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Conserved domains on  [gi|45553387|ref|NP_996222|]
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adenosylhomocysteinase like 2, isoform C [Drosophila melanogaster]

Protein Classification

adenosylhomocysteinase family protein( domain architecture ID 11278876)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
69-491 0e+00

S-adenosyl-L-homocysteine hydrolase;


:

Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 800.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387     69 CVKSISKSAFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNIYSTQNA 148
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    149 VAAALAEAGIPIFAWRGETEEEFWWCLDRAIY-SDGWQPNLILDDGGDATHLMLKKYPDYFKAIRGIVEESVTGVHRLYM 227
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTwPDGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    228 LSKGGKLTVPAINVNDSVTKNKFDTFYTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDP 307
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    308 ICALQAAMDGFRVVRLNEVIRTVDVVVTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGLHT-PELTWERVRSQV 386
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    387 DHIRWPDGRMIILLAEGRLVNLSCSTISSFVVSVASST-QALALIELFSAPGRYKSDVYLLPKKMDEYVASLHLATFDAH 465
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATGHPSFVMSNSFTnQVLAQIELFTKPGKYKNGVYVLPKKLDEKVARLHLEKLGAK 400

                          410       420
                   ....*....|....*....|....*.
gi 45553387    466 LTELTDEQSKFMGLNKAGPFKANYYR 491
Cdd:smart00996 401 LTKLTKEQADYIGVPVEGPFKPDHYR 426
 
Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
69-491 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 800.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387     69 CVKSISKSAFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNIYSTQNA 148
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    149 VAAALAEAGIPIFAWRGETEEEFWWCLDRAIY-SDGWQPNLILDDGGDATHLMLKKYPDYFKAIRGIVEESVTGVHRLYM 227
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTwPDGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    228 LSKGGKLTVPAINVNDSVTKNKFDTFYTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDP 307
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    308 ICALQAAMDGFRVVRLNEVIRTVDVVVTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGLHT-PELTWERVRSQV 386
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    387 DHIRWPDGRMIILLAEGRLVNLSCSTISSFVVSVASST-QALALIELFSAPGRYKSDVYLLPKKMDEYVASLHLATFDAH 465
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATGHPSFVMSNSFTnQVLAQIELFTKPGKYKNGVYVLPKKLDEKVARLHLEKLGAK 400

                          410       420
                   ....*....|....*....|....*.
gi 45553387    466 LTELTDEQSKFMGLNKAGPFKANYYR 491
Cdd:smart00996 401 LTKLTKEQADYIGVPVEGPFKPDHYR 426
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
67-491 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 758.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    67 DFCVKSISKSAFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNIYSTQ 146
Cdd:pfam05221   1 DYKVADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   147 NAVAAALAEAGIPIFAWRGETEEEFWWCLDRAIY--SDGWQPNLILDDGGDATHLMLKKYPDYFKAIRGIVEESVTGVHR 224
Cdd:pfam05221  81 DHAAAAIAAAGVPVFAWKGETLEEYWWCTEQALTwpPDGGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   225 LYMLSKGGKLTVPAINVNDSVTKNKFDTFYTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYVTE 304
Cdd:pfam05221 161 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   305 VDPICALQAAMDGFRVVRLNEVIRTVDVVVTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGL--HTPELTWERV 382
Cdd:pfam05221 241 IDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNIGHFDNEIDEIVLalLKGVKWVNIK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   383 RsQVDHIRWPDGRMIILLAEGRLVNLSCST--------IssfvvsvASSTQALALIELFSAPGRYKSDVYLLPKKMDEYV 454
Cdd:pfam05221 321 P-QVDDITFPDGKSIIVLAEGRLVNLGCATghpsfvmsN-------SFTNQVLAQIELWTNDKEYENGVYVLPKKLDEKV 392

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 45553387   455 ASLHLATFDAHLTELTDEQSKFMGLNKAGPFKANYYR 491
Cdd:pfam05221 393 ARLHLEKLGAKLTELTKEQADYIGVPVEGPFKPDHYR 429
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 77-480 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: 692.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  77 AFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNIYSTQNAVAAALAEA 156
Cdd:cd00401   1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 157 GIPIFAWRGETEEEFWWCLDRAIysdGWQPNLILDDGGDATHLMLKKYPDYFKAIRGIVEESVTGVHRLYMLSKGGKLTV 236
Cdd:cd00401  81 GIPVFAWKGETEEEYWWCIEQAL---DHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 237 PAINVNDSVTKNKFDTFYTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAAMD 316
Cdd:cd00401 158 PAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMD 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 317 GFRVVRLNEVIRTVDVVVTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGLHTPELTWERVRSQVDHIRWPDGRM 396
Cdd:cd00401 238 GFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRR 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 397 IILLAEGRLVNLSCST-----IssfvVSVASSTQALALIELFSAPGRYKSDVYLLPKKMDEYVASLHLATFDAHLTELTD 471
Cdd:cd00401 318 IILLAEGRLVNLACATghpsfV----MDMSFANQALAQIELWKNRDKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTE 393


