEYINSWTAGT 425
Cdd:COG0499  400 VKIDTLTEEQAEYLGSWVEGP 420
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 3-425 0e+00

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 706.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   3 ATSTKPKYEIKDLALAATGRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADAILIAS 82
Cdd:PRK05476   1 TTATGTDYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  83 NPLSTQDDVAASLVADhDIPVFAIKGEDNETYHRHVQIALD-HRPNVIIDDGSDVVATLIQQRQHQIADIIGTTEETTTG 161
Cdd:PRK05476  81 NPFSTQDDVAAALAAA-GIPVFAWKGETLEEYWECIERALDgHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 162 IVRLKAMFRDGVLTFPAMNVNDADTKHFFDNRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVI 241
Cdd:PRK05476 160 VHRLYAMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 242 VTEIDPVRAIEAVMDGFRVLPMSEAAPEGDLFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSLGATATEVKQ 321
Cdd:PRK05476 240 VTEVDPICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWRE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 322 VRNFTQEYRMPNGKSVVVLGEGRLINLAAAEGHPSAVMDMSFANQALACEYLVKNKGSLEPGIHSIPTEVDQEIARLKLQ 401
Cdd:PRK05476 320 IKPQVDEYTLPDGKRIILLAEGRLVNLGAATGHPSEVMDMSFANQALAQIELFTNRGKLEPGVYVLPKELDEEVARLKLK 399

                        410       420
                 ....*....|....*....|....
gi 505003523 402 AMGINIDSLTAEQEEYINSWTAGT 425
Cdd:PRK05476 400 ALGVKLDELTEEQAEYIGVWVEGP 423
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 19-421 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: 686.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  19 ATGRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADAILIASNPLSTQDDVAASLVAD 98
Cdd:cd00401    1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  99 hDIPVFAIKGEDNETYHRHVQIALDHRPNVIIDDGSDVVATLIQQRQHQIADIIGTTEETTTGIVRLKAMFRDGVLTFPA 178
Cdd:cd00401   81 -GIPVFAWKGETEEEYWWCIEQALDHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLFPA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 179 MNVNDADTKHFFDNRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMDGF 258
Cdd:cd00401  160 IAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMDGF 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 259 RVLPMSEAAPEGDLFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSLGATATEVKQVRNFTQEYRMPNGKSVV 338
Cdd:cd00401  240 EVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRRII 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 339 VLGEGRLINLAAAEGHPSAVMDMSFANQALACEYLVKNKGSLEPGIHSIPTEVDQEIARLKLQAMGINIDSLTAEQEEYI 418
Cdd:cd00401  320 LLAEGRLVNLACATGHPSFVMDMSFANQALAQIELWKNRDKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQAEYL 399


                 ...
gi 505003523 419 NSW 421
Cdd:cd00401  400 GSW 402
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 21-425 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: 673.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   21 GRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADAILIASNPLSTQDDVAASLVADHD 100
Cdd:TIGR00936   3 GRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAALAKGAG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  101 IPVFAIKGEDNETYHRHVQIALDHRPNVIIDDGSDVVATLIQQRQHQIADIIGTTEETTTGIVRLKAMFRDGVLTFPAMN 180
Cdd:TIGR00936  83 IPVFAWRGETNEEYYWAIEQVLDHEPNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLKFPAIN 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  181 VNDADTKHFFDNRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMDGFRV 260
Cdd:TIGR00936 163 VNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAMDGFRV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  261 LPMSEAAPEGDLFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSLGATATEVKQVRNFTQEYRMPNGKSVVVL 340
Cdd:TIGR00936 243 MTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGRRIYLL 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  341 GEGRLINLAAAEGHPSAVMDMSFANQALACEYLVKNKGSLEPGIHSIPTEVDQEIARLKLQAMGINIDSLTAEQEEYINS 420
Cdd:TIGR00936 323 AEGRLVNLAAAEGHPSEVMDMSFANQALAAEYLWKNHDKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQKEYLGS 402


                  ....*
gi 505003523  421 WTAGT 425
Cdd:TIGR00936 403 WEEGT 407
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
12-419 1.71e-147

