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Conserved domains on  [gi|41386739|ref|NP_958497|]
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adenosylhomocysteinase like 2b [Danio rerio]

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;
167-590 0e+00

S-adenosyl-L-homocysteine hydrolase;


:

Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 876.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    167 CIKNIKQADFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYSTQNE 246
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    247 VAAALAEGGFSVFAWKGESEDDFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQ 325
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPdGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    326 LSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDP 405
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    406 ICALQACMDGFRLVKLSEVIRQVDIVITCTGNKNVVVREYMDRMKNGCIVCNMGHSNTEIDVASLRT-PELTWERVRSQV 484
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    485 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 563
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEKLGA 399

                          410       420
                   ....*....|....*....|....*..
gi 41386739    564 HLTELSDEQAKYLGLNKNGPFKPNYYR 590
Cdd:smart00996 400 KLTKLTKEQADYIGVPVEGPFKPDHYR 426
 
Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
167-590 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 876.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    167 CIKNIKQADFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYSTQNE 246
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    247 VAAALAEGGFSVFAWKGESEDDFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQ 325
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPdGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    326 LSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDP 405
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    406 ICALQACMDGFRLVKLSEVIRQVDIVITCTGNKNVVVREYMDRMKNGCIVCNMGHSNTEIDVASLRT-PELTWERVRSQV 484
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    485 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 563
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEKLGA 399

                          410       420
                   ....*....|....*....|....*..
gi 41386739    564 HLTELSDEQAKYLGLNKNGPFKPNYYR 590
Cdd:smart00996 400 KLTKLTKEQADYIGVPVEGPFKPDHYR 426
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
165-590 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 41386739   165 DFCIKNIKQADFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYSTQ 244
Cdd:pfam05221   1 DYKVADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   245 NEVAAALAEGGFSVFAWKGESEDDFWWCIDRCVN--VEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHR 322
Cdd:pfam05221  81 DHAAAAIAAAGVPVFAWKGETLEEYWWCTEQALTwpPDGGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   323 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTE 402
Cdd:pfam05221 161 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   403 IDPICALQACMDGFRLVKLSEVIRQVDIVITCTGNKNVVVREYMDRMK--NGCIVCNMGHSNTEIDVASLRTPELTWERV 480
Cdd:pfam05221 241 IDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKmmAIVCNIGHFDNEIDEIVLALLKGVKWVNIK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   481 RsQVDHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNaPEGRYKQDVYLLPKKMDEYVASLHLP 559
Cdd:pfam05221 321 P-QVDDITFPDGKSIIVLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELWT-NDKEYENGVYVLPKKLDEKVARLHLE 398

                         410       420       430
                  ....*....|....*....|....*....|.
gi 41386739   560 TFDAHLTELSDEQAKYLGLNKNGPFKPNYYR 590
Cdd:pfam05221 399 KLGAKLTELTKEQADYIGVPVEGPFKPDHYR 429
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 175-579 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: 754.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 175 DFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYSTQNEVAAALAEG 254
Cdd:cd00401   1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 255 GFSVFAWKGESEDDFWWCIDRCVnveGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCV 334
Cdd:cd00401  81 GIPVFAWKGETEEEYWWCIEQAL---DHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 335 PAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACMD 414
Cdd:cd00401 158 PAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMD 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 415 GFRLVKLSEVIRQVDIVITCTGNKNVVVREYMDRMKNGCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKR 494
Cdd:cd00401 238 GFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRR 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 495 IVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELSDEQA 573
Cdd:cd00401 318 IILLAEGRLVNLACATgHPSFVMDMSFANQALAQIELWKNR-DKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQA 396


                ....*.
gi 41386739 574 KYLGLN 579
Cdd:cd00401 397 EYLGSW 402
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 165-585 0e+00

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 678.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  165 DFCIKNIKQADFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYSTQ 244
Cdd:PRK05476   7 DYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNPFSTQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  245