                ....*....
gi 45553387 472 EQSKFMGLN 480
Cdd:cd00401 394 EQAEYLGSW 402
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 63-486 0e+00

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 639.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   63 AGGTDFCVKSISKSAFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNI 142
Cdd:PRK05476   3 ATGTDYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  143 YSTQNAVAAALAEAGIPIFAWRGETEEEFWWCLDRAIysDGWQPNLILDDGGDATHLMLKKYPDYFKAIRGIVEESVTGV 222
Cdd:PRK05476  83 FSTQDDVAAALAAAGIPVFAWKGETLEEYWECIERAL--DGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  223 HRLYMLSKGGKLTVPAINVNDSVTKNKFDTFYTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYV 302
Cdd:PRK05476 161 HRLYAMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  303 TEVDPICALQAAMDGFRVVRLNEVIRTVDVVVTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGLHTPELTWERV 382
Cdd:PRK05476 241 TEVDPICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  383 RSQVDHIRWPDGRMIILLAEGRLVNLSCST------------IssfvvsvasstQALALIELFSAPGRYKSDVYLLPKKM 450
Cdd:PRK05476 321 KPQVDEYTLPDGKRIILLAEGRLVNLGAATghpsevmdmsfaN-----------QALAQIELFTNRGKLEPGVYVLPKEL 389

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 45553387  451 DEYVASLHLATFDAHLTELTDEQSKFMGLNKAGPFK 486
Cdd:PRK05476 390 DEEVARLKLKALGVKLDELTEEQAEYIGVWVEGPFK 425
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
63-484 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 626.31  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  63 AGGTDFCVKSISKSAFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNI 142
Cdd:COG0499   1 TAPMDYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 143 YSTQNAVAAALAEAGIPIFAWRGETEEEFWWCLDRAIysdGWQPNLILDDGGDATHLMLKKYPDYFKAIRGIVEESVTGV 222
Cdd:COG0499  81 LSTQDDVAAALAAAGIPVFAWKGETLEEYYWCIEQAL---DHGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 223 HRLYMLSKGGKLTVPAINVNDSVTKNKFDTFYTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYV 302
Cdd:COG0499 158 HRLRAMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIV 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 303 TEVDPICALQAAMDGFRVVRLNEVIRTVDVVVTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGLHTPELTWERV 382
Cdd:COG0499 238 TEVDPICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREI 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 383 RSQVDHIRWPDGRMIILLAEGRLVNLSCST------------IssfvvsvasstQALALIELFSAPGRYKSDVYLLPKKM 450
Cdd:COG0499 318 RPQVDEYTLPDGRRIYLLAEGRLVNLAAATghpsevmdmsfaN-----------QALAQIYLVKNGDKLEPGVYVLPKEL 386

                       410       420       430
                ....*....|....*....|....*....|....
gi 45553387 451 DEYVASLHLATFDAHLTELTDEQSKFMGLNKAGP 484
Cdd:COG0499 387 DEEVARLKLEALGVKIDTLTEEQAEYLGSWVEGP 420
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 77-484 6.24e-177

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: 502.70  E-value: 6.24e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    77 AFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNIYSTQN-AVAAALAE 155
Cdd:TIGR00936   1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDdVAAALAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   156 AGIPIFAWRGETEEEFWWCLDRAIYSdgwQPNLILDDGGDATHLMLKKYPDYFKAIRGIVEESVTGVHRLYMLSKGGKLT 235
Cdd:TIGR00936  81 AGIPVFAWRGETNEEYYWAIEQVLDH---EPNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   236 VPAINVNDSVTKNKFDTFYTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAAM 315
Cdd:TIGR00936 158 FPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   316 DGFRVVRLNEVIRTVDVVVTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGLHTPELTWERVRSQVDHIRWPDGR 395
Cdd:TIGR00936 238 DGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   396 MIILLAEGRLVNLSCSTISSFVVSVASST-QALALIELFSAPGRYKSDVYLLPKKMDEYVASLHLATFDAHLTELTDEQS 474
Cdd:TIGR00936 318 RIYLLAEGRLVNLAAAEGHPSEVMDMSFAnQALAAEYLWKNHDKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQK 397

                         410
                  ....*....|
gi 45553387   475 KFMGLNKAGP 484
Cdd:TIGR00936 398 EYLGSWEEGT 407
 
Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
69-491 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 800.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387     69 CVKSISKSAFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNIYSTQNA 148
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    149 VAAALAEAGIPIFAWRGETEEEFWWCLDRAIY-SDGWQPNLILDDGGDATHLMLKKYPDYFKAIRGIVEESVTGVHRLYM 227
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTwPDGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    228 LSKGGKLTVPAINVNDSVTKNKFDTFYTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDP 307
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    308 ICALQAAMDGFRVVRLNEVIRTVDVVVTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGLHT-PELTWERVRSQV 386
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    387 DHIRWPDGRMIILLAEGRLVNLSCSTISSFVVSVASST-QALALIELFSAPGRYKSDVYLLPKKMDEYVASLHLATFDAH 465
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATGHPSFVMSNSFTnQVLAQIELFTKPGKYKNGVYVLPKKLDEKVARLHLEKLGAK 400