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 425.80  E-value: 1.71e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523    12 IKDLALAATGRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADAILIASNPLSTQDDV 91
Cdd:smart00996   2 VADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDHA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523    92 AASLVADhDIPVFAIKGEDNETY----HRHVQIALDHRPNVIIDDGSDvvAT-LIQQRQHQIADIIGTTEETTTGIV-RL 165
Cdd:smart00996  82 AAAIAAA-GVPVFAWKGETLEEYwwciEQTLTWPDGWGPNMILDDGGD--ATlLVHKKYPRMLKKIRGVSEETTTGVhRL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   166 KAMFRDGVLTFPAMNVNDADTKHFFDNRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTEI 245
Cdd:smart00996 159 YQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   246 DPVRAIEAVMDGFRVLPMSEAAPEGDLFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSL----GATATEVK- 320
Cdd:smart00996 239 DPICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLrnnpGLKWENIKp 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   321 QVrnftQEYRMPNGKSVVVLGEGRLINLAAAEGHPSAVMDMSFANQALACEYLVKNKGSLEPGIHSIPTEVDQEIARLKL 400
Cdd:smart00996 319 QV----DHITFPDGKRIILLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELFTKPGKYKNGVYVLPKKLDEKVARLHL 394

                          410
                   ....*....|....*....
gi 505003523   401 QAMGINIDSLTAEQEEYIN 419
Cdd:smart00996 395 EKLGAKLTKLTKEQADYIG 413
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
10-419 5.85e-138

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 401.82  E-value: 5.85e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   10 YEIKDLALAATGRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADaILIAS-NPLSTQ 88
Cdd:pfam05221   2 YKVADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAE-VRWAScNIFSTQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   89 DDVAASLVADhDIPVFAIKGEDNETYHRHVQIALDH-----RPNVIIDDGSDvvAT-LIQQRQHQIADIIGTTEETTTGI 162
Cdd:pfam05221  81 DHAAAAIAAA-GVPVFAWKGETLEEYWWCTEQALTWppdggGPNMILDDGGD--ATlLVHKKYPRIAKGIKGVSEETTTG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  163 V-RLKAMFRDGVLTFPAMNVNDADTKHFFDNRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVI 241
Cdd:pfam05221 158 VhRLYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  242 VTEIDPVRAIEAVMDGFRVLPMSEAAPEGDLFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSLGATATEVKQ 321
Cdd:pfam05221 238 VTEIDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNIGHFDNEIDEIVLALLKGVKWV 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  322 VRNFTQ-EYRMPNGKSVVVLGEGRLINLAAAEGHPSAVMDMSFANQALACEYLVKNKGSLEPGIHSIPTEVDQEIARLKL 400
Cdd:pfam05221 318 NIKPQVdDITFPDGKSIIVLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELWTNDKEYENGVYVLPKKLDEKVARLHL 397

                         410
                  ....*....|....*....
gi 505003523  401 QAMGINIDSLTAEQEEYIN 419
Cdd:pfam05221 398 EKLGAKLTELTKEQADYIG 416
PTZ00075 PTZ00075
Adenosylhomocysteinase; Provisional
 6-419 3.19e-136

Adenosylhomocysteinase; Provisional


Pssm-ID: 240258  Cd Length: 476  Bit Score: 399.03  E-value: 3.19e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   6 TKPKYEIKDLALAATGRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADAILIASNPL 85
Cdd:PTZ00075   1 PMTDYKVKDISLAEFGRKEIELAENEMPGLMALREEYGPSKPLKGARITGCLHMTVQTAVLIETLKALGAEVRWCSCNIF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  86 STQDDVAASLVADHDIPVFAIKGEDNETYHRHVQIALDHR----PNVIIDDGSDvvATLI----------QQRQHQIADI 151
Cdd:PTZ00075  81 STQDHAAAAIAKAGSVPVFAWKGETLEEYWWCTEQALKWPngdgPNLIVDDGGD--ATLLvhegvkaeklYEEKGILPDP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 152 IGTTEETTTGIV---------------------------------RLKAMFRDGVLTFPAMNVNDADTKHFFDNRYGTGQ 198
Cdd:PTZ00075 159 LDPSNEDEKCLLtvlkklltknpdkwtnlvkkivgvseetttgvhRLYKMLKKGELLFPAINVNDSVTKSKFDNIYGCRH 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 199 STLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMDGFRVLPMSEAAPEGDLFITVTG 278
Cdd:PTZ00075 239 SLIDGIFRATDVMIAGKTVVVCGYGDVGKGCAQALRGFGARVVVTEIDPICALQAAMEGYQVVTLEDVVETADIFVTATG 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 279 NKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSL----GATATEVK-QVRNFTqeyrMPNGKSVVVLGEGRLINLAAAEG 353
Cdd:PTZ00075 319 NKDIITLEHMRRMKNNAIVGNIGHFDNEIQVAELeaypGIEIVEIKpQVDRYT----FPDGKGIILLAEGRLVNLGCATG 394

