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Conserved domains on  [gi|342307099|ref|NP_067389|]
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putative adenosylhomocysteinase 3 isoform 1 [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;
189-612 0e+00

S-adenosyl-L-homocysteine hydrolase;


:

Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 877.26  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   189 CVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNE 268
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   269 VAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQ 347
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPdGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   348 LSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDP 427
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   428 ICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRT-PELTWERVRSQV 506
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   507 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 585
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEKLGA 399

                          410       420
                   ....*....|....*....|....*..
gi 342307099   586 HLTELTDEQAKYLGLNKNGPFKPNYYR 612
Cdd:smart00996 400 KLTKLTKEQADYIGVPVEGPFKPDHYR 426
 
Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
189-612 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 877.26  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   189 CVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNE 268
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   269 VAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQ 347
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPdGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   348 LSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDP 427
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   428 ICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRT-PELTWERVRSQV 506
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   507 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 585
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEKLGA 399

                          410       420
                   ....*....|....*....|....*..
gi 342307099   586 HLTELTDEQAKYLGLNKNGPFKPNYYR 612
Cdd:smart00996 400 KLTKLTKEQADYIGVPVEGPFKPDHYR 426
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
187-612 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 835.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  187 DFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTL 266
Cdd:pfam05221   1 DYKVADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  267 NEVAAALAESGFPVFAWKGESEDDFWWCIDRCVN--VEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHR 344
Cdd:pfam05221  81 DHAAAAIAAAGVPVFAWKGETLEEYWWCTEQALTwpPDGGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  345 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTE 424
Cdd:pfam05221 161 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  425 IDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCN--MGHSNTEIDVASLRTPELTWERV 502
Cdd:pfam05221 241 IDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNigHFDNEIDEIVLALLKGVKWVNIK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  503 RsQVDHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNaPEGRYKQDVYLLPKKMDEYVASLHLP 581
Cdd:pfam05221 321 P-QVDDITFPDGKSIIVLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELWT-NDKEYENGVYVLPKKLDEKVARLHLE 398

                         410       420       430
                  ....*....|....*....|....*....|.
gi 342307099  582 TFDAHLTELTDEQAKYLGLNKNGPFKPNYYR 612
Cdd:pfam05221 399 KLGAKLTELTKEQADYIGVPVEGPFKPDHYR 429
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 197-601 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: 755.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 197 EFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAES 276
Cdd:cd00401    1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 277 GFPVFAWKGESEDDFWWCIDRCVnveGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCV 356
Cdd:cd00401   81 GIPVFAWKGETEEEYWWCIEQAL---DHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 357 PAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMD 436
Cdd:cd00401  158 PAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMD 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 437 GFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKR 516
Cdd:cd00401  238 GFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRR 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 517 IVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQA 595
Cdd:cd00401  318 IILLAEGRLVNLACATgHPSFVMDMSFANQALAQIELWKNR-DKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQA 396


                 ....*.
gi 342307099 596 KYLGLN 601
Cdd:cd00401  397 EYLGSW 402
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 187-607 0e+00

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 675.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 187 DFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTL 266
Cdd:PRK05476   7 DYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNPFSTQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 267 NEVAAALAESGFPVFAWKGESEDDFWWCIDRCVnvEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLY 346
Cdd:PRK05476  87 DDVAAALAAAGIPVFAWKGETLEEYWECIERAL--DGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGVHRLY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 347 QLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEID 426
Cdd:PRK05476 165 AMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVD 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 427 PICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQV 506
Cdd:PRK05476 245 PICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKPQV 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 507 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 585
Cdd:PRK05476 325 DEYTLPDGKRIILLAEGRLVNLGAATgHPSEVMDMSFANQALAQIELFTNR-GKLEPGVYVLPKELDEEVARLKLKALGV 403

                        410       420
                 ....*....|....*....|..
gi 342307099 586 HLTELTDEQAKYLGLNKNGPFK 607
Cdd:PRK05476 404 KLDELTEEQAEYIGVWVEGPFK 425
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
187-605 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 668.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 187 DFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTL 266
Cdd:COG0499    5 DYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNPLSTQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 267 NEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNvegWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLY 346
Cdd:COG0499   85 DDVAAALAAAGIPVFAWKGETLEEYYWCIEQALD---HGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHRLR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 347 QLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEID 426
Cdd:COG0499  162 AMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVD 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 427 PICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQV 506
Cdd:COG0499  242 PICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRPQV 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 507 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 585
Cdd:COG0499  322 DEYTLPDGRRIYLLAEGRLVNLAAATgHPSEVMDMSFANQALAQIYLVKNG-DKLEPGVYVLPKELDEEVARLKLEALGV 400

