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Conserved domains on  [gi|1720419014|ref|XP_030111503|]
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putative adenosylhomocysteinase 3 isoform X7 [Mus musculus]

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
EC:  3.13.2.1
Gene Ontology:  GO:0033353|GO:0070403
PubMed:  715439|11325033
SCOP:  4000098

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
1-403 0e+00

S-adenosyl-L-homocysteine hydrolase;


:

Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 828.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014    1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESED 80
Cdd:smart00996  22 MPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDHAAAAIAAAGVPVFAWKGETLE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   81 DFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQ 159
Cdd:smart00996 102 EYWWCIEQTLTWPdGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQMAKKGKLLFPAINVNDSVTKS 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  160 KFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIR 239
Cdd:smart00996 182 KFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDPICALQAAMDGFEVVTMEEVAP 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  240 QVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRT-PELTWERVRSQVDHVIWPDGKRIVLLAEGRLLN 318
Cdd:smart00996 262 QADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQVDHITFPDGKRIILLAEGRLVN 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  319 LSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPF 397
Cdd:smart00996 342 LGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEKLGAKLTKLTKEQADYIGVPVEGPF 420


                   ....*.
gi 1720419014  398 KPNYYR 403
Cdd:smart00996 421 KPDHYR 426
 
Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
1-403 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 828.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014    1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESED 80
Cdd:smart00996  22 MPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDHAAAAIAAAGVPVFAWKGETLE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   81 DFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQ 159
Cdd:smart00996 102 EYWWCIEQTLTWPdGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQMAKKGKLLFPAINVNDSVTKS 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  160 KFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIR 239
Cdd:smart00996 182 KFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDPICALQAAMDGFEVVTMEEVAP 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  240 QVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRT-PELTWERVRSQVDHVIWPDGKRIVLLAEGRLLN 318
Cdd:smart00996 262 QADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQVDHITFPDGKRIILLAEGRLVN 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  319 LSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPF 397
Cdd:smart00996 342 LGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEKLGAKLTKLTKEQADYIGVPVEGPF 420


                   ....*.
gi 1720419014  398 KPNYYR 403
Cdd:smart00996 421 KPDHYR 426
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
1-403 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 779.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESED 80
Cdd:pfam05221  24 MPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDHAAAAIAAAGVPVFAWKGETLE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  81 DFWWCIDRCVN--VEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTK 158
Cdd:pfam05221 104 EYWWCTEQALTwpPDGGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHRLYQMAKKGKLLFPAINVNDSVTK 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 159 QKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVI 238
Cdd:pfam05221 184 SKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDPICALQAAMEGYEVVTMEDVV 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 239 RQVDIVITCTGNKNVVTREHLDRMKNSCIVCN--MGHSNTEIDVASLRTPELTWERVRsQVDHVIWPDGKRIVLLAEGRL 316
Cdd:pfam05221 264 GEADIFITTTTNTNVITVEHMDHMKMMAIVCNigHFDNEIDEIVLALLKGVKWVNIKP-QVDDITFPDGKSIIVLAEGRL 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 317 LNLSCST-VPTFVLSITATTQALALIELYNaPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNG 395
Cdd:pfam05221 343 VNLGCATgHPSFVMSNSFTNQVLAQIELWT-NDKEYENGVYVLPKKLDEKVARLHLEKLGAKLTELTKEQADYIGVPVEG 421


                  ....*...
gi 1720419014 396 PFKPNYYR 403
Cdd:pfam05221 422 PFKPDHYR 429
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 1-392 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: 723.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESED 80
Cdd:cd00401    14 MPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEAGIPVFAWKGETEE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  81 DFWWCIDRCVnveGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQK 160
Cdd:cd00401    94 EYWWCIEQAL---DHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLFPAIAVNDAVTKHK 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 161 FDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQ 240
Cdd:cd00401   171 FDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMDGFEVMPMEEAAKI 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 241 VDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLS 320
Cdd:cd00401   251 GDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRRIILLAEGRLVNLA 330