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505003523 354 HPSAVMDMSFANQALACEYLVKNK--GSLEPGIHSIPTEVDQEIARLKLQAMGINIDSLTAEQEEYIN 419
Cdd:PTZ00075 395 HPSFVMSNSFTNQVLAQIELWENRdtGKYPNGVYKLPKELDEKVARLHLKKLGAKLTKLTDKQAEYIG 462
PLN02494 PLN02494
adenosylhomocysteinase
 10-419 2.92e-104

adenosylhomocysteinase


Pssm-ID: 178111 [Multi-domain]  Cd Length: 477  Bit Score: 317.19  E-value: 2.92e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  10 YEIKDLALAATGRQRIEWAGREMPVLRQIRDRFAQEKPLAGIRLVACCHVTTETAHLAIALKAGGADAILIASNPLSTQD 89
Cdd:PLN02494   6 YKVKDMSQADFGRLEIELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNIFSTQD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  90 DVAASLVADhDIPVFAIKGEDNETYHRHVQIALD----HRPNVIIDDGSD------------------------------ 135
Cdd:PLN02494  86 HAAAAIARD-SAAVFAWKGETLQEYWWCTERALDwgpgGGPDLIVDDGGDatllihegvkaeeefekdgtlpdptstdna 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 136 ---VVATLIQQ-------RQHQIADIIGTTEETTTGIV-RLKAMFRDGVLTFPAMNVNDADTKHFFDNRYGTGQSTLDGI 204
Cdd:PLN02494 165 efkIVLTIIKDglkvdpkKYHKMKERLVGVSEETTTGVkRLYQMQKNGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDGL 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 205 IRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMDGFRVLPMSEAAPEGDLFITVTGNKHVIR 284
Cdd:PLN02494 245 MRATDVMIAGKVAVICGYGDVGKGCAAAMKAAGARVIVTEIDPICALQALMEGYQVLTLEDVVSEADIFVTTTGNKDIIM 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 285 AEHFEAMKDGAIVCNSGHFDIEIDLKSLgATATEVKQ--VRNFTQEYRMPNGKS-VVVLGEGRLINLAAAEGHPSAVMDM 361
Cdd:PLN02494 325 VDHMRKMKNNAIVCNIGHFDNEIDMLGL-ETYPGVKRitIKPQTDRWVFPDTGSgIIVLAEGRLMNLGCATGHPSFVMSC 403

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 362 SFANQALACEYLVKNK--GSLEPGIHSIPTEVDQEIARLKLQAMGINIDSLTAEQEEYIN 419
Cdd:PLN02494 404 SFTNQVIAQLELWNEKksGKYEKKVYVLPKHLDEKVAALHLGKLGAKLTKLSKDQADYIN 463
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
192-353 5.42e-101

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


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 297.44  E-value: 5.42e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   192 NRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMDGFRVLPMSEAAPEGD 271
Cdd:smart00997   1 NRYGTGESLLDGILRATNVLLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPIRALEAAMDGFEVMKMEEAAKRAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   272 LFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSLGATATEVKQVRNFTQEYRMPNGKSVVVLGEGRLINLAAA 351
Cdd:smart00997  81 IFVTATGNKDVITREHFRAMKDGAILANAGHFDVEIDVAALEELAVEKREVRPQVDEYTLPDGKRIYLLAEGRLVNLAAA 160


                   ..
gi 505003523   352 EG 353
Cdd:smart00997 161 TG 162
AdoHcyase_NAD pfam00670
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
192-353 1.46e-67

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


Pssm-ID: 395543 [Multi-domain]  Cd Length: 162  Bit Score: 212.21  E-value: 1.46e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  192 NRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMDGFRVLPMSEAAPEGD 271
Cdd:pfam00670   1 NLYGCRESLIDGIKRATDVMIAGKVAVVCGYGDVGKGCAASLKGQGARVIVTEIDPICALQAAMEGFQVVTLEEVVDKAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  272 LFITVTGNKHVIRAEHFEAMKDGAIVCNSGHFDIEIDLKSLGATATEVKQVRNFTQEYRMPNGKSVVVLGEGRLINLAAA 351
Cdd:pfam00670  81 IFVTTTGNKDIITGEHMAKMKNDAIVCNIGHFDNEIDVAWLEANGKKKENIKPQVDRYTLPDGKHIILLAEGRLVNLGCA 160


                  ..
gi 505003523  352 EG 353
Cdd:pfam00670 161 TG 162
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 177-366 1.57e-29

