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Conserved domains on  [gi|26343517|dbj|BAC35415|]
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unnamed protein product [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
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;
84-507 0e+00

S-adenosyl-L-homocysteine hydrolase;


:

Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 880.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517     84 CVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNE 163
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    164 VAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQ 242
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPdGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    243 LSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDP 322
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    323 ICALQACMDGFRVVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRT-PELTWERVRSQV 401
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    402 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 480
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEKLGA 399

                          410       420
                   ....*....|....*....|....*..
gi 26343517    481 HLTELTDEQAKYLGLNKNGPFKPNYYR 507
Cdd:smart00996 400 KLTKLTKEQADYIGVPVEGPFKPDHYR 426
 
Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
84-507 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 880.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517     84 CVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNE 163
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    164 VAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQ 242
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPdGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    243 LSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDP 322
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    323 ICALQACMDGFRVVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRT-PELTWERVRSQV 401
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    402 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 480
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEKLGA 399

                          410       420
                   ....*....|....*....|....*..
gi 26343517    481 HLTELTDEQAKYLGLNKNGPFKPNYYR 507
Cdd:smart00996 400 KLTKLTKEQADYIGVPVEGPFKPDHYR 426
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
82-507 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 838.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    82 DFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTL 161
Cdd:pfam05221   1 DYKVADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   162 NEVAAALAESGFPVFAWKGESEDDFWWCIDRCVN--VEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHR 239
Cdd:pfam05221  81 DHAAAAIAAAGVPVFAWKGETLEEYWWCTEQALTwpPDGGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   240 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTE 319
Cdd:pfam05221 161 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   320 IDPICALQACMDGFRVVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCN--MGHSNTEIDVASLRTPELTWERV 397
Cdd:pfam05221 241 IDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNigHFDNEIDEIVLALLKGVKWVNIK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   398 RsQVDHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNaPEGRYKQDVYLLPKKMDEYVASLHLP 476
Cdd:pfam05221 321 P-QVDDITFPDGKSIIVLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELWT-NDKEYENGVYVLPKKLDEKVARLHLE 398

                         410       420       430
                  ....*....|....*....|....*....|.
gi 26343517   477 TFDAHLTELTDEQAKYLGLNKNGPFKPNYYR 507
Cdd:pfam05221 399 KLGAKLTELTKEQADYIGVPVEGPFKPDHYR 429
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 92-496 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: 761.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  92 EFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAES 171
Cdd:cd00401   1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 172 GFPVFAWKGESEDDFWWCIDRCVnveGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCV 251
Cdd:cd00401  81 GIPVFAWKGETEEEYWWCIEQAL---DHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 252 PAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMD 331
Cdd:cd00401 158 PAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMD 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 332 GFRVVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKR 411
Cdd:cd00401 238 GFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRR 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 412 IVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQA 490
Cdd:cd00401 318 IILLAEGRLVNLACATgHPSFVMDMSFANQALAQIELWKNR-DKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQA 396


                ....*.
gi 26343517 491 KYLGLN 496
Cdd:cd00401 397 EYLGSW 402
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 82-502 0e+00

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 682.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   82 DFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTL 161
Cdd:PRK05476   7 DYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNPFSTQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  162 NEVAAALAESGFPVFAWKGESEDDFWWCIDRCVnvEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLY 241
Cdd:PRK05476  87 DDVAAALAAAGIPVFAWKGETLEEYWECIERAL--DGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGVHRLY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  242 QLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEID 321
Cdd:PRK05476 165 AMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVD 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  322 PICALQACMDGFRVVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQV 401
Cdd:PRK05476 245 PICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKPQV 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  402 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 480
Cdd:PRK05476 325 DEYTLPDGKRIILLAEGRLVNLGAATgHPSEVMDMSFANQALAQIELFTNR-GKLEPGVYVLPKELDEEVARLKLKALGV 403