                          410       420
                   ....*....|....*....|....*.
gi 45553387    466 LTELTDEQSKFMGLNKAGPFKANYYR 491
Cdd:smart00996 401 LTKLTKEQADYIGVPVEGPFKPDHYR 426
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
67-491 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 758.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    67 DFCVKSISKSAFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNIYSTQ 146
Cdd:pfam05221   1 DYKVADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   147 NAVAAALAEAGIPIFAWRGETEEEFWWCLDRAIY--SDGWQPNLILDDGGDATHLMLKKYPDYFKAIRGIVEESVTGVHR 224
Cdd:pfam05221  81 DHAAAAIAAAGVPVFAWKGETLEEYWWCTEQALTwpPDGGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   225 LYMLSKGGKLTVPAINVNDSVTKNKFDTFYTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYVTE 304
Cdd:pfam05221 161 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   305 VDPICALQAAMDGFRVVRLNEVIRTVDVVVTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGL--HTPELTWERV 382
Cdd:pfam05221 241 IDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNIGHFDNEIDEIVLalLKGVKWVNIK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   383 RsQVDHIRWPDGRMIILLAEGRLVNLSCST--------IssfvvsvASSTQALALIELFSAPGRYKSDVYLLPKKMDEYV 454
Cdd:pfam05221 321 P-QVDDITFPDGKSIIVLAEGRLVNLGCATghpsfvmsN-------SFTNQVLAQIELWTNDKEYENGVYVLPKKLDEKV 392

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 45553387   455 ASLHLATFDAHLTELTDEQSKFMGLNKAGPFKANYYR 491
Cdd:pfam05221 393 ARLHLEKLGAKLTELTKEQADYIGVPVEGPFKPDHYR 429
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 77-480 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: 692.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  77 AFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNIYSTQNAVAAALAEA 156
Cdd:cd00401   1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 157 GIPIFAWRGETEEEFWWCLDRAIysdGWQPNLILDDGGDATHLMLKKYPDYFKAIRGIVEESVTGVHRLYMLSKGGKLTV 236
Cdd:cd00401  81 GIPVFAWKGETEEEYWWCIEQAL---DHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 237 PAINVNDSVTKNKFDTFYTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAAMD 316
Cdd:cd00401 158 PAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMD 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 317 GFRVVRLNEVIRTVDVVVTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGLHTPELTWERVRSQVDHIRWPDGRM 396
Cdd:cd00401 238 GFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRR 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 397 IILLAEGRLVNLSCST-----IssfvVSVASSTQALALIELFSAPGRYKSDVYLLPKKMDEYVASLHLATFDAHLTELTD 471
Cdd:cd00401 318 IILLAEGRLVNLACATghpsfV----MDMSFANQALAQIELWKNRDKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTE 393


                ....*....
gi 45553387 472 EQSKFMGLN 480
Cdd:cd00401 394 EQAEYLGSW 402
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 63-486 0e+00

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 639.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   63 AGGTDFCVKSISKSAFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNI 142
Cdd:PRK05476   3 ATGTDYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  143 YSTQNAVAAALAEAGIPIFAWRGETEEEFWWCLDRAIysDGWQPNLILDDGGDATHLMLKKYPDYFKAIRGIVEESVTGV 222
Cdd:PRK05476  83 FSTQDDVAAALAAAGIPVFAWKGETLEEYWECIERAL--DGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  223 HRLYMLSKGGKLTVPAINVNDSVTKNKFDTFYTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYV 302
Cdd:PRK05476 161 HRLYAMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  303 TEVDPICALQAAMDGFRVVRLNEVIRTVDVVVTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGLHTPELTWERV 382
Cdd:PRK05476 241 TEVDPICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  383 RSQVDHIRWPDGRMIILLAEGRLVNLSCST------------IssfvvsvasstQALALIELFSAPGRYKSDVYLLPKKM 450
Cdd:PRK05476 321 KPQVDEYTLPDGKRIILLAEGRLVNLGAATghpsevmdmsfaN-----------QALAQIELFTNRGKLEPGVYVLPKEL 389