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: 116.95  E-value: 1.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 177 PAMNVNDADTKHFFDNRYGTGQSTLDGIIRATNLL----------LAGKTVVVAGYGWCGKGTALRARGMGANVIVTEID 246
Cdd:cd12154  113 TAIAVEGVELPLLTSNSIGAGELSVQFIARFLEVQqpgrlggapdVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDIN 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 247 PVRAIEAVMDG-FRVLPMSEAAPEGDLFITVTG----NKHVIR-AEHFEAMKDGAIVCNSGHFDIEIDLKSLgatatevk 320
Cdd:cd12154  193 VEALEQLEELGgKNVEELEEALAEADVIVTTTLlpgkRAGILVpEELVEQMKPGSVIVNVAVGAVGCVQALH-------- 264

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 505003523 321 qvrnftqEYRMPNGKSVVVLGEGRLINLAAAEGHPSAVMDMSFANQ 366
Cdd:cd12154  265 -------TQLLEEGHGVVHYGDVNMPGPGCAMGVPWDATLRLAANT 303
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 212-301 2.09e-11

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: 62.13  E-value: 2.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMDGFRVLPMSEAAPEGDlFITVT-----GNKHVIRAE 286
Cdd:pfam02826  34 LSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSLDELLAESD-VVSLHlpltpETRHLINAE 112

                          90
                  ....*....|....*
gi 505003523  287 HFEAMKDGAIVCNSG 301
Cdd:pfam02826 113 RLALMKPGAILINTA 127
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 212-301 2.57e-10

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: 61.36  E-value: 2.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTeiDP-VRAIEAVMDGFR-VLPMSEAAPEGDlFITVT-----GNKHVIR 284
Cdd:COG0111  138 LRGKTVGIVGLGRIGRAVARRLRAFGMRVLAY--DPsPKPEEAADLGVGlVDSLDELLAEAD-VVSLHlpltpETRGLIG 214

                         90
                 ....*....|....*..
gi 505003523 285 AEHFEAMKDGAIVCNSG 301
Cdd:COG0111  215 AEELAAMKPGAILINTA 231
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
 212-299 2.59e-09

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: 58.20  E-value: 2.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTeiDP-VRAIEAVMDGFRVLPMSEAAPEGDlFITV-----TGNKHVIRA 285
Cdd:cd12173  136 LRGKTLGIVGLGRIGREVARRARAFGMKVLAY--DPyISAERAAAGGVELVSLDELLAEAD-FISLhtpltPETRGLINA 212

                         90
                 ....*....|....
gi 505003523 286 EHFEAMKDGAIVCN 299
Cdd:cd12173  213 EELAKMKPGAILIN 226
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
 212-299 3.39e-09

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: 57.55  E-value: 3.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAiEAVMDGFRVLPMSEAAPEGDlFIT--VT---GNKHVIRAE 286
Cdd:cd05303  137 LRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDE-QAVELGVKTVSLEELLKNSD-FISlhVPltpETKHMINKK 214

                         90
                 ....*....|...
gi 505003523 287 HFEAMKDGAIVCN 299
Cdd:cd05303  215 ELELMKDGAIIIN 227
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 212-299 5.45e-09

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: 57.20  E-value: 5.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMDGFRVLPMSEAAPEGD---LFITVT-GNKHVIRAEH 287
Cdd:cd12175  140 LSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFRDPEAEEKDLGVRYVELDELLAESDvvsLHVPLTpETRHLIGAEE 219

                         90
                 ....*....|..
gi 505003523 288 FEAMKDGAIVCN 299
Cdd:cd12175  220 LAAMKPGAILIN 231
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
 212-299 6.64e-09

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: 57.02  E-value: 6.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTeiDPVRAIEAVMDGFRVLPMSEAAPEGDlFITVT-----GNKHVIRAE 286
Cdd:COG1052  141 LSGKTLGIIGLGRIGQAVARRAKGFGMKVLYY--DRSPKPEVAELGAEYVSLDELLAESD-IVSLHcpltpETRHLINAE 217

                         90
                 ....*....|...
gi 505003523 287 HFEAMKDGAIVCN 299
Cdd:COG1052  218 ELALMKPGAILIN 230
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 212-299 8.71e-09

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: 56.48  E-value: 8.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTeiDPVRAIEAVMD-GFRVLPMSEAAPEGDlFITV-----TGNKHVIRA 285
Cdd:cd05198  138 LEGKTVGIVGLGRIGQRVAKRLQAFGMKVLYY--DRTRKPEPEEDlGFRVVSLDELLAQSD-VVVLhlpltPETRHLINE 214

                         90
                 ....*....|....
gi 505003523 286 EHFEAMKDGAIVCN 299
Cdd:cd05198  215 EELALMKPGAVLVN 228
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 212-299 1.08e-08