                        410       420
                 ....*....|....*....|..
gi 26343517  481 HLTELTDEQAKYLGLNKNGPFK 502
Cdd:PRK05476 404 KLDELTEEQAEYIGVWVEGPFK 425
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
82-500 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 675.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  82 DFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTL 161
Cdd:COG0499   5 DYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNPLSTQ 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 162 NEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNvegWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLY 241
Cdd:COG0499  85 DDVAAALAAAGIPVFAWKGETLEEYYWCIEQALD---HGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHRLR 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 242 QLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEID 321
Cdd:COG0499 162 AMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVD 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 322 PICALQACMDGFRVVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQV 401
Cdd:COG0499 242 PICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRPQV 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 402 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 480
Cdd:COG0499 322 DEYTLPDGRRIYLLAEGRLVNLAAATgHPSEVMDMSFANQALAQIYLVKNG-DKLEPGVYVLPKELDEEVARLKLEALGV 400

                       410       420
                ....*....|....*....|
gi 26343517 481 HLTELTDEQAKYLGLNKNGP 500
Cdd:COG0499 401 KIDTLTEEQAEYLGSWVEGP 420
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 92-500 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: 532.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    92 EFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAES 171
Cdd:TIGR00936   1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAALAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   172 -GFPVFAWKGESEDDFWWCIDRCVNVEgwqPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLC 250
Cdd:TIGR00936  81 aGIPVFAWRGETNEEYYWAIEQVLDHE---PNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   251 VPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACM 330
Cdd:TIGR00936 158 FPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   331 DGFRVVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGK 410
Cdd:TIGR00936 238 DGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   411 RIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQ 489
Cdd:TIGR00936 318 RIYLLAEGRLVNLAAAEgHPSEVMDMSFANQALAAEYLWKNH-DKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQ 396

                         410
                  ....*....|.
gi 26343517   490 AKYLGLNKNGP 500
Cdd:TIGR00936 397 KEYLGSWEEGT 407
 
Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
84-507 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 880.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517     84 CVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNE 163
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    164 VAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQ 242
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPdGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    243 LSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDP 322
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    323 ICALQACMDGFRVVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRT-PELTWERVRSQV 401
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    402 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 480
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEKLGA 399

                          410       420
                   ....*....|....*....|....*..
gi 26343517    481 HLTELTDEQAKYLGLNKNGPFKPNYYR 507
Cdd:smart00996 400 KLTKLTKEQADYIGVPVEGPFKPDHYR 426
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
82-507 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 838.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    82 DFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTL 161
Cdd:pfam05221   1 DYKVADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   162 NEVAAALAESGFPVFAWKGESEDDFWWCIDRCVN--VEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHR 239
Cdd:pfam05221  81 DHAAAAIAAAGVPVFAWKGETLEEYWWCTEQALTwpPDGGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   240 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTE 319
Cdd:pfam05221 161 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   320 IDPICALQACMDGFRVVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCN--MGHSNTEIDVASLRTPELTWERV 397
Cdd:pfam05221 241 IDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNigHFDNEIDEIVLALLKGVKWVNIK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   398 RsQVDHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNaPEGRYKQDVYLLPKKMDEYVASLHLP 476
Cdd:pfam05221 321 P-QVDDITFPDGKSIIVLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELWT-NDKEYENGVYVLPKKLDEKVARLHLE 398

                         410       420       430
                  ....*....|....*....|....*....|.
gi 26343517   477 TFDAHLTELTDEQAKYLGLNKNGPFKPNYYR 507
Cdd:pfam05221 399 KLGAKLTELTKEQADYIGVPVEGPFKPDHYR 429
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 92-496 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: 761.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  92 EFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAES 171
Cdd:cd00401   1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 172 GFPVFAWKGESEDDFWWCIDRCVnveGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCV 251
Cdd:cd00401  81 GIPVFAWKGETEEEYWWCIEQAL---DHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 252 PAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMD 331
Cdd:cd00401 158 PAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMD 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 332 GFRVVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKR 411
Cdd:cd00401 238 GFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRR 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 412 IVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQA 490
Cdd:cd00401 318 IILLAEGRLVNLACATgHPSFVMDMSFANQALAQIELWKNR-DKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQA 396


                ....*.
gi 26343517 491 KYLGLN 496
Cdd:cd00401 397 EYLGSW 402
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 82-502 0e+00