                        410       420
                 ....*....|....*....|
gi 342307099 586 HLTELTDEQAKYLGLNKNGP 605
Cdd:COG0499  401 KIDTLTEEQAEYLGSWVEGP 420
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 197-605 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: 530.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  197 EFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAES 276
Cdd:TIGR00936   1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAALAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  277 -GFPVFAWKGESEDDFWWCIDRCVNVEgwqPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLC 355
Cdd:TIGR00936  81 aGIPVFAWRGETNEEYYWAIEQVLDHE---PNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  356 VPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACM 435
Cdd:TIGR00936 158 FPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  436 DGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGK 515
Cdd:TIGR00936 238 DGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  516 RIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQ 594
Cdd:TIGR00936 318 RIYLLAEGRLVNLAAAEgHPSEVMDMSFANQALAAEYLWKNH-DKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQ 396

                         410
                  ....*....|.
gi 342307099  595 AKYLGLNKNGP 605
Cdd:TIGR00936 397 KEYLGSWEEGT 407
 
Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
189-612 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 877.26  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   189 CVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNE 268
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   269 VAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQ 347
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPdGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   348 LSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDP 427
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   428 ICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRT-PELTWERVRSQV 506
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   507 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 585
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEKLGA 399

                          410       420
                   ....*....|....*....|....*..
gi 342307099   586 HLTELTDEQAKYLGLNKNGPFKPNYYR 612
Cdd:smart00996 400 KLTKLTKEQADYIGVPVEGPFKPDHYR 426
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
187-612 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 835.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  187 DFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTL 266
Cdd:pfam05221   1 DYKVADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  267 NEVAAALAESGFPVFAWKGESEDDFWWCIDRCVN--VEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHR 344
Cdd:pfam05221  81 DHAAAAIAAAGVPVFAWKGETLEEYWWCTEQALTwpPDGGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  345 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTE 424
Cdd:pfam05221 161 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  425 IDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCN--MGHSNTEIDVASLRTPELTWERV 502
Cdd:pfam05221 241 IDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNigHFDNEIDEIVLALLKGVKWVNIK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  503 RsQVDHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNaPEGRYKQDVYLLPKKMDEYVASLHLP 581
Cdd:pfam05221 321 P-QVDDITFPDGKSIIVLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELWT-NDKEYENGVYVLPKKLDEKVARLHLE 398

                         410       420       430
                  ....*....|....*....|....*....|.
gi 342307099  582 TFDAHLTELTDEQAKYLGLNKNGPFKPNYYR 612
Cdd:pfam05221 399 KLGAKLTELTKEQADYIGVPVEGPFKPDHYR 429
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 197-601 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: 755.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 197 EFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAES 276
Cdd:cd00401    1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 277 GFPVFAWKGESEDDFWWCIDRCVnveGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCV 356
Cdd:cd00401   81 GIPVFAWKGETEEEYWWCIEQAL---DHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 357 PAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMD 436
Cdd:cd00401  158 PAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMD 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 437 GFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKR 516
Cdd:cd00401  238 GFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRR 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 517 IVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQA 595
Cdd:cd00401  318 IILLAEGRLVNLACATgHPSFVMDMSFANQALAQIELWKNR-DKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQA 396


                 ....*.
gi 342307099 596 KYLGLN 601
Cdd:cd00401  397 EYLGSW 402
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 187-607 0e+00

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 675.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 187 DFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTL 266
Cdd:PRK05476   7 DYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNPFSTQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 267 NEVAAALAESGFPVFAWKGESEDDFWWCIDRCVnvEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLY 346
Cdd:PRK05476  87 DDVAAALAAAGIPVFAWKGETLEEYWECIERAL--DGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGVHRLY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 347 QLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEID 426
Cdd:PRK05476 165 AMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVD 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 427 PICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQV 506
Cdd:PRK05476 245 PICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKPQV 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 507 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 585
Cdd:PRK05476 325 DEYTLPDGKRIILLAEGRLVNLGAATgHPSEVMDMSFANQALAQIELFTNR-GKLEPGVYVLPKELDEEVARLKLKALGV 403