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720419014 321 CST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLN 392
Cdd:cd00401   331 CATgHPSFVMDMSFANQALAQIELWKNR-DKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQAEYLGSW 402
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 1-398 0e+00

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 634.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESED 80
Cdd:PRK05476   30 MPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNPFSTQDDVAAALAAAGIPVFAWKGETLE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  81 DFWWCIDRCVnvEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQK 160
Cdd:PRK05476  110 EYWECIERAL--DGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGVHRLYAMAKDGALKFPAINVNDSVTKSK 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 161 FDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQ 240
Cdd:PRK05476  188 FDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVDPICALQAAMDGFRVMTMEEAAEL 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 241 VDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLS 320
Cdd:PRK05476  268 GDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKPQVDEYTLPDGKRIILLAEGRLVNLG 347

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720419014 321 CST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPFK 398
Cdd:PRK05476  348 AATgHPSEVMDMSFANQALAQIELFTNR-GKLEPGVYVLPKELDEEVARLKLKALGVKLDELTEEQAEYIGVWVEGPFK 425
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
1-396 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 630.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESED 80
Cdd:COG0499    28 MPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNPLSTQDDVAAALAAAGIPVFAWKGETLE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  81 DFWWCIDRCVNvegWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQK 160
Cdd:COG0499   108 EYYWCIEQALD---HGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHRLRAMAKEGALKFPAIAVNDAVTKSL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 161 FDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQ 240
Cdd:COG0499   185 FDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVDPICALEAAMDGFRVMPMEEAAKL 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 241 VDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLS 320
Cdd:COG0499   265 GDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRPQVDEYTLPDGRRIYLLAEGRLVNLA 344

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720419014 321 CST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGP 396
Cdd:COG0499   345 AATgHPSEVMDMSFANQALAQIYLVKNG-DKLEPGVYVLPKELDEEVARLKLEALGVKIDTLTEEQAEYLGSWVEGP 420
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 1-396 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: 508.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAES-GFPVFAWKGESE 79
Cdd:TIGR00936  14 MPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAALAKGaGIPVFAWRGETN 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  80 DDFWWCIDRCVNVEgwqPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQ 159
Cdd:TIGR00936  94 EEYYWAIEQVLDHE---PNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLKFPAINVNDAYTKS 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 160 KFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIR 239
Cdd:TIGR00936 171 LFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAMDGFRVMTMEEAAK 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 240 QVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNL 319
Cdd:TIGR00936 251 IGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGRRIYLLAEGRLVNL 330

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720419014 320 SCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGP 396
Cdd:TIGR00936 331 AAAEgHPSEVMDMSFANQALAAEYLWKNH-DKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQKEYLGSWEEGT 407
 
Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
1-403 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 828.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014    1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESED 80
Cdd:smart00996  22 MPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDHAAAAIAAAGVPVFAWKGETLE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   81 DFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQ 159
Cdd:smart00996 102 EYWWCIEQTLTWPdGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQMAKKGKLLFPAINVNDSVTKS 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  160 KFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIR 239
Cdd:smart00996 182 KFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDPICALQAAMDGFEVVTMEEVAP 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  240 QVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRT-PELTWERVRSQVDHVIWPDGKRIVLLAEGRLLN 318
Cdd:smart00996 262 QADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQVDHITFPDGKRIILLAEGRLVN 341

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  319 LSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPF 397
Cdd:smart00996 342 LGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEKLGAKLTKLTKEQADYIGVPVEGPF 420


                   ....*.
gi 1720419014  398 KPNYYR 403
Cdd:smart00996 421 KPDHYR 426
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
1-403 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 779.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESED 80
Cdd:pfam05221  24 MPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDHAAAAIAAAGVPVFAWKGETLE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  81 DFWWCIDRCVN--VEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTK 158
Cdd:pfam05221 104 EYWWCTEQALTwpPDGGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHRLYQMAKKGKLLFPAINVNDSVTK 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 159 QKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVI 238
Cdd:pfam05221 184 SKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDPICALQAAMEGYEVVTMEDVV 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 239 RQVDIVITCTGNKNVVTREHLDRMKNSCIVCN--MGHSNTEIDVASLRTPELTWERVRsQVDHVIWPDGKRIVLLAEGRL 316
Cdd:pfam05221 264 GEADIFITTTTNTNVITVEHMDHMKMMAIVCNigHFDNEIDEIVLALLKGVKWVNIKP-QVDDITFPDGKSIIVLAEGRL 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 317 LNLSCST-VPTFVLSITATTQALALIELYNaPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNG 395
Cdd:pfam05221 343 VNLGCATgHPSFVMSNSFTNQVLAQIELWT-NDKEYENGVYVLPKKLDEKVARLHLEKLGAKLTELTKEQADYIGVPVEG 421