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 45553387  451 DEYVASLHLATFDAHLTELTDEQSKFMGLNKAGPFK 486
Cdd:PRK05476 390 DEEVARLKLKALGVKLDELTEEQAEYIGVWVEGPFK 425
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
63-484 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 626.31  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  63 AGGTDFCVKSISKSAFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNI 142
Cdd:COG0499   1 TAPMDYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 143 YSTQNAVAAALAEAGIPIFAWRGETEEEFWWCLDRAIysdGWQPNLILDDGGDATHLMLKKYPDYFKAIRGIVEESVTGV 222
Cdd:COG0499  81 LSTQDDVAAALAAAGIPVFAWKGETLEEYYWCIEQAL---DHGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 223 HRLYMLSKGGKLTVPAINVNDSVTKNKFDTFYTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYV 302
Cdd:COG0499 158 HRLRAMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIV 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 303 TEVDPICALQAAMDGFRVVRLNEVIRTVDVVVTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGLHTPELTWERV 382
Cdd:COG0499 238 TEVDPICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREI 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 383 RSQVDHIRWPDGRMIILLAEGRLVNLSCST------------IssfvvsvasstQALALIELFSAPGRYKSDVYLLPKKM 450
Cdd:COG0499 318 RPQVDEYTLPDGRRIYLLAEGRLVNLAAATghpsevmdmsfaN-----------QALAQIYLVKNGDKLEPGVYVLPKEL 386

                       410       420       430
                ....*....|....*....|....*....|....
gi 45553387 451 DEYVASLHLATFDAHLTELTDEQSKFMGLNKAGP 484
Cdd:COG0499 387 DEEVARLKLEALGVKIDTLTEEQAEYLGSWVEGP 420
PTZ00075 PTZ00075
Adenosylhomocysteinase; Provisional
 66-492 0e+00

Adenosylhomocysteinase; Provisional


Pssm-ID: 240258  Cd Length: 476  Bit Score: 576.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   66 TDFCVKSISKSAFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNIYST 145
Cdd:PTZ00075   3 TDYKVKDISLAEFGRKEIELAENEMPGLMALREEYGPSKPLKGARITGCLHMTVQTAVLIETLKALGAEVRWCSCNIFST 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  146 QNAVAAALAEAG-IPIFAWRGETEEEFWWCLDRAI-YSDGWQPNLILDDGGDATHLMLK--------------------- 202
Cdd:PTZ00075  83 QDHAAAAIAKAGsVPVFAWKGETLEEYWWCTEQALkWPNGDGPNLIVDDGGDATLLVHEgvkaeklyeekgilpdpldps 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  203 --------------------KYPDYFKAIRGIVEESVTGVHRLYMLSKGGKLTVPAINVNDSVTKNKFDTFYTCRDSILD 262
Cdd:PTZ00075 163 nedekclltvlkklltknpdKWTNLVKKIVGVSEETTTGVHRLYKMLKKGELLFPAINVNDSVTKSKFDNIYGCRHSLID 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  263 SLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAAMDGFRVVRLNEVIRTVDVVVTATGNKNV 342
Cdd:PTZ00075 243 GIFRATDVMIAGKTVVVCGYGDVGKGCAQALRGFGARVVVTEIDPICALQAAMEGYQVVTLEDVVETADIFVTATGNKDI 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  343 ITRDHMNRMKNGCILCNMGHSCSEIDVNGLHT-PELTWERVRSQVDHIRWPDGRMIILLAEGRLVNLSCSTISSFVVSVA 421
Cdd:PTZ00075 323 ITLEHMRRMKNNAIVGNIGHFDNEIQVAELEAyPGIEIVEIKPQVDRYTFPDGKGIILLAEGRLVNLGCATGHPSFVMSN 402

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45553387  422 SST-QALALIELFS--APGRYKSDVYLLPKKMDEYVASLHLATFDAHLTELTDEQSKFMGLNKAGPFKANYYRY 492
Cdd:PTZ00075 403 SFTnQVLAQIELWEnrDTGKYPNGVYKLPKELDEKVARLHLKKLGAKLTKLTDKQAEYIGVPVDGPYKSDHYRY 476
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 77-484 6.24e-177

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: 502.70  E-value: 6.24e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    77 AFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNIYSTQN-AVAAALAE 155
Cdd:TIGR00936   1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDdVAAALAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   156 AGIPIFAWRGETEEEFWWCLDRAIYSdgwQPNLILDDGGDATHLMLKKYPDYFKAIRGIVEESVTGVHRLYMLSKGGKLT 235
Cdd:TIGR00936  81 AGIPVFAWRGETNEEYYWAIEQVLDH---EPNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   236 VPAINVNDSVTKNKFDTFYTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAAM 315
Cdd:TIGR00936 158 FPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   316 DGFRVVRLNEVIRTVDVVVTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGLHTPELTWERVRSQVDHIRWPDGR 395
Cdd:TIGR00936 238 DGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   396 MIILLAEGRLVNLSCSTISSFVVSVASST-QALALIELFSAPGRYKSDVYLLPKKMDEYVASLHLATFDAHLTELTDEQS 474
Cdd:TIGR00936 318 RIYLLAEGRLVNLAAAEGHPSEVMDMSFAnQALAAEYLWKNHDKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQK 397