                        410       420
                 ....*....|....*....|..
gi 342307099 586 HLTELTDEQAKYLGLNKNGPFK 607
Cdd:PRK05476 404 KLDELTEEQAEYIGVWVEGPFK 425
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
187-605 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 668.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 187 DFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTL 266
Cdd:COG0499    5 DYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNPLSTQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 267 NEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNvegWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLY 346
Cdd:COG0499   85 DDVAAALAAAGIPVFAWKGETLEEYYWCIEQALD---HGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHRLR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 347 QLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEID 426
Cdd:COG0499  162 AMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVD 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 427 PICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQV 506
Cdd:COG0499  242 PICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRPQV 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 507 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 585
Cdd:COG0499  322 DEYTLPDGRRIYLLAEGRLVNLAAATgHPSEVMDMSFANQALAQIYLVKNG-DKLEPGVYVLPKELDEEVARLKLEALGV 400

                        410       420
                 ....*....|....*....|
gi 342307099 586 HLTELTDEQAKYLGLNKNGP 605
Cdd:COG0499  401 KIDTLTEEQAEYLGSWVEGP 420
PTZ00075 PTZ00075
Adenosylhomocysteinase; Provisional
 186-613 0e+00

Adenosylhomocysteinase; Provisional


Pssm-ID: 240258  Cd Length: 476  Bit Score: 609.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 186 SDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYST 265
Cdd:PTZ00075   3 TDYKVKDISLAEFGRKEIELAENEMPGLMALREEYGPSKPLKGARITGCLHMTVQTAVLIETLKALGAEVRWCSCNIFST 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 266 LNEVAAALAESGF-PVFAWKGESEDDFWWCIDRCVNvegWQ----PNMILDDGGDLTHWIYK------------------ 322
Cdd:PTZ00075  83 QDHAAAAIAKAGSvPVFAWKGETLEEYWWCTEQALK---WPngdgPNLIVDDGGDATLLVHEgvkaeklyeekgilpdpl 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 323 -----------------------KYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRES 379
Cdd:PTZ00075 160 dpsnedekclltvlkklltknpdKWTNLVKKIVGVSEETTTGVHRLYKMLKKGELLFPAINVNDSVTKSKFDNIYGCRHS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 380 ILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGN 459
Cdd:PTZ00075 240 LIDGIFRATDVMIAGKTVVVCGYGDVGKGCAQALRGFGARVVVTEIDPICALQAAMEGYQVVTLEDVVETADIFVTATGN 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 460 KNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRT-PELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCST-VPTFV 537
Cdd:PTZ00075 320 KDIITLEHMRRMKNNAIVGNIGHFDNEIQVAELEAyPGIEIVEIKPQVDRYTFPDGKGIILLAEGRLVNLGCATgHPSFV 399

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 342307099 538 LSITATTQALALIELY-NAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPFKPNYYRY 613
Cdd:PTZ00075 400 MSNSFTNQVLAQIELWeNRDTGKYPNGVYKLPKELDEKVARLHLKKLGAKLTKLTDKQAEYIGVPVDGPYKSDHYRY 476
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 197-605 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: 530.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  197 EFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAES 276
Cdd:TIGR00936   1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAALAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  277 -GFPVFAWKGESEDDFWWCIDRCVNVEgwqPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLC 355
Cdd:TIGR00936  81 aGIPVFAWRGETNEEYYWAIEQVLDHE---PNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  356 VPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACM 435
Cdd:TIGR00936 158 FPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  436 DGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGK 515
Cdd:TIGR00936 238 DGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  516 RIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQ 594
Cdd:TIGR00936 318 RIYLLAEGRLVNLAAAEgHPSEVMDMSFANQALAAEYLWKNH-DKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQ 396

                         410
                  ....*....|.
gi 342307099  595 AKYLGLNKNGP 605
Cdd:TIGR00936 397 KEYLGSWEEGT 407
PLN02494 PLN02494
adenosylhomocysteinase
 187-613 1.12e-178

adenosylhomocysteinase


Pssm-ID: 178111 [Multi-domain]  Cd Length: 477  Bit Score: 514.41  E-value: 1.12e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 187 DFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTL 266
Cdd:PLN02494   5 EYKVKDMSQADFGRLEIELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNIFSTQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 267 NEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIY------------------------ 321
Cdd:PLN02494  85 DHAAAAIARDSAAVFAWKGETLQEYWWCTERALDWGpGGGPDLIVDDGGDATLLIHegvkaeeefekdgtlpdptstdna 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 322 -----------------KKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGL 384
Cdd:PLN02494 165 efkivltiikdglkvdpKKYHKMKERLVGVSEETTTGVKRLYQMQKNGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDGL 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 385 KRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVT 464
Cdd:PLN02494 245 MRATDVMIAGKVAVICGYGDVGKGCAAAMKAAGARVIVTEIDPICALQALMEGYQVLTLEDVVSEADIFVTTTGNKDIIM 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 465 REHLDRMKNSCIVCNMGHSNTEIDVASLRT-PELTWERVRSQVDHVIWPDGKR-IVLLAEGRLLNLSCST-VPTFVLSIT 541
Cdd:PLN02494 325 VDHMRKMKNNAIVCNIGHFDNEIDMLGLETyPGVKRITIKPQTDRWVFPDTGSgIIVLAEGRLMNLGCATgHPSFVMSCS 404