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: 56.03  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVteIDPVRAIEAV----MDGFRVLPMSEAAPEGDlFITV-----TGNKHV 282
Cdd:cd12174  133 LRGKTLGVIGLGNIGRLVANAALALGMKVIG--YDPYLSVEAAwklsVEVQRVTSLEELLATAD-YITLhvpltDETRGL 209

                         90
                 ....*....|....*..
gi 505003523 283 IRAEHFEAMKDGAIVCN 299
Cdd:cd12174  210 INAELLAKMKPGAILLN 226
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 206-299 1.61e-08

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: 55.57  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 206 RATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAiEAVMDGFRVLPMSEAAPEGDlFITVT-----GNK 280
Cdd:cd12172  134 RPVGTELYGKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDEE-FAKEHGVEFVSLEELLKESD-FISLHlpltpETR 211

                         90
                 ....*....|....*....
gi 505003523 281 HVIRAEHFEAMKDGAIVCN 299
Cdd:cd12172  212 HLINAAELALMKPGAILIN 230
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 212-301 6.21e-08

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: 54.06  E-value: 6.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPvRAIEAVMDgfRVLPMS---EAAPEGDlFITVT-----GNKHVI 283
Cdd:cd05300  132 LAGKTVLIVGLGDIGREIARRAKAFGMRVIGVRRSG-RPAPPVVD--EVYTPDeldELLPEAD-YVVNAlpltpETRGLF 207

                         90
                 ....*....|....*...
gi 505003523 284 RAEHFEAMKDGAIVCNSG 301
Cdd:cd05300  208 NAERFAAMKPGAVLINVG 225
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 188-312 8.39e-08

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: 53.40  E-value: 8.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 188 HFFDNRYGTGQSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVmdgfRVLPMS--- 264
Cdd:cd12165  111 VEYDNDLRRGIWHGRAGEEPESKELRGKTVGILGYGHIGREIARLLKAFGMRVIGVSRSPKEDEGAD----FVGTLSdld 186

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 505003523 265 EAAPEGDL-FITVTGNKH---VIRAEHFEAMKDGAIVCNSGHFDIeIDLKSL 312
Cdd:cd12165  187 EALEQADVvVVALPLTKQtrgLIGAAELAAMKPGAILVNVGRGPV-VDEEAL 237
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 212-300 4.12e-07

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: 51.38  E-value: 4.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTeiDP-VRAIEAVMDGFRVLPMSEAAPEGDlFIT----VT-GNKHVIRA 285
Cdd:cd12171  145 LRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVY--DPyVDPEKIEADGVKKVSLEELLKRSD-VVSlharLTpETRGMIGA 221

                         90
                 ....*....|....*
gi 505003523 286 EHFEAMKDGAIVCNS 300
Cdd:cd12171  222 EEFALMKPTAYFINT 236
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 216-308 4.73e-07

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 49.04  E-value: 4.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523   216 TVVVAGYGWCGKGTALRARGMGANVIVTEIDPV--RAIEAVMDG-FRVL-----PMSEAAPEGDLFIT---VTGNK--HV 282
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPArlRQLESLLGArFTTLysqaeLLEEAVKEADLVIGavlIPGAKapKL 101

                           90       100
                   ....*....|....*....|....*.
gi 505003523   283 IRAEHFEAMKDGAIVCnsghfDIEID 308
Cdd:smart01002 102 VTREMVKSMKPGSVIV-----DVAAD 122
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 212-301 1.40e-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: 240639 [Multi-domain]  Cd Length: 307  Bit Score: 49.76  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPvraieAVMDGFRVLPMSEAAPEGDlFITV-----TGNKHVIRAE 286
Cdd:cd12162  145 LAGKTLGIIGYGNIGQAVARIARAFGMKVLFAERKG-----APPLREGYVSLDELLAQSD-VISLhcpltPETRNLINAE 218

                         90
                 ....*....|....*
gi 505003523 287 HFEAMKDGAIVCNSG 301
Cdd:cd12162  219 ELAKMKPGAILINTA 233
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 212-301 3.37e-06

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-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: 240659  Cd Length: 328  Bit Score: 48.59  E-value: 3.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVteIDPVRAIEAVMDGFRVLPMSEAAPEGDlFIT-----VTGNKHVIRAE 286
Cdd:cd12183  142 LHGKTVGVIGTGKIGQAFARILKGFGCRVLA--YDPYPNPELAKLGVEYVDLDELLAESD-IISlhcplTPETHHLINAE 218

                         90
                 ....*....|....*
gi 505003523 287 HFEAMKDGAIVCNSG 301
Cdd:cd12183  219 TIAKMKDGVMLINTS 233
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 212-312 5.21e-06