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 682.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   82 DFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTL 161
Cdd:PRK05476   7 DYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNPFSTQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  162 NEVAAALAESGFPVFAWKGESEDDFWWCIDRCVnvEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLY 241
Cdd:PRK05476  87 DDVAAALAAAGIPVFAWKGETLEEYWECIERAL--DGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGVHRLY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  242 QLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEID 321
Cdd:PRK05476 165 AMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVD 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  322 PICALQACMDGFRVVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQV 401
Cdd:PRK05476 245 PICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKPQV 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  402 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 480
Cdd:PRK05476 325 DEYTLPDGKRIILLAEGRLVNLGAATgHPSEVMDMSFANQALAQIELFTNR-GKLEPGVYVLPKELDEEVARLKLKALGV 403

                        410       420
                 ....*....|....*....|..
gi 26343517  481 HLTELTDEQAKYLGLNKNGPFK 502
Cdd:PRK05476 404 KLDELTEEQAEYIGVWVEGPFK 425
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
82-500 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 675.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  82 DFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTL 161
Cdd:COG0499   5 DYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNPLSTQ 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 162 NEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNvegWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLY 241
Cdd:COG0499  85 DDVAAALAAAGIPVFAWKGETLEEYYWCIEQALD---HGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHRLR 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 242 QLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEID 321
Cdd:COG0499 162 AMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVD 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 322 PICALQACMDGFRVVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQV 401
Cdd:COG0499 242 PICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRPQV 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 402 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 480
Cdd:COG0499 322 DEYTLPDGRRIYLLAEGRLVNLAAATgHPSEVMDMSFANQALAQIYLVKNG-DKLEPGVYVLPKELDEEVARLKLEALGV 400

                       410       420
                ....*....|....*....|
gi 26343517 481 HLTELTDEQAKYLGLNKNGP 500
Cdd:COG0499 401 KIDTLTEEQAEYLGSWVEGP 420
PTZ00075 PTZ00075
Adenosylhomocysteinase; Provisional
 81-508 0e+00

Adenosylhomocysteinase; Provisional


Pssm-ID: 240258  Cd Length: 476  Bit Score: 608.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   81 SDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYST 160
Cdd:PTZ00075   3 TDYKVKDISLAEFGRKEIELAENEMPGLMALREEYGPSKPLKGARITGCLHMTVQTAVLIETLKALGAEVRWCSCNIFST 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  161 LNEVAAALAESGF-PVFAWKGESEDDFWWCIDRCVNvegWQ----PNMILDDGGDLTHWIYK------------------ 217
Cdd:PTZ00075  83 QDHAAAAIAKAGSvPVFAWKGETLEEYWWCTEQALK---WPngdgPNLIVDDGGDATLLVHEgvkaeklyeekgilpdpl 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  218 -----------------------KYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRES 274
Cdd:PTZ00075 160 dpsnedekclltvlkklltknpdKWTNLVKKIVGVSEETTTGVHRLYKMLKKGELLFPAINVNDSVTKSKFDNIYGCRHS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  275 ILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRVVKLNEVIRQVDIVITCTGN 354
Cdd:PTZ00075 240 LIDGIFRATDVMIAGKTVVVCGYGDVGKGCAQALRGFGARVVVTEIDPICALQAAMEGYQVVTLEDVVETADIFVTATGN 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  355 KNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRT-PELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCST-VPTFV 432
Cdd:PTZ00075 320 KDIITLEHMRRMKNNAIVGNIGHFDNEIQVAELEAyPGIEIVEIKPQVDRYTFPDGKGIILLAEGRLVNLGCATgHPSFV 399

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26343517  433 LSITATTQALALIELY-NAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPFKPNYYRY 508
Cdd:PTZ00075 400 MSNSFTNQVLAQIELWeNRDTGKYPNGVYKLPKELDEKVARLHLKKLGAKLTKLTDKQAEYIGVPVDGPYKSDHYRY 476
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 92-500 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: 532.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    92 EFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAES 171
Cdd:TIGR00936   1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAALAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   172 -GFPVFAWKGESEDDFWWCIDRCVNVEgwqPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLC 250
Cdd:TIGR00936  81 aGIPVFAWRGETNEEYYWAIEQVLDHE---PNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   251 VPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACM 330
Cdd:TIGR00936 158 FPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   331 DGFRVVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGK 410
Cdd:TIGR00936 238 DGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   411 RIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQ 489
Cdd:TIGR00936 318 RIYLLAEGRLVNLAAAEgHPSEVMDMSFANQALAAEYLWKNH-DKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQ 396