                         410
                  ....*....|
gi 45553387   475 KFMGLNKAGP 484
Cdd:TIGR00936 398 EYLGSWEEGT 407
PLN02494 PLN02494
adenosylhomocysteinase
 63-492 1.46e-164

adenosylhomocysteinase


Pssm-ID: 178111 [Multi-domain]  Cd Length: 477  Bit Score: 473.97  E-value: 1.46e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   63 AGGTDFCVKSISKSAFGRREIEIAESEMPGIMTLRKRAKDEKPLKGANIVGCTHVNAQSAVLIETLVQLGATVRWAACNI 142
Cdd:PLN02494   1 SSGREYKVKDMSQADFGRLEIELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  143 YSTQNAVAAALAEAGIPIFAWRGETEEEFWWCLDRAI-YSDGWQPNLILDDGGDATHLM--------------------- 200
Cdd:PLN02494  81 FSTQDHAAAAIARDSAAVFAWKGETLQEYWWCTERALdWGPGGGPDLIVDDGGDATLLIhegvkaeeefekdgtlpdpts 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  201 ----------------LKKYPDYFKAIR----GIVEESVTGVHRLYMLSKGGKLTVPAINVNDSVTKNKFDTFYTCRDSI 260
Cdd:PLN02494 161 tdnaefkivltiikdgLKVDPKKYHKMKerlvGVSEETTTGVKRLYQMQKNGTLLFPAINVNDSVTKSKFDNLYGCRHSL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  261 LDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAAMDGFRVVRLNEVIRTVDVVVTATGNK 340
Cdd:PLN02494 241 PDGLMRATDVMIAGKVAVICGYGDVGKGCAAAMKAAGARVIVTEIDPICALQALMEGYQVLTLEDVVSEADIFVTTTGNK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  341 NVITRDHMNRMKNGCILCNMGHSCSEIDVNGLHT-PELTWERVRSQVDHIRWPD-GRMIILLAEGRLVNLSCSTISSFVV 418
Cdd:PLN02494 321 DIIMVDHMRKMKNNAIVCNIGHFDNEIDMLGLETyPGVKRITIKPQTDRWVFPDtGSGIIVLAEGRLMNLGCATGHPSFV 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45553387  419 SVASST-QALALIELFS--APGRYKSDVYLLPKKMDEYVASLHLATFDAHLTELTDEQSKFMGLNKAGPFKANYYRY 492
Cdd:PLN02494 401 MSCSFTnQVIAQLELWNekKSGKYEKKVYVLPKHLDEKVAALHLGKLGAKLTKLSKDQADYINVPVEGPYKPAHYRY 477
AdoHcyase_NAD pfam00670
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
252-413 3.81e-107

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


Pssm-ID: 395543 [Multi-domain]  Cd Length: 162  Bit Score: 315.45  E-value: 3.81e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   252 TFYTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAAMDGFRVVRLNEVIRTVD 331
Cdd:pfam00670   1 NLYGCRESLIDGIKRATDVMIAGKVAVVCGYGDVGKGCAASLKGQGARVIVTEIDPICALQAAMEGFQVVTLEEVVDKAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   332 VVVTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGLHTPELTWERVRSQVDHIRWPDGRMIILLAEGRLVNLSCS 411
Cdd:pfam00670  81 IFVTTTGNKDIITGEHMAKMKNDAIVCNIGHFDNEIDVAWLEANGKKKENIKPQVDRYTLPDGKHIILLAEGRLVNLGCA 160


                  ..
gi 45553387   412 TI 413
Cdd:pfam00670 161 TG 162
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
254-412 6.36e-98

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


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 292.05  E-value: 6.36e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    254 YTCRDSILDSLKRTTDIMFGGKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAAMDGFRVVRLNEVIRTVDVV 333
Cdd:smart00997   3 YGTGESLLDGILRATNVLLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPIRALEAAMDGFEVMKMEEAAKRADIF 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45553387    334 VTATGNKNVITRDHMNRMKNGCILCNMGHSCSEIDVNGLHTPELTWERVRSQVDHIRWPDGRMIILLAEGRLVNLSCST 412
Cdd:smart00997  83 VTATGNKDVITREHFRAMKDGAILANAGHFDVEIDVAALEELAVEKREVRPQVDEYTLPDGKRIYLLAEGRLVNLAAAT 161
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 111-410 2.19e-36