                  ....*...
gi 1720419014 396 PFKPNYYR 403
Cdd:pfam05221 422 PFKPDHYR 429
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 1-392 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: 723.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESED 80
Cdd:cd00401    14 MPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEAGIPVFAWKGETEE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  81 DFWWCIDRCVnveGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQK 160
Cdd:cd00401    94 EYWWCIEQAL---DHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLFPAIAVNDAVTKHK 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 161 FDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQ 240
Cdd:cd00401   171 FDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMDGFEVMPMEEAAKI 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 241 VDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLS 320
Cdd:cd00401   251 GDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRRIILLAEGRLVNLA 330

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720419014 321 CST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLN 392
Cdd:cd00401   331 CATgHPSFVMDMSFANQALAQIELWKNR-DKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQAEYLGSW 402
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 1-398 0e+00

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 634.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESED 80
Cdd:PRK05476   30 MPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNPFSTQDDVAAALAAAGIPVFAWKGETLE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  81 DFWWCIDRCVnvEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQK 160
Cdd:PRK05476  110 EYWECIERAL--DGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGVHRLYAMAKDGALKFPAINVNDSVTKSK 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 161 FDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQ 240
Cdd:PRK05476  188 FDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVDPICALQAAMDGFRVMTMEEAAEL 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 241 VDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLS 320
Cdd:PRK05476  268 GDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKPQVDEYTLPDGKRIILLAEGRLVNLG 347

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720419014 321 CST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPFK 398
Cdd:PRK05476  348 AATgHPSEVMDMSFANQALAQIELFTNR-GKLEPGVYVLPKELDEEVARLKLKALGVKLDELTEEQAEYIGVWVEGPFK 425
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
1-396 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 630.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESED 80
Cdd:COG0499    28 MPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNPLSTQDDVAAALAAAGIPVFAWKGETLE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  81 DFWWCIDRCVNvegWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQK 160
Cdd:COG0499   108 EYYWCIEQALD---HGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHRLRAMAKEGALKFPAIAVNDAVTKSL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 161 FDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQ 240
Cdd:COG0499   185 FDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVDPICALEAAMDGFRVMPMEEAAKL 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 241 VDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLS 320
Cdd:COG0499   265 GDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRPQVDEYTLPDGRRIYLLAEGRLVNLA 344

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720419014 321 CST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGP 396
Cdd:COG0499   345 AATgHPSEVMDMSFANQALAQIYLVKNG-DKLEPGVYVLPKELDEEVARLKLEALGVKIDTLTEEQAEYLGSWVEGP 420
PTZ00075 PTZ00075
Adenosylhomocysteinase; Provisional
 1-404 0e+00