                         410
                  ....*....|.
gi 26343517   490 AKYLGLNKNGP 500
Cdd:TIGR00936 397 KEYLGSWEEGT 407
PLN02494 PLN02494
adenosylhomocysteinase
 82-508 0e+00

adenosylhomocysteinase


Pssm-ID: 178111 [Multi-domain]  Cd Length: 477  Bit Score: 518.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   82 DFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTL 161
Cdd:PLN02494   5 EYKVKDMSQADFGRLEIELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNIFSTQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  162 NEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIY------------------------ 216
Cdd:PLN02494  85 DHAAAAIARDSAAVFAWKGETLQEYWWCTERALDWGpGGGPDLIVDDGGDATLLIHegvkaeeefekdgtlpdptstdna 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  217 -----------------KKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGL 279
Cdd:PLN02494 165 efkivltiikdglkvdpKKYHKMKERLVGVSEETTTGVKRLYQMQKNGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDGL 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  280 KRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRVVKLNEVIRQVDIVITCTGNKNVVT 359
Cdd:PLN02494 245 MRATDVMIAGKVAVICGYGDVGKGCAAAMKAAGARVIVTEIDPICALQALMEGYQVLTLEDVVSEADIFVTTTGNKDIIM 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  360 REHLDRMKNSCIVCNMGHSNTEIDVASLRT-PELTWERVRSQVDHVIWPDGKR-IVLLAEGRLLNLSCST-VPTFVLSIT 436
Cdd:PLN02494 325 VDHMRKMKNNAIVCNIGHFDNEIDMLGLETyPGVKRITIKPQTDRWVFPDTGSgIIVLAEGRLMNLGCATgHPSFVMSCS 404

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26343517  437 ATTQALALIELYNAPE-GRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPFKPNYYRY 508
Cdd:PLN02494 405 FTNQVIAQLELWNEKKsGKYEKKVYVLPKHLDEKVAALHLGKLGAKLTKLSKDQADYINVPVEGPYKPAHYRY 477
AdoHcyase_NAD pfam00670
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
267-427 1.90e-106

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


Pssm-ID: 395543 [Multi-domain]  Cd Length: 162  Bit Score: 314.29  E-value: 1.90e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   267 NLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRVVKLNEVIRQVD 346
Cdd:pfam00670   1 NLYGCRESLIDGIKRATDVMIAGKVAVVCGYGDVGKGCAASLKGQGARVIVTEIDPICALQAAMEGFQVVTLEEVVDKAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   347 IVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCS 426
Cdd:pfam00670  81 IFVTTTGNKDIITGEHMAKMKNDAIVCNIGHFDNEIDVAWLEANGKKKENIKPQVDRYTLPDGKHIILLAEGRLVNLGCA 160


                  .
gi 26343517   427 T 427
Cdd:pfam00670 161 T 161
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
267-428 2.23e-104

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


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 309.00  E-value: 2.23e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    267 NLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRVVKLNEVIRQVD 346
Cdd:smart00997   1 NRYGTGESLLDGILRATNVLLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPIRALEAAMDGFEVMKMEEAAKRAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    347 IVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCS 426
Cdd:smart00997  81 IFVTATGNKDVITREHFRAMKDGAILANAGHFDVEIDVAALEELAVEKREVRPQVDEYTLPDGKRIYLLAEGRLVNLAAA 160