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: 136.59  E-value: 2.19e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 111 IVGCTHVNAQ------SAVLIETLVQLGATVRWAACNIYSTQNAVAAAlaeagipIFAWRGETEEEFwwcldraiysDGW 184
Cdd:cd12154   1 IAGPKEIKNEefrvglSPSVVATLVEAGHEVRVETGAGIGAGFADQAY-------VQAGAIVVTLAK----------ALW 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 185 QPNLILDDGGDATHL---MLKKYPdyfkaIRGIVEESVTGVHRLYMLSKGgKLTVPAINVNDSVTKNKFDTFYTCRDSIL 261
Cdd:cd12154  64 SLDVVLKVKEPLTNAeyaLIQKLG-----DRLLFTYTIGADHRDLTEALA-RAGLTAIAVEGVELPLLTSNSIGAGELSV 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 262 DSLKRTTDIMFGG----------KQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAAMDG-FRVVRLNEVIRTV 330
Cdd:cd12154 138 QFIARFLEVQQPGrlggapdvagKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGgKNVEELEEALAEA 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 331 DVVVTATGNKN-----VITRDHMNRMKNGCILCNMGHSCSEIDVnglhtpelTWERVRSQVDHIrwpdgrmIILLAEGRL 405
Cdd:cd12154 218 DVIVTTTLLPGkragiLVPEELVEQMKPGSVIVNVAVGAVGCVQ--------ALHTQLLEEGHG-------VVHYGDVNM 282


                ....*
gi 45553387 406 VNLSC 410
Cdd:cd12154 283 PGPGC 287
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 274-361 3.52e-08

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: 53.27  E-value: 3.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   274 GKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAAMDGFRVVRLNEVIRTVDVVVTAT----GNKNVITRDHMN 349
Cdd:pfam02826  36 GKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSLDELLAESDVVSLHLpltpETRHLINAERLA 115

                          90
                  ....*....|..
gi 45553387   350 RMKNGCILCNMG 361
Cdd:pfam02826 116 LMKPGAILINTA 127
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 274-361 2.51e-07

Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomains but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants.


Pssm-ID: 240625 [Multi-domain]  Cd Length: 313  Bit Score: 52.52  E-value: 2.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 274 GKQVVICGYGDVGKGCAQSLKGQGCIVY-----VTEVDPICALQAAMDgfrvvRLNEVIRTVDVVVTA------TgnKNV 342
Cdd:cd05300 134 GKTVLIVGLGDIGREIARRAKAFGMRVIgvrrsGRPAPPVVDEVYTPD-----ELDELLPEADYVVNAlpltpeT--RGL 206

                        90
                ....*....|....*....
gi 45553387 343 ITRDHMNRMKNGCILCNMG 361
Cdd:cd05300 207 FNAERFAAMKPGAVLINVG 225
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 275-344 7.37e-07

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 50.84  E-value: 7.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 275 KQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAAMDGFRVVRLN----EV-----IRTVDVVVTATGN--KNVI 343
Cdd:COG0569  96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDatdeEVleeagIEDADAVIAATGDdeANIL 175


                .
gi 45553387 344 T 344
Cdd:COG0569 176 A 176
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
 274-361 4.43e-06

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: 48.44  E-value: 4.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 274 GKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAAMDGFRVVRLNEVIRTVDVVVTAT----GNKNVITRDHMN 349
Cdd:cd12157 144 GKTVGILGMGALGRAIARRLSGFGATLLYYDPHPLDQAEEQALNLRRVELDELLESSDFLVLALpltpDTLHLINAEALA 223

                        90
                ....*....|..
gi 45553387 350 RMKNGCILCNMG 361
Cdd:cd12157 224 KMKPGALLVNPC 235
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 271-361 4.45e-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: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 48.34  E-value: 4.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 271 MFGGKQVVICGYGDVGKGCAQSLKGQGC-IVYVTE-VDPICALQAAmdGFRVVRLNEVIRTVDVVVTAT----GNKNVIT 344
Cdd:cd12175 139 ELSGKTVGIVGLGNIGRAVARRLRGFGVeVIYYDRfRDPEAEEKDL--GVRYVELDELLAESDVVSLHVpltpETRHLIG 216

                        90
                ....*....|....*..
gi 45553387 345 RDHMNRMKNGCILCNMG 361
Cdd:cd12175 217 AEELAAMKPGAILINTA 233
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 277-358 4.60e-06

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: 46.35  E-value: 4.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387    277 VVICGYGDVGKGCAQSLKGQGCIVYVTEVDP--ICALQAAMDG-FRVVRLN-----EVIRTVDVVVTA---TGNK--NVI 343
Cdd:smart01002  23 VVVIGAGVVGLGAAATAKGLGAEVTVLDVRParLRQLESLLGArFTTLYSQaelleEAVKEADLVIGAvliPGAKapKLV 102

                           90
                   ....*....|....*
gi 45553387    344 TRDHMNRMKNGCILC 358
Cdd:smart01002 103 TREMVKSMKPGSVIV 117
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 272-359 6.71e-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: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 48.09  E-value: 6.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 272 FGGKQVVICGYGDVGKGCAQSLK-GQGC--IVYvtevDP-ICALQAAMDGFRVVRLNEVIRTVDVVV----TATGNKNVI 343
Cdd:cd12177 145 LSGKTVGIIGYGNIGSRVAEILKeGFNAkvLAY----DPyVSEEVIKKKGAKPVSLEELLAESDIISlhapLTEETYHMI 220