Adenosylhomocysteinase; Provisional


Pssm-ID: 240258  Cd Length: 476  Bit Score: 570.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGF-PVFAWKGESE 79
Cdd:PTZ00075   27 MPGLMALREEYGPSKPLKGARITGCLHMTVQTAVLIETLKALGAEVRWCSCNIFSTQDHAAAAIAKAGSvPVFAWKGETL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  80 DDFWWCIDRCVNvegWQ----PNMILDDGGDLTHWIYK-----------------------------------------K 114
Cdd:PTZ00075  107 EEYWWCTEQALK---WPngdgPNLIVDDGGDATLLVHEgvkaeklyeekgilpdpldpsnedekclltvlkklltknpdK 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 115 YPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYG 194
Cdd:PTZ00075  184 WTNLVKKIVGVSEETTTGVHRLYKMLKKGELLFPAINVNDSVTKSKFDNIYGCRHSLIDGIFRATDVMIAGKTVVVCGYG 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 195 EVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHS 274
Cdd:PTZ00075  264 DVGKGCAQALRGFGARVVVTEIDPICALQAAMEGYQVVTLEDVVETADIFVTATGNKDIITLEHMRRMKNNAIVGNIGHF 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 275 NTEIDVASLRT-PELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELY-NAPEGRY 351
Cdd:PTZ00075  344 DNEIQVAELEAyPGIEIVEIKPQVDRYTFPDGKGIILLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELWeNRDTGKY 423

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720419014 352 KQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPFKPNYYRY 404
Cdd:PTZ00075  424 PNGVYKLPKELDEKVARLHLKKLGAKLTKLTDKQAEYIGVPVDGPYKSDHYRY 476
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 1-396 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: 508.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAES-GFPVFAWKGESE 79
Cdd:TIGR00936  14 MPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAALAKGaGIPVFAWRGETN 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  80 DDFWWCIDRCVNVEgwqPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQ 159
Cdd:TIGR00936  94 EEYYWAIEQVLDHE---PNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLKFPAINVNDAYTKS 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 160 KFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIR 239
Cdd:TIGR00936 171 LFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAMDGFRVMTMEEAAK 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 240 QVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNL 319
Cdd:TIGR00936 251 IGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGRRIYLLAEGRLVNL 330

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720419014 320 SCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGP 396
Cdd:TIGR00936 331 AAAEgHPSEVMDMSFANQALAAEYLWKNH-DKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQKEYLGSWEEGT 407
PLN02494 PLN02494
adenosylhomocysteinase
 1-404 3.86e-170

adenosylhomocysteinase


Pssm-ID: 178111 [Multi-domain]  Cd Length: 477  Bit Score: 484.37  E-value: 3.86e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014   1 MPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESED 80
Cdd:PLN02494   28 MPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNIFSTQDHAAAAIARDSAAVFAWKGETLQ 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  81 DFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIY-----------------------------------------KKYPNM 118
Cdd:PLN02494  108 EYWWCTERALDWGpGGGPDLIVDDGGDATLLIHegvkaeeefekdgtlpdptstdnaefkivltiikdglkvdpKKYHKM 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 119 FKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGK 198
Cdd:PLN02494  188 KERLVGVSEETTTGVKRLYQMQKNGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDGLMRATDVMIAGKVAVICGYGDVGK 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 199 GCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEI 278
Cdd:PLN02494  268 GCAAAMKAAGARVIVTEIDPICALQALMEGYQVLTLEDVVSEADIFVTTTGNKDIIMVDHMRKMKNNAIVCNIGHFDNEI 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 279 DVASLRT-PELTWERVRSQVDHVIWPDGKR-IVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPE-GRYKQD 354
Cdd:PLN02494  348 DMLGLETyPGVKRITIKPQTDRWVFPDTGSgIIVLAEGRLMNLGCATgHPSFVMSCSFTNQVIAQLELWNEKKsGKYEKK 427

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720419014 355 VYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPFKPNYYRY 404
Cdd:PLN02494  428 VYVLPKHLDEKVAALHLGKLGAKLTKLSKDQADYINVPVEGPYKPAHYRY 477
AdoHcyase_NAD pfam00670
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
163-323 8.83e-106

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


Pssm-ID: 395543 [Multi-domain]  Cd Length: 162  Bit Score: 308.90  E-value: 8.83e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 163 NLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVD 242
Cdd:pfam00670   1 NLYGCRESLIDGIKRATDVMIAGKVAVVCGYGDVGKGCAASLKGQGARVIVTEIDPICALQAAMEGFQVVTLEEVVDKAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 243 IVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCS 322
Cdd:pfam00670  81 IFVTTTGNKDIITGEHMAKMKNDAIVCNIGHFDNEIDVAWLEANGKKKENIKPQVDRYTLPDGKHIILLAEGRLVNLGCA 160