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 342307099 542 ATTQALALIELYNAPE-GRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPFKPNYYRY 613
Cdd:PLN02494 405 FTNQVIAQLELWNEKKsGKYEKKVYVLPKHLDEKVAALHLGKLGAKLTKLSKDQADYINVPVEGPYKPAHYRY 477
AdoHcyase_NAD pfam00670
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
372-532 6.17e-105

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


Pssm-ID: 395543 [Multi-domain]  Cd Length: 162  Bit Score: 313.90  E-value: 6.17e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  372 NLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVD 451
Cdd:pfam00670   1 NLYGCRESLIDGIKRATDVMIAGKVAVVCGYGDVGKGCAASLKGQGARVIVTEIDPICALQAAMEGFQVVTLEEVVDKAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  452 IVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCS 531
Cdd:pfam00670  81 IFVTTTGNKDIITGEHMAKMKNDAIVCNIGHFDNEIDVAWLEANGKKKENIKPQVDRYTLPDGKHIILLAEGRLVNLGCA 160


                  .
gi 342307099  532 T 532
Cdd:pfam00670 161 T 161
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
372-533 4.33e-102

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


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 306.30  E-value: 4.33e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   372 NLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVD 451
Cdd:smart00997   1 NRYGTGESLLDGILRATNVLLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPIRALEAAMDGFEVMKMEEAAKRAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   452 IVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCS 531
Cdd:smart00997  81 IFVTATGNKDVITREHFRAMKDGAILANAGHFDVEIDVAALEELAVEKREVRPQVDEYTLPDGKRIYLLAEGRLVNLAAA 160


                   ..
gi 342307099   532 TV 533
Cdd:smart00997 161 TG 162
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 231-552 4.34e-36

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


Pssm-ID: 240631 [Multi-domain]  Cd Length: 310  Bit Score: 137.36  E-value: 4.34e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 231 IVGCTHITAQTA------VLMETLGALGAQCRWAACNIYSTLNEVAAALAEsgfpvfawkgeseddfwWCIDRCVNVEGW 304
Cdd:cd12154    1 IAGPKEIKNEEFrvglspSVVATLVEAGHEVRVETGAGIGAGFADQAYVQA-----------------GAIVVTLAKALW 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 305 QPNMILDDGGDLTHWIYKkypnMFKK--IKGIVEESVTGVHRLY--QLSKAGklcVPAMNVNDSVTKQKFDNLYCCRESI 380
Cdd:cd12154   64 SLDVVLKVKEPLTNAEYA----LIQKlgDRLLFTYTIGADHRDLteALARAG---LTAIAVEGVELPLLTSNSIGAGELS 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 381 LDGLKRTTDMMFGG----------KQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLV-KLNEVIRQ 449
Cdd:cd12154  137 VQFIARFLEVQQPGrlggapdvagKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKNVeELEEALAE 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 450 VDIVITCTGNKN-----VVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELtwervrsqvdhviwpDGKRIVLLAEGR 524
Cdd:cd12154  217 ADVIVTTTLLPGkragiLVPEELVEQMKPGSVIVNVAVGAVGCVQALHTQLLE---------------EGHGVVHYGDVN 281

                        330       340
                 ....*....|....*....|....*....
gi 342307099 525 LLNLSC-STVPTFVLSITATTQALALIEL 552
Cdd:cd12154  282 MPGPGCaMGVPWDATLRLAANTLPALVKL 310
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 395-524 1.96e-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: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 395 KQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLN----EV-----IRQVDIVITCTGN--KNVV 463
Cdd:COG0569   96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDatdeEVleeagIEDADAVIAATGDdeANIL 175

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342307099 464 TrehldrmknsCIVC-NMGHSNTeidVASLRTPELTWERVRSQVDHVIWPD---GKRIVLLAEGR 524
Cdd:COG0569  176 A----------CLLAkELGVPRI---IARANDPEYADLLERLGADVVISPErlaARRIARLLLRP 227
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 397-477 6.53e-07