                   ..
gi 26343517    427 TV 428
Cdd:smart00997 161 TG 162
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 126-447 2.06e-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: 142.37  E-value: 2.06e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 126 IVGCTHITAQTA------VLMETLGALGAQCRWAACNIYSTLNEVAAALAEsgfpvfawkgeseddfwWCIDRCVNVEGW 199
Cdd:cd12154   1 IAGPKEIKNEEFrvglspSVVATLVEAGHEVRVETGAGIGAGFADQAYVQA-----------------GAIVVTLAKALW 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 200 QPNMILDDGGDLTHWIYKkypnMFKK--IKGIVEESVTGVHRLY--QLSKAGklcVPAMNVNDSVTKQKFDNLYCCRESI 275
Cdd:cd12154  64 SLDVVLKVKEPLTNAEYA----LIQKlgDRLLFTYTIGADHRDLteALARAG---LTAIAVEGVELPLLTSNSIGAGELS 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 276 LDGLKRTTDMMFGG----------KQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDG-FRVVKLNEVIRQ 344
Cdd:cd12154 137 VQFIARFLEVQQPGrlggapdvagKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGgKNVEELEEALAE 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 345 VDIVITCTGNKN-----VVTREHLDRMKNSCIVCNMGHSNTEIDVASLrtPELTWErvrsqvdhviwpdGKRIVLLAEGR 419
Cdd:cd12154 217 ADVIVTTTLLPGkragiLVPEELVEQMKPGSVIVNVAVGAVGCVQALH--TQLLEE-------------GHGVVHYGDVN 281

                       330       340
                ....*....|....*....|....*....
gi 26343517 420 LLNLSC-STVPTFVLSITATTQALALIEL 447
Cdd:cd12154 282 MPGPGCaMGVPWDATLRLAANTLPALVKL 310
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 290-419 1.99e-08

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: 55.84  E-value: 1.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 290 KQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRVVKLN----EV-----IRQVDIVITCTGN--KNVV 358
Cdd:COG0569  96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDatdeEVleeagIEDADAVIAATGDdeANIL 175

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26343517 359 TrehldrmknsCIVC-NMGHSNTeidVASLRTPELTWERVRSQVDHVIWPD---GKRIVLLAEGR 419
Cdd:COG0569 176 A----------CLLAkELGVPRI---IARANDPEYADLLERLGADVVISPErlaARRIARLLLRP 227
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 292-372 1.32e-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: 50.97  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517    292 VVVCGYGEVGKGCCAALKAMGSIVYVTEIDP--ICALQACMDG-FRVVKLN-----EVIRQVDIVITC---TGNK--NVV 358
Cdd:smart01002  23 VVVIGAGVVGLGAAATAKGLGAEVTVLDVRParLRQLESLLGArFTTLYSQaelleEAVKEADLVIGAvliPGAKapKLV 102

                           90
                   ....*....|....*
gi 26343517    359 TREHLDRMK-NSCIV 372
Cdd:smart01002 103 TREMVKSMKpGSVIV 117
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 289-376 1.31e-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: 47.13  E-value: 1.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 289 GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQacmDGFRVV---KLNEVIRQVDIVITC------TgnKNVVT 359
Cdd:cd05300 134 GKTVLIVGLGDIGREIARRAKAFGMRVIGVRRSGRPAPP---VVDEVYtpdELDELLPEADYVVNAlpltpeT--RGLFN 208

                        90
                ....*....|....*..
gi 26343517 360 REHLDRMKNSCIVCNMG 376
Cdd:cd05300 209 AERFAAMKPGAVLINVG 225
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 273-365 2.10e-05

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 46.72  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  273 ESILDGLKrttdmmfgGKQVVVCGYGEVGKGCCAALKAMG-SIVYVT----EIdpicALQ-ACMDGFRVV---KLNEVIR 343
Cdd:PRK00045 174 KQIFGDLS--------GKKVLVIGAGEMGELVAKHLAEKGvRKITVAnrtlER----AEElAEEFGGEAIpldELPEALA 241

                         90       100
                 ....*....|....*....|...
gi 26343517  344 QVDIVITCTGNKN-VVTREHLDR 365
Cdd:PRK00045 242 EADIVISSTGAPHpIIGKGMVER 264
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 289-376 4.79e-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: 44.02  E-value: 4.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   289 GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRVVKLNEVIRQVDIV-ITCTGNK---NVVTREHLD 364
Cdd:pfam02826  36 GKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSLDELLAESDVVsLHLPLTPetrHLINAERLA 115