                  .
gi 1720419014 323 T 323
Cdd:pfam00670 161 T 161
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
163-324 2.35e-103

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


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 302.83  E-value: 2.35e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  163 NLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVD 242
Cdd:smart00997   1 NRYGTGESLLDGILRATNVLLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPIRALEAAMDGFEVMKMEEAAKRAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  243 IVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCS 322
Cdd:smart00997  81 IFVTATGNKDVITREHFRAMKDGAILANAGHFDVEIDVAALEELAVEKREVRPQVDEYTLPDGKRIYLLAEGRLVNLAAA 160


                   ..
gi 1720419014  323 TV 324
Cdd:smart00997 161 TG 162
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 22-343 6.88e-38

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: 138.90  E-value: 6.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  22 IVGCTHITAQTA------VLMETLGALGAQCRWAACNIYSTLNEVAAALAEsgfpvfawkgeseddfwWCIDRCVNVEGW 95
Cdd:cd12154     1 IAGPKEIKNEEFrvglspSVVATLVEAGHEVRVETGAGIGAGFADQAYVQA-----------------GAIVVTLAKALW 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  96 QPNMILDDGGDLTHWIYKkypnMFKK--IKGIVEESVTGVHRLY--QLSKAGklcVPAMNVNDSVTKQKFDNLYCCRESI 171
Cdd:cd12154    64 SLDVVLKVKEPLTNAEYA----LIQKlgDRLLFTYTIGADHRDLteALARAG---LTAIAVEGVELPLLTSNSIGAGELS 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 172 LDGLKRTTDMMFGG----------KQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLV-KLNEVIRQ 240
Cdd:cd12154   137 VQFIARFLEVQQPGrlggapdvagKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKNVeELEEALAE 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 241 VDIVITCTGNKN-----VVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELtwervrsqvdhviwpDGKRIVLLAEGR 315
Cdd:cd12154   217 ADVIVTTTLLPGkragiLVPEELVEQMKPGSVIVNVAVGAVGCVQALHTQLLE---------------EGHGVVHYGDVN 281

                         330       340
                  ....*....|....*....|....*....
gi 1720419014 316 LLNLSC-STVPTFVLSITATTQALALIEL 343
Cdd:cd12154   282 MPGPGCaMGVPWDATLRLAANTLPALVKL 310
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 186-315 1.04e-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: 53.15  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 186 KQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLN----EV-----IRQVDIVITCTGN--KNVV 254
Cdd:COG0569    96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDatdeEVleeagIEDADAVIAATGDdeANIL 175

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720419014 255 TrehldrmknsCIVC-NMGHSNTeidVASLRTPELTWERVRSQVDHVIWPD---GKRIVLLAEGR 315
Cdd:COG0569   176 A----------CLLAkELGVPRI---IARANDPEYADLLERLGADVVISPErlaARRIARLLLRP 227
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 188-268 3.20e-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: 49.43  E-value: 3.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014  188 VVVCGYGEVGKGCCAALKAMGSIVYVTEIDP--ICALQACMDG-FRLVKLN-----EVIRQVDIVITC---TGNK--NVV 254
Cdd:smart01002  23 VVVIGAGVVGLGAAATAKGLGAEVTVLDVRParLRQLESLLGArFTTLYSQaelleEAVKEADLVIGAvliPGAKapKLV 102

                           90
                   ....*....|....*
gi 1720419014  255 TREHLDRMK-NSCIV 268
Cdd:smart01002 103 TREMVKSMKpGSVIV 117
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 169-261 3.74e-06

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 48.64  E-value: 3.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 169 ESILDGLKrttdmmfgGKQVVVCGYGEVGKGCCAALKAMG-SIVYVT----EIDPICALQACMDGFRLVKLNEVIRQVDI 243
Cdd:PRK00045  174 KQIFGDLS--------GKKVLVIGAGEMGELVAKHLAEKGvRKITVAnrtlERAEELAEEFGGEAIPLDELPEALAEADI 245