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: 240655 [Multi-domain]  Cd Length: 317  Bit Score: 48.00  E-value: 5.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTeiDPVR---AIEAVMdGFRVLPMSEAAPEGDlFIT-----VTGNKHVI 283
Cdd:cd12178  142 LAGKTLGIIGMGRIGQAVARRAKAFGMKILYY--NRHRlseETEKEL-GATYVDLDELLKESD-FVSlhapyTPETHHLI 217

                         90       100
                 ....*....|....*....|....*....
gi 505003523 284 RAEHFEAMKDGAIVCNSGHFDIeIDLKSL 312
Cdd:cd12178  218 DAAAFKLMKPTAYLINAARGPL-VDEKAL 245
IlvN pfam07991
Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase ...
 211-297 8.60e-06

Acetohydroxy acid isomeroreductase, NADPH-binding domain; Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. This N-terminal region of the enzyme carries the binding-site for NADPH. The active-site for enzymatic activity lies in the C-terminal part, IlvC, pfam01450.


Pssm-ID: 285265  Cd Length: 165  Bit Score: 45.61  E-value: 8.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  211 LLAGKTVVVAGYGWCGKGTALRARGMGANVIV-TEIDPVRAIEAVMDGFRVLPMSEAAPEGDLFITVTGN---KHVIRAE 286
Cdd:pfam07991   1 VLKGKKIAVIGYGSQGHAHALNLRDSGVNVIVgLREGSKSWKKAKKDGFEVYTVAEAAKKADVIMILIPDevqAEVYEEE 80

                          90
                  ....*....|.
gi 505003523  287 HFEAMKDGAIV 297
Cdd:pfam07991  81 IAPNLKEGAAL 91
IlvC COG0059
Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and ...
 211-272 1.15e-05

Ketol-acid reductoisomerase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Ketol-acid reductoisomerase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439829 [Multi-domain]  Cd Length: 328  Bit Score: 46.98  E-value: 1.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505003523 211 LLAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIE-AVMDGFRVLPMSEAAPEGDL 272
Cdd:COG0059   14 LLKGKKVAVIGYGSQGHAHALNLRDSGVDVVVGLREGSKSWKkAEEDGFEVMTVAEAAKRADV 76
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
 212-299 1.19e-05

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: 46.88  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMdGFRVLPMSEAAPEGDlFIT--VTGNK---HVIRAE 286
Cdd:cd12187  137 LAGKTLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEELAERL-GFRYVSLEELLQESD-IISlhVPYTPqthHLINRE 214

                         90
                 ....*....|...
gi 505003523 287 HFEAMKDGAIVCN 299
Cdd:cd12187  215 NFALMKPGAVLIN 227
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 212-301 2.68e-05

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240643 [Multi-domain]  Cd Length: 300  Bit Score: 45.66  E-value: 2.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGwcGKGTALRARGMGANVIVT-------EIDPVRAIEAvmdgfrvLPmsEAAPEGDLFITVT----GNK 280
Cdd:cd12166  130 LADRRVLIVGYG--SIGRAIERRLAPFEVRVTrvartarPGEQVHGIDE-------LP--ALLPEADVVVLIVpltdETR 198

                         90       100
                 ....*....|....*....|.
gi 505003523 281 HVIRAEHFEAMKDGAIVCNSG 301
Cdd:cd12166  199 GLVDAEFLARMPDGALLVNVA 219
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
 206-301 4.05e-05

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: 45.27  E-value: 4.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 206 RATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVI--------VTEIDPVRAIEAvmdgfrvlpMSEAAPEGDLFITV- 276
Cdd:cd12155  127 DSSLLELYGKTILFLGTGSIGQEIAKRLKAFGMKVIgvntsgrdVEYFDKCYPLEE---------LDEVLKEADIVVNVl 197

                         90       100
                 ....*....|....*....|....*...
gi 505003523 277 ---TGNKHVIRAEHFEAMKDGAIVCNSG 301
Cdd:cd12155  198 pltEETHHLFDEAFFEQMKKGALFINVG 225
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 212-301 4.17e-05

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: 45.37  E-value: 4.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTeiDPVRAIEAVMDGFRVLPMSEAAPEGDLfIT-----VTGNKHVIRAE 286
Cdd:cd01619  141 LEDQTVGVVGTGKIGRAVAQRAKGFGMKVIAY--DPFRNPELEDKGVKYVSLEELFKNSDI-ISlhvplTPENHHMINEE 217

                         90
                 ....*....|....*
gi 505003523 287 HFEAMKDGAIVCNSG 301
Cdd:cd01619  218 AFKLMKKGVIIINTA 232
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
 214-308 7.33e-05