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


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 49.04  E-value: 6.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099   397 VVVCGYGEVGKGCCAALKAMGSIVYVTEIDP--ICALQACMDG-FRLVKLN-----EVIRQVDIVITC---TGNK--NVV 463
Cdd:smart01002  23 VVVIGAGVVGLGAAATAKGLGAEVTVLDVRParLRQLESLLGArFTTLYSQaelleEAVKEADLVIGAvliPGAKapKLV 102

                           90
                   ....*....|....*
gi 342307099   464 TREHLDRMK-NSCIV 477
Cdd:smart01002 103 TREMVKSMKpGSVIV 117
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 378-470 7.20e-06

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 48.64  E-value: 7.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 378 ESILDGLKrttdmmfgGKQVVVCGYGEVGKGCCAALKAMG-SIVYVT----EIDPICALQACMDGFRLVKLNEVIRQVDI 452
Cdd:PRK00045 174 KQIFGDLS--------GKKVLVIGAGEMGELVAKHLAEKGvRKITVAnrtlERAEELAEEFGGEAIPLDELPEALAEADI 245

                         90
                 ....*....|....*....
gi 342307099 453 VITCTGNKN-VVTREHLDR 470
Cdd:PRK00045 246 VISSTGAPHpIIGKGMVER 264
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 394-481 2.72e-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: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 394 GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDIVITC------TgnKNVVTREH 467
Cdd:cd05300  134 GKTVLIVGLGDIGREIARRAKAFGMRVIGVRRSGRPAPPVVDEVYTPDELDELLPEADYVVNAlpltpeT--RGLFNAER 211

                         90
                 ....*....|....
gi 342307099 468 LDRMKNSCIVCNMG 481
Cdd:cd05300  212 FAAMKPGAVLINVG 225
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 394-481 8.06e-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: 8.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  394 GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDIV-ITCTGNK---NVVTREHLD 469
Cdd:pfam02826  36 GKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSLDELLAESDVVsLHLPLTPetrHLINAERLA 115

                          90
                  ....*....|..
gi 342307099  470 RMKNSCIVCNMG 481
Cdd:pfam02826 116 LMKPGAILINTA 127
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 378-470 3.40e-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: 3.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 378 ESILDGLKrttdmmfgGKQVVVCGYGEVGKGCCAALKAMG-SIVYVT-------EidpicALQACMDG--FRLVKLNEVI 447
Cdd:COG0373  174 KKIFGDLS--------GKTVLVIGAGEMGELAARHLAAKGvKRITVAnrtleraE-----ELAEEFGGeaVPLEELPEAL 240

                         90       100
                 ....*....|....*....|....
gi 342307099 448 RQVDIVITCTGNKN-VVTREHLDR 470
Cdd:COG0373  241 AEADIVISSTGAPHpVITKEMVER 264
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 397-477 5.31e-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: 41.71  E-value: 5.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099  397 VVVCGYGEVGKGCCAALKAMGSIVYVTEIDP--ICALQACMdGFRLVK--------LNEVIRQVDIVITC---TGNK--N 461
Cdd:pfam01262  31 VLVIGGGVAGLNAAATAKGLGAIVTILDVRParLEQLESIL-GAKFVEtlysqaelIAEAVKEADLVIGTaliPGAKapK 109

                          90
                  ....*....|....*..
gi 342307099  462 VVTREHLDRMKN-SCIV 477
Cdd:pfam01262 110 LVTREMVKSMKPgSVIV 126
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 391-481 5.57e-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: 5.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 391 MFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFrLVKLNEVIRQVDIVITCT----GNKNVVTRE 466
Cdd:cd12165  134 ELRGKTVGILGYGHIGREIARLLKAFGMRVIGVSRSPKEDEGADFVGT-LSDLDEALEQADVVVVALpltkQTRGLIGAA 212

                         90
                 ....*....|....*
gi 342307099 467 HLDRMKNSCIVCNMG 481
Cdd:cd12165  213 ELAAMKPGAILVNVG 227
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 394-479 6.16e-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: 6.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 394 GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQAcMDGFRLVKLNEVIRQVDIVITCTG----NKNVVTREHLD 469
Cdd:cd05198  140 GKTVGIVGLGRIGQRVAKRLQAFGMKVLYYDRTRKPEPEE-DLGFRVVSLDELLAQSDVVVLHLPltpeTRHLINEEELA 218