                        90
                ....*....|....*.
gi 45553387 344 TRDHMNRMKNGCILCN 359
Cdd:cd12177 221 NEKAFSKMKKGVILVN 236
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 271-361 1.15e-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: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 47.24  E-value: 1.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 271 MFGGKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAAMDGFrVVRLNEVIRTVDVVVTAT----GNKNVITRD 346
Cdd:cd12165 134 ELRGKTVGILGYGHIGREIARLLKAFGMRVIGVSRSPKEDEGADFVGT-LSDLDEALEQADVVVVALpltkQTRGLIGAA 212

                        90
                ....*....|....*
gi 45553387 347 HMNRMKNGCILCNMG 361
Cdd:cd12165 213 ELAAMKPGAILVNVG 227
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 274-360 1.17e-05

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: 47.17  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 274 GKQVVICGYGDVGKGCAQSLKGQGCIVYVteVDPICALQAA----MDGFRVVRLNEVIRTVDVV---VTAT-GNKNVITR 345
Cdd:cd12174 135 GKTLGVIGLGNIGRLVANAALALGMKVIG--YDPYLSVEAAwklsVEVQRVTSLEELLATADYItlhVPLTdETRGLINA 212

                        90
                ....*....|....*
gi 45553387 346 DHMNRMKNGCILCNM 360
Cdd:cd12174 213 ELLAKMKPGAILLNF 227
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 277-344 4.06e-05

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 42.90  E-value: 4.06e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45553387   277 VVICGYGDVGKGCAQSLKgQGCIVYVTEVDPICALQAAMDGFRVVRLN----EV-----IRTVDVVVTATGN--KNVIT 344
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELS-EGGDVVVIDKDEERVEELREEGVPVVVGDatdeEVleeagIEEADAVIAATGDdeANILI 78
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
 264-346 3.47e-04

NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding domain of the Methylene-Tetrahydrofolate Dehydrogenase/cyclohydrolase (m-THF DH/cyclohydrolase) bifunctional enzyme. Tetrahydrofolate is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofucntional DH, as well as bifunctional m-THF m-THF DHm-THF DHDH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains the bifunctional DH/cyclohydrolase. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains.


Pssm-ID: 133448  Cd Length: 168  Bit Score: 41.39  E-value: 3.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 264 LKRTTDIMFGGKQVVICGYGD-VGKGCAQSLKGQGCIVyvtevdPICALQAAmdgfrvvRLNEVIRTVDVVVTATGNKNV 342
Cdd:cd01080  34 LLKRYGIDLAGKKVVVVGRSNiVGKPLAALLLNRNATV------TVCHSKTK-------NLKEHTKQADIVIVAVGKPGL 100


                ....
gi 45553387 343 ITRD 346
Cdd:cd01080 101 VKGD 104
PRK13403 PRK13403
ketol-acid reductoisomerase; Provisional
 252-333 4.10e-04

ketol-acid reductoisomerase; Provisional


Pssm-ID: 106361 [Multi-domain]  Cd Length: 335  Bit Score: 42.43  E-value: 4.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  252 TFYTcRDSILDSLKrttdimfgGKQVVICGYGDVGKGCAQSLKGQGCIVyVTEVDPICALQAA-MDGFRVVRLNEVIRTV 330
Cdd:PRK13403   3 TYYE-KDANVELLQ--------GKTVAVIGYGSQGHAQAQNLRDSGVEV-VVGVRPGKSFEVAkADGFEVMSVSEAVRTA 72


                 ...
gi 45553387  331 DVV 333
Cdd:PRK13403  73 QVV 75
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 259-350 4.61e-04

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 42.48  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  259 SILDSLKrttdimfgGKQVVICGYGDVGKGCAQSLKGQGC-IVYVT----EVdpicALQ-AAMDGFRVVRLNE---VIRT 329
Cdd:PRK00045 175 QIFGDLS--------GKKVLVIGAGEMGELVAKHLAEKGVrKITVAnrtlER----AEElAEEFGGEAIPLDElpeALAE 242

                         90       100
                 ....*....|....*....|..
gi 45553387  330 VDVVVTATGNKN-VITRDHMNR 350
Cdd:PRK00045 243 ADIVISSTGAPHpIIGKGMVER 264
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
274-361 5.04e-04

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 42.28  E-value: 5.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387  274 GKQVVICGYGDVGKGCAQSLKGQGCIV--YVTevdpicALQAAMDGFRVVRLNEVIRTVDVV-VTATGN---KNVITRDH 347
Cdd:PRK08410 145 GKKWGIIGLGTIGKRVAKIAQAFGAKVvyYST------SGKNKNEEYERVSLEELLKTSDIIsIHAPLNektKNLIAYKE 218

                         90
                 ....*....|....
gi 45553387  348 MNRMKNGCILCNMG 361
Cdd:PRK08410 219 LKLLKDGAILINVG 232
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 259-352 1.25e-03