                          90
                  ....*....|....*....
gi 1720419014 244 VITCTGNKN-VVTREHLDR 261
Cdd:PRK00045  246 VISSTGAPHpIIGKGMVER 264
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 185-272 1.48e-05

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: 46.36  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 185 GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDIVITC------TgnKNVVTREH 258
Cdd:cd05300   134 GKTVLIVGLGDIGREIARRAKAFGMRVIGVRRSGRPAPPVVDEVYTPDELDELLPEADYVVNAlpltpeT--RGLFNAER 211

                          90
                  ....*....|....
gi 1720419014 259 LDRMKNSCIVCNMG 272
Cdd:cd05300   212 FAAMKPGAVLINVG 225
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 185-272 4.78e-05

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: 43.64  E-value: 4.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 185 GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDIV-ITCTGNK---NVVTREHLD 260
Cdd:pfam02826  36 GKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSLDELLAESDVVsLHLPLTPetrHLINAERLA 115

                          90
                  ....*....|..
gi 1720419014 261 RMKNSCIVCNMG 272
Cdd:pfam02826 116 LMKPGAILINTA 127
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 169-261 1.47e-04

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: 43.56  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 169 ESILDGLKrttdmmfgGKQVVVCGYGEVGKGCCAALKAMG-SIVYVT-------EidpicALQACMDG--FRLVKLNEVI 238
Cdd:COG0373   174 KKIFGDLS--------GKTVLVIGAGEMGELAARHLAAKGvKRITVAnrtleraE-----ELAEEFGGeaVPLEELPEAL 240

                          90       100
                  ....*....|....*....|....
gi 1720419014 239 RQVDIVITCTGNKN-VVTREHLDR 261
Cdd:COG0373   241 AEADIVISSTGAPHpVITKEMVER 264
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 188-268 2.60e-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: 42.10  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 188 VVVCGYGEVGKGCCAALKAMGSIVYVTEIDP--ICALQACMdGFRLVK--------LNEVIRQVDIVITC---TGNK--N 252
Cdd:pfam01262  31 VLVIGGGVAGLNAAATAKGLGAIVTILDVRParLEQLESIL-GAKFVEtlysqaelIAEAVKEADLVIGTaliPGAKapK 109

                          90
                  ....*....|....*..
gi 1720419014 253 VVTREHLDRMKN-SCIV 268
Cdd:pfam01262 110 LVTREMVKSMKPgSVIV 126
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 182-272 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: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 42.23  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 182 MFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFrLVKLNEVIRQVDIVITCT----GNKNVVTRE 257
Cdd:cd12165   134 ELRGKTVGILGYGHIGREIARLLKAFGMRVIGVSRSPKEDEGADFVGT-LSDLDEALEQADVVVVALpltkQTRGLIGAA 212

                          90
                  ....*....|....*
gi 1720419014 258 HLDRMKNSCIVCNMG 272
Cdd:cd12165   213 ELAAMKPGAILVNVG 227
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 185-270 3.45e-04

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: 42.23  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 185 GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQAcMDGFRLVKLNEVIRQVDIVITCTG----NKNVVTREHLD 260
Cdd:cd05198   140 GKTVGIVGLGRIGQRVAKRLQAFGMKVLYYDRTRKPEPEE-DLGFRVVSLDELLAQSDVVVLHLPltpeTRHLINEEELA 218

                          90
                  ....*....|
gi 1720419014 261 RMKNSCIVCN 270
Cdd:cd05198   219 LMKPGAVLVN 228
PRK08306 PRK08306
dipicolinate synthase subunit DpsA;
185-282 3.85e-04

dipicolinate synthase subunit DpsA;


Pssm-ID: 181371 [Multi-domain]  Cd Length: 296  Bit Score: 42.13  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 185 GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPicALQA-----CMDGFRLVKLNEVIRQVDIVItctgnkN-----VV 254
Cdd:PRK08306  152 GSNVLVLGFGRTGMTLARTLKALGANVTVGARKS--AHLAritemGLSPFHLSELAEEVGKIDIIF------NtipalVL 223