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: 240653  Cd Length: 304  Bit Score: 44.49  E-value: 7.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 214 GKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMdgfRVLPMSEAAPEGDlFIT--VTG---NKHVIRAEHF 288
Cdd:cd12176  140 GKTLGIIGYGHIGSQLSVLAEALGMRVIFYDIAEKLPLGNAR---QVSSLEELLAEAD-FVTlhVPAtpsTKNMIGAEEI 215

                         90       100
                 ....*....|....*....|.
gi 505003523 289 EAMKDGAIVCN-SGHFDIEID 308
Cdd:cd12176  216 AQMKKGAILINaSRGTVVDID 236
PRK13403 PRK13403
ketol-acid reductoisomerase; Provisional
 211-305 1.32e-04

ketol-acid reductoisomerase; Provisional


Pssm-ID: 106361 [Multi-domain]  Cd Length: 335  Bit Score: 43.58  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 211 LLAGKTVVVAGYGWCGKGTALRARGMGANVIVTeIDPVRAIE-AVMDGFRVLPMSEA---APEGDLFITVTGNKHVIRAE 286
Cdd:PRK13403  13 LLQGKTVAVIGYGSQGHAQAQNLRDSGVEVVVG-VRPGKSFEvAKADGFEVMSVSEAvrtAQVVQMLLPDEQQAHVYKAE 91

                         90
                 ....*....|....*....
gi 505003523 287 HFEAMKDGAIVCNSGHFDI 305
Cdd:PRK13403  92 VEENLREGQMLLFSHGFNI 110
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
 209-301 1.67e-04

D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which 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: 240635 [Multi-domain]  Cd Length: 343  Bit Score: 43.29  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 209 NLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTeiDPVRAIEAVMDGFRvlPMSEAAPEGDLF-----ITVTGN---K 280
Cdd:cd12158  110 GFSLKGKTVGIVGVGNVGSRLARRLEALGMNVLLC--DPPRAEAEGDPGFV--SLEELLAEADIItlhvpLTRDGEhptY 185

                         90       100
                 ....*....|....*....|.
gi 505003523 281 HVIRAEHFEAMKDGAIVCNSG 301
Cdd:cd12158  186 HLLDEDFLAALKPGQILINAS 206
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 212-300 1.80e-04

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: 43.08  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTA-LRARGMGANVIVTeiDP-VRAIEAVMDGFRVLPMSEAAPEGD---LFITVT-GNKHVIRA 285
Cdd:cd12177  145 LSGKTVGIIGYGNIGSRVAeILKEGFNAKVLAY--DPyVSEEVIKKKGAKPVSLEELLAESDiisLHAPLTeETYHMINE 222

                         90
                 ....*....|....*
gi 505003523 286 EHFEAMKDGAIVCNS 300
Cdd:cd12177  223 KAFSKMKKGVILVNT 237
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 193-297 1.82e-04

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 42.48  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523  193 RYGTGQSTLDGIIRATnllLAGKtVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRA--IEAVMDGFRVLPM------- 263
Cdd:pfam01262  11 KFFGGRGTLAGGVPGV---APAK-VLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLeqLESILGAKFVETLysqaeli 86

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 505003523  264 SEAAPEGDLFIT---VTGNK--HVIRAEHFEAMKDGAIV 297
Cdd:pfam01262  87 AEAVKEADLVIGtalIPGAKapKLVTREMVKSMKPGSVI 125
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 210-308 1.97e-04

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 43.16  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 210 LLLAGKT------VVVAGYGWCGKGTALRARGMGANVIVTEIDP--VRAIEAVMDGfRVLPM-------SEAAPEGDLFI 274
Cdd:cd05305  158 VLLGGVPgvppakVVILGAGVVGENAARVALGLGAEVTVLDINLerLRYLDDIFGG-RVTTLysnpanlEEALKEADLVI 236

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 505003523 275 T---VTGNK--HVIRAEHFEAMKDGA-IVcnsghfDIEID 308
Cdd:cd05305  237 GavlIPGAKapKLVTEEMVKTMKPGSvIV------DVAID 270
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 188-301 3.10e-04

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: 42.55  E-value: 3.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 188 HFFDNRYGTGqSTLDGIIRATNLLLAGKTVVVAGYGWCGKGTALRARGMGANVIVTeiDP-VRAIEAVMDGFRVLPMSEA 266
Cdd:cd12167  125 PRFAAAYRAG-RDWGWPTRRGGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVY--DPyLPAAEAAALGVELVSLDEL 201