                         90
                 ....*....|
gi 342307099 470 RMKNSCIVCN 479
Cdd:cd05198  219 LMKPGAVLVN 228
PRK08306 PRK08306
dipicolinate synthase subunit DpsA;
394-491 6.87e-04

dipicolinate synthase subunit DpsA;


Pssm-ID: 181371 [Multi-domain]  Cd Length: 296  Bit Score: 42.13  E-value: 6.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 394 GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPicALQA-----CMDGFRLVKLNEVIRQVDIVItctgnkN-----VV 463
Cdd:PRK08306 152 GSNVLVLGFGRTGMTLARTLKALGANVTVGARKS--AHLAritemGLSPFHLSELAEEVGKIDIIF------NtipalVL 223

                         90       100
                 ....*....|....*....|....*...
gi 342307099 464 TREHLDRMKNSCIVcnmghsnteIDVAS 491
Cdd:PRK08306 224 TKEVLSKMPPEALI---------IDLAS 242
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 377-481 1.16e-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: 41.40  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 377 RESILDGLKRTTD----MMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDI 452
Cdd:cd12175  121 DRELRAGRWGRPEgrpsRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFRDPEAEEKDLGVRYVELDELLAESDV 200

                         90       100       110
                 ....*....|....*....|....*....|...
gi 342307099 453 VITCT----GNKNVVTREHLDRMKNSCIVCNMG 481
Cdd:cd12175  201 VSLHVpltpETRHLIGAEELAAMKPGAILINTA 233
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 378-458 1.21e-03

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: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 378 ESILDGLKrttdmmfgGKQVVVCGYGEVGKGCCAALKAMG-SIVYVTEIDPICALQ-ACMDGFRLVKLNEV---IRQVDI 452
Cdd:cd05213  170 EKIFGNLK--------GKKVLVIGAGEMGELAAKHLAAKGvAEITIANRTYERAEElAKELGGNAVPLDELlelLNEADV 241


                 ....*.
gi 342307099 453 VITCTG 458
Cdd:cd05213  242 VISATG 247
PLN02928 PLN02928
oxidoreductase family protein
 394-481 1.95e-03

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 40.82  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 394 GKQVVVCGYGEVGKGCCAALKAMGSIVYVT------EIDPICALQACmDGFRLV-------KLNEVIRQVDIVITC---- 456
Cdd:PLN02928 159 GKTVFILGYGAIGIELAKRLRPFGVKLLATrrswtsEPEDGLLIPNG-DVDDLVdekggheDIYEFAGEADIVVLCctlt 237

                         90       100
                 ....*....|....*....|....*
gi 342307099 457 TGNKNVVTREHLDRMKNSCIVCNMG 481
Cdd:PLN02928 238 KETAGIVNDEFLSSMKKGALLVNIA 262
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 392-479 2.97e-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: 2.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 392 FGGKQVVVCGYGEVGKgCCAALKAMGSIVYVTEIDP-ICALQACMDGFRLVKLNEVIRQVDIVITC----TGNKNVVTRE 466
Cdd:cd12177  145 LSGKTVGIIGYGNIGS-RVAEILKEGFNAKVLAYDPyVSEEVIKKKGAKPVSLEELLAESDIISLHapltEETYHMINEK 223

                         90
                 ....*....|...
gi 342307099 467 HLDRMKNSCIVCN 479
Cdd:cd12177  224 AFSKMKKGVILVN 236
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 394-459 5.06e-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: 5.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 394 GKQVVVCGYGEVGKGCCAALKAMG-SIVYVTEIDP-------------ICALQACMDGFRLVKLNEVI--RQVDIVITCT 457
Cdd:cd05285  163 GDTVLVFGAGPIGLLTAAVAKAFGaTKVVVTDIDPsrlefakelgathTVNVRTEDTPESAEKIAELLggKGPDVVIECT 242


                 ..
gi 342307099 458 GN 459
Cdd:cd05285  243 GA 244
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 383-477 8.08e-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: 37.96  E-value: 8.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342307099 383 GLKRTTDMMFG-----GKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQAC-MDGFRLVKLNEVIRQ-VDIVIT 455
Cdd:cd01075   12 GMKAAAEHLLGtdsleGKTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAeLFGATVVAPEEIYSVdADVFAP 91

                         90       100
                 ....*....|....*....|..
gi 342307099 456 CtGNKNVVTREHLDRMKNSCIV 477
Cdd:cd01075   92 C-ALGGVINDDTIPQLKAKAIA 112
 
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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