                          90
                  ....*....|..
gi 26343517   365 RMKNSCIVCNMG 376
Cdd:pfam02826 116 LMKPGAILINTA 127
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 273-365 1.28e-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: 44.33  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 273 ESILDGLKrttdmmfgGKQVVVCGYGEVGKGCCAALKAMG-SIVYVT-------EidpicALQACMDGfRVVKLNE---V 341
Cdd:COG0373 174 KKIFGDLS--------GKTVLVIGAGEMGELAARHLAAKGvKRITVAnrtleraE-----ELAEEFGG-EAVPLEElpeA 239

                        90       100
                ....*....|....*....|....*
gi 26343517 342 IRQVDIVITCTGNKN-VVTREHLDR 365
Cdd:COG0373 240 LAEADIVISSTGAPHpVITKEMVER 264
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 292-372 1.38e-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: 43.25  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   292 VVVCGYGEVGKGCCAALKAMGSIVYVTEIDP--ICALQACMDG--FRVVKLN-----EVIRQVDIVITC---TGNK--NV 357
Cdd:pfam01262  31 VLVIGGGVAGLNAAATAKGLGAIVTILDVRParLEQLESILGAkfVETLYSQaeliaEAVKEADLVIGTaliPGAKapKL 110

                          90
                  ....*....|....*.
gi 26343517   358 VTREHLDRMKN-SCIV 372
Cdd:pfam01262 111 VTREMVKSMKPgSVIV 126
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 289-374 1.62e-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: 43.77  E-value: 1.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 289 GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQAcMDGFRVVKLNEVIRQVDIVITCTG----NKNVVTREHLD 364
Cdd:cd05198 140 GKTVGIVGLGRIGQRVAKRLQAFGMKVLYYDRTRKPEPEE-DLGFRVVSLDELLAQSDVVVLHLPltpeTRHLINEEELA 218

                        90
                ....*....|
gi 26343517 365 RMKNSCIVCN 374
Cdd:cd05198 219 LMKPGAVLVN 228
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 273-353 3.60e-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: 42.64  E-value: 3.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 273 ESILDGLKrttdmmfgGKQVVVCGYGEVGKGCCAALKAMG-SIVYVTEIDPICALQ-ACMDGFRVVKLNEV---IRQVDI 347
Cdd:cd05213 170 EKIFGNLK--------GKKVLVIGAGEMGELAAKHLAAKGvAEITIANRTYERAEElAKELGGNAVPLDELlelLNEADV 241


                ....*.
gi 26343517 348 VITCTG 353
Cdd:cd05213 242 VISATG 247
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 286-376 3.96e-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: 42.62  E-value: 3.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 286 MFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFrVVKLNEVIRQVDIVITCT----GNKNVVTRE 361
Cdd:cd12165 134 ELRGKTVGILGYGHIGREIARLLKAFGMRVIGVSRSPKEDEGADFVGT-LSDLDEALEQADVVVVALpltkQTRGLIGAA 212

                        90
                ....*....|....*
gi 26343517 362 HLDRMKNSCIVCNMG 376
Cdd:cd12165 213 ELAAMKPGAILVNVG 227
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 292-354 7.91e-04

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: 39.05  E-value: 7.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26343517   292 VVVCGYGEVGKGCCAALKAMGSIVyVTEIDPICALQACMDGFRVVKLN----EV-----IRQVDIVITCTGN 354
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSEGGDVV-VIDKDEERVEELREEGVPVVVGDatdeEVleeagIEEADAVIAATGD 71
PLN02928 PLN02928
oxidoreductase family protein
 289-376 1.02e-03

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 41.20  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  289 GKQVVVCGYGEVGKGCCAALKAMGSIVYVT------EIDPICALQACMDGFRVVK------LNEVIRQVDIVITC----T 352
Cdd:PLN02928 159 GKTVFILGYGAIGIELAKRLRPFGVKLLATrrswtsEPEDGLLIPNGDVDDLVDEkgghedIYEFAGEADIVVLCctltK 238

                         90       100
                 ....*....|....*....|....
gi 26343517  353 GNKNVVTREHLDRMKNSCIVCNMG 376
Cdd:PLN02928 239 ETAGIVNDEFLSSMKKGALLVNIA 262
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 278-372 1.15e-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: 40.27  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 278 GLKRTTDMMFG-----GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQAC-MDGFRVVKLNEVIRQ-VDIVIT 350
Cdd:cd01075  12 GMKAAAEHLLGtdsleGKTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAeLFGATVVAPEEIYSVdADVFAP 91