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 505003523 267 APEGDLFITVTG----NKHVIRAEHFEAMKDGAIVCNSG 301
Cdd:cd12167  202 LARSDVVSLHAPltpeTRGMIDARLLALMRDGATFINTA 240
PLN02928 PLN02928
oxidoreductase family protein
 212-312 4.42e-04

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 41.98  E-value: 4.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVT------EIDPVRAIEAVMDGFRV------LPMSEAAPEGDLFITV--- 276
Cdd:PLN02928 157 LFGKTVFILGYGAIGIELAKRLRPFGVKLLATrrswtsEPEDGLLIPNGDVDDLVdekgghEDIYEFAGEADIVVLCctl 236

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 505003523 277 -TGNKHVIRAEHFEAMKDGAIVCN---SGHFDIEIDLKSL 312
Cdd:PLN02928 237 tKETAGIVNDEFLSSMKKGALLVNiarGGLLDYDAVLAAL 276
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
 212-301 1.01e-03

Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. 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.


Pssm-ID: 240634 [Multi-domain]  Cd Length: 318  Bit Score: 40.73  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMDGFRVLPMSEAAPEGDLFITVT----GNKHVIRAEH 287
Cdd:cd12157  142 LDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHPLDQAEEQALNLRRVELDELLESSDFLVLALpltpDTLHLINAEA 221

                         90
                 ....*....|....
gi 505003523 288 FEAMKDGAIVCNSG 301
Cdd:cd12157  222 LAKMKPGALLVNPC 235
PRK05479 PRK05479
ketol-acid reductoisomerase; Provisional
 211-272 1.08e-03

ketol-acid reductoisomerase; Provisional


Pssm-ID: 235491 [Multi-domain]  Cd Length: 330  Bit Score: 40.84  E-value: 1.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505003523 211 LLAGKTVVVAGYGWCGKGTALRARGMGANVIVTeidpVR-----AIEAVMDGFRVLPMSEAAPEGDL 272
Cdd:PRK05479  14 LIKGKKVAIIGYGSQGHAHALNLRDSGVDVVVG----LRegsksWKKAEADGFEVLTVAEAAKWADV 76
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
 212-299 1.67e-03

D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase, HPR) catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. In humans, HPR deficiency causes primary hyperoxaluria type 2, characterized by over-excretion of L-glycerate and oxalate in the urine, possibly due to an imbalance in competition with L-lactate dehydrogenase, another formate dehydrogenase (FDH)-like enzyme. GDH, like FDH and other members of the D-specific hydroxyacid dehydrogenase family that also includes L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase, typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form, despite often low sequence identity. 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: 240626 [Multi-domain]  Cd Length: 309  Bit Score: 40.07  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMDGFRVlPMSEAAPEGD-LFITVTGN---KHVIRAEH 287
Cdd:cd05301  142 LHGKTLGIVGMGRIGQAVARRAKGFGMKILYHNRSRKPEAEEELGARYV-SLDELLAESDfVSLHCPLTpetRHLINAER 220

                         90
                 ....*....|..
gi 505003523 288 FEAMKDGAIVCN 299
Cdd:cd05301  221 LALMKPTAILIN 232
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
212-322 5.38e-03

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 38.53  E-value: 5.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 212 LAGKTVVVAGYGWCGKGTALRARGMGANVIVTEIdPVRAIEAvmdgfRVLPMSEAAPEGDlFITV-----TGNKHVIRAE 286
Cdd:PRK06487 146 LEGKTLGLLGHGELGGAVARLAEAFGMRVLIGQL-PGRPARP-----DRLPLDELLPQVD-ALTLhcpltEHTRHLIGAR 218

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 505003523 287 HFEAMKDGAIVCNSGHFDI--EIDL------KSLGATATEVKQV 322
Cdd:PRK06487 219 ELALMKPGALLINTARGGLvdEQALadalrsGHLGGAATDVLSV 262
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
 216-301 7.80e-03

(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic domains; (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. HGDH is a member of the D-2-hydroxyacid NAD(+)-dependent dehydrogenase family; 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: 240660  Cd Length: 330  Bit Score: 38.04  E-value: 7.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505003523 216 TVVVAGYGWCGKGTALRARGMGANVIVTEIDPVRAIEAVMDgfrVLPMSEAAPEGDLfITV------TGNKHVIRAEHFE 289
Cdd:cd12184  147 TVGIIGTGRIGLTAAKLFKGLGAKVIGYDIYPSDAAKDVVT---FVSLDELLKKSDI-ISLhvpyikGKNDKLINKEFIS 222

                         90
                 ....*....|..
gi 505003523 290 AMKDGAIVCNSG 301
Cdd:cd12184  223 KMKDGAILINTA 234
 
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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