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 39.09  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   259 SILDSLKrttdimfgGKQVVICGYGDVGKGCAQSLKGQGC----IVYVTeVDPICALQAAMDGFRVVRLNEV---IRTVD 331
Cdd:pfam01488   5 KIFGDLK--------DKKVLLIGAGEMGELVAKHLLAKGAkevtIANRT-IERAQELAEKFGGVEALPLDDLkeyLAEAD 75

                          90       100
                  ....*....|....*....|..
gi 45553387   332 VVVTATGNKN-VITRDHMNRMK 352
Cdd:pfam01488  76 IVISATSSPTpIITKEMVERAL 97
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
276-321 1.25e-03

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


Pssm-ID: 440839 [Multi-domain]  Cd Length: 279  Bit Score: 40.87  E-value: 1.25e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 45553387 276 QVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAAMDGFRVV 321
Cdd:COG1226 126 HVIIAGFGRVGQIVARLLRAEGIPFVVIDLDPERVEELRRFGIKVY 171
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
 274-359 1.75e-03

D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240663 [Multi-domain]  Cd Length: 329  Bit Score: 40.34  E-value: 1.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 274 GKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALqAAMDGFRVVRLNEVIRTVDVV---VTAT-GNKNVITRDHMN 349
Cdd:cd12187 139 GKTLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEEL-AERLGFRYVSLEELLQESDIIslhVPYTpQTHHLINRENFA 217

                        90
                ....*....|
gi 45553387 350 RMKNGCILCN 359
Cdd:cd12187 218 LMKPGAVLIN 227
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 263-352 2.16e-03

NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133444  Cd Length: 200  Bit Score: 39.50  E-value: 2.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 263 SLKRTTDIMFG-----GKQVVICGYGDVGKGCAQSLKGQGCIVYVTEVDPICALQAA-MDGFRVVRLNEVIRT-VDVVV- 334
Cdd:cd01075  12 GMKAAAEHLLGtdsleGKTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAeLFGATVVAPEEIYSVdADVFAp 91

                        90
                ....*....|....*...
gi 45553387 335 TATGnkNVITRDHMNRMK 352
Cdd:cd01075  92 CALG--GVINDDTIPQLK 107
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 277-369 2.70e-03

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: 40.08  E-value: 2.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 277 VVICGYGDVGKGCAQSLKGQGCIVYVTEVDP--ICALQAAMDGfRVV-------RLNEVIRTVDVVVTA---TGNK--NV 342
Cdd:cd05305 171 VVILGAGVVGENAARVALGLGAEVTVLDINLerLRYLDDIFGG-RVTtlysnpaNLEEALKEADLVIGAvliPGAKapKL 249

                        90       100
                ....*....|....*....|....*..
gi 45553387 343 ITRDHMNRMKNGCILcnmghscseIDV 369
Cdd:cd05305 250 VTEEMVKTMKPGSVI---------VDV 267
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 277-354 3.57e-03

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: 39.02  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387   277 VVICGYGDVGKGCAQSLKGQGCIVYVTEVDPIcALQAAMDGF--RVVR--------LNEVIRTVDVVVTA---TGNK--N 341
Cdd:pfam01262  31 VLVIGGGVAGLNAAATAKGLGAIVTILDVRPA-RLEQLESILgaKFVEtlysqaelIAEAVKEADLVIGTaliPGAKapK 109

                          90
                  ....*....|...
gi 45553387   342 VITRDHMNRMKNG 354
Cdd:pfam01262 110 LVTREMVKSMKPG 122
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 260-348 3.86e-03

Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440142 [Multi-domain]  Cd Length: 425  Bit Score: 39.71  E-value: 3.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 260 ILDSLKrttdimfgGKQVVICGYGDVGKGCAQSLKGQGC-IVYVT-------EvdpicALQAAMDGfRVVRLNE---VIR 328
Cdd:COG0373 176 IFGDLS--------GKTVLVIGAGEMGELAARHLAAKGVkRITVAnrtleraE-----ELAEEFGG-EAVPLEElpeALA 241

                        90       100
                ....*....|....*....|.
gi 45553387 329 TVDVVVTATGNKN-VITRDHM 348
Cdd:COG0373 242 EADIVISSTGAPHpVITKEMV 262
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
276-361 9.32e-03

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 38.28  E-value: 9.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553387 276 QVVICGY-GDVGKGCAQSLKGQGCIVYVT--EVDPICALQAAM---DGFRV---VRLNEVIRTVDVVVTAT-GNKNVITR 345
Cdd:COG5322 153 TVAVVGAtGSIGSVCARLLAREVKRLTLVarNLERLEELAEEIlrnPGGKVtitTDIDEALREADIVVTVTsAVGAIIDP 232

                        90
                ....*....|....*.
gi 45553387 346 DHmnrMKNGCILCNMG 361
Cdd:COG5322 233 ED---LKPGAVVCDVA 245
 
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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