                        90       100
                ....*....|....*....|..
gi 26343517 351 CtGNKNVVTREHLDRMKNSCIV 372
Cdd:cd01075  92 C-ALGGVINDDTIPQLKAKAIA 112
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 289-354 1.30e-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: 40.94  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 289 GKQVVVCGYGEVGKGCCAALKAMG-SIVYVTEIDP-------------ICALQACMDGFRVVKLNEVI--RQVDIVITCT 352
Cdd:cd05285 163 GDTVLVFGAGPIGLLTAAVAKAFGaTKVVVTDIDPsrlefakelgathTVNVRTEDTPESAEKIAELLggKGPDVVIECT 242


                ..
gi 26343517 353 GN 354
Cdd:cd05285 243 GA 244
PRK08306 PRK08306
dipicolinate synthase subunit DpsA;
289-386 1.34e-03

dipicolinate synthase subunit DpsA;


Pssm-ID: 181371 [Multi-domain]  Cd Length: 296  Bit Score: 40.59  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517  289 GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPiCALQACMD-GFRVVKLNEV---IRQVDIVItctgnkN-----VVT 359
Cdd:PRK08306 152 GSNVLVLGFGRTGMTLARTLKALGANVTVGARKS-AHLARITEmGLSPFHLSELaeeVGKIDIIF------NtipalVLT 224

                         90       100
                 ....*....|....*....|....*..
gi 26343517  360 REHLDRMKNSCIVcnmghsnteIDVAS 386
Cdd:PRK08306 225 KEVLSKMPPEALI---------IDLAS 242
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 287-374 1.51e-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: 40.77  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 287 FGGKQVVVCGYGEVGKgCCAALKAMGSIVYVTEIDP-ICALQACMDGFRVVKLNEVIRQVDIVITC----TGNKNVVTRE 361
Cdd:cd12177 145 LSGKTVGIIGYGNIGS-RVAEILKEGFNAKVLAYDPyVSEEVIKKKGAKPVSLEELLAESDIISLHapltEETYHMINEK 223

                        90
                ....*....|...
gi 26343517 362 HLDRMKNSCIVCN 374
Cdd:cd12177 224 AFSKMKKGVILVN 236
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 272-376 1.92e-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: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 40.25  E-value: 1.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 272 RESILDGLKRTTD----MMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRVVKLNEVIRQVDI 347
Cdd:cd12175 121 DRELRAGRWGRPEgrpsRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFRDPEAEEKDLGVRYVELDELLAESDV 200

                        90       100       110
                ....*....|....*....|....*....|...
gi 26343517 348 VITCT----GNKNVVTREHLDRMKNSCIVCNMG 376
Cdd:cd12175 201 VSLHVpltpETRHLIGAEELAAMKPGAILINTA 233
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 273-367 2.72e-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: 38.32  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517   273 ESILDGLKrttdmmfgGKQVVVCGYGEVGKGCCAALKAMGsivyVTEI-------DPICALQACMDGFRVVKLNEV---I 342
Cdd:pfam01488   4 KKIFGDLK--------DKKVLLIGAGEMGELVAKHLLAKG----AKEVtianrtiERAQELAEKFGGVEALPLDDLkeyL 71

                          90       100
                  ....*....|....*....|....*.
gi 26343517   343 RQVDIVITCTGNKN-VVTREHLDRMK 367
Cdd:pfam01488  72 AEADIVISATSSPTpIITKEMVERAL 97
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 287-368 9.48e-03

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 38.39  E-value: 9.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343517 287 FGGKQVVVCGYGEVGKGCCAALKAMG-SIVYVTE-------------IDPICALQACMDGFRVVKLNEV--IRQVDIVIT 350
Cdd:cd08231 176 GAGDTVVVQGAGPLGLYAVAAAKLAGaRRVIVIDgsperlelarefgADATIDIDELPDPQRRAIVRDItgGRGADVVIE 255

                        90
                ....*....|....*...
gi 26343517 351 CTGNKNVVtREHLDRMKN 368
Cdd:cd08231 256 ASGHPAAV-PEGLELLRR 272
 
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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