                          90       100
                  ....*....|....*....|....*...
gi 1720419014 255 TREHLDRMKNSCIVcnmghsnteIDVAS 282
Cdd:PRK08306  224 TKEVLSKMPPEALI---------IDLAS 242
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 168-272 5.80e-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: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 41.40  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 168 RESILDGLKRTTD----MMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDI 243
Cdd:cd12175   121 DRELRAGRWGRPEgrpsRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFRDPEAEEKDLGVRYVELDELLAESDV 200

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1720419014 244 VITCT----GNKNVVTREHLDRMKNSCIVCNMG 272
Cdd:cd12175   201 VSLHVpltpETRHLIGAEELAAMKPGAILINTA 233
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 169-249 6.34e-04

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (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: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 41.48  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 169 ESILDGLKrttdmmfgGKQVVVCGYGEVGKGCCAALKAMG-SIVYVTEIDPICALQ-ACMDGFRLVKLNEV---IRQVDI 243
Cdd:cd05213   170 EKIFGNLK--------GKKVLVIGAGEMGELAAKHLAAKGvAEITIANRTYERAEElAKELGGNAVPLDELlelLNEADV 241


                  ....*.
gi 1720419014 244 VITCTG 249
Cdd:cd05213   242 VISATG 247
PLN02928 PLN02928
oxidoreductase family protein
 185-272 1.08e-03

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 40.82  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 185 GKQVVVCGYGEVGKGCCAALKAMGSIVYVT------EIDPICALQACmDGFRLV-------KLNEVIRQVDIVITC---- 247
Cdd:PLN02928  159 GKTVFILGYGAIGIELAKRLRPFGVKLLATrrswtsEPEDGLLIPNG-DVDDLVdekggheDIYEFAGEADIVVLCctlt 237

                          90       100
                  ....*....|....*....|....*
gi 1720419014 248 TGNKNVVTREHLDRMKNSCIVCNMG 272
Cdd:PLN02928  238 KETAGIVNDEFLSSMKKGALLVNIA 262
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 183-270 1.68e-03

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


Pssm-ID: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 40.00  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 183 FGGKQVVVCGYGEVGKgCCAALKAMGSIVYVTEIDP-ICALQACMDGFRLVKLNEVIRQVDIVITC----TGNKNVVTRE 257
Cdd:cd12177   145 LSGKTVGIIGYGNIGS-RVAEILKEGFNAKVLAYDPyVSEEVIKKKGAKPVSLEELLAESDIISLHapltEETYHMINEK 223

                          90
                  ....*....|...
gi 1720419014 258 HLDRMKNSCIVCN 270
Cdd:cd12177   224 AFSKMKKGVILVN 236
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 185-250 2.93e-03

Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 39.40  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 185 GKQVVVCGYGEVGKGCCAALKAMG-SIVYVTEIDP-------------ICALQACMDGFRLVKLNEVI--RQVDIVITCT 248
Cdd:cd05285   163 GDTVLVFGAGPIGLLTAAVAKAFGaTKVVVTDIDPsrlefakelgathTVNVRTEDTPESAEKIAELLggKGPDVVIECT 242


                  ..
gi 1720419014 249 GN 250
Cdd:cd05285   243 GA 244
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 174-268 3.94e-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: 38.34  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720419014 174 GLKRTTDMMFG-----GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQAC-MDGFRLVKLNEVIRQ-VDIVIT 246
Cdd:cd01075    12 GMKAAAEHLLGtdsleGKTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAeLFGATVVAPEEIYSVdADVFAP 91

                          90       100
                  ....*....|....*....|..
gi 1720419014 247 CtGNKNVVTREHLDRMKNSCIV 268
Cdd:cd01075    92 C-ALGGVINDDTIPQLKAKAIA 112
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 188-250 7.97e-03

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: 35.96  E-value: 7.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720419014 188 VVVCGYGEVGKGCCAALKAMGSIVyVTEIDPICALQACMDGFRLVKLN----EV-----IRQVDIVITCTGN 250
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSEGGDVV-VIDKDEERVEELREEGVPVVVGDatdeEVleeagIEEADAVIAATGD 71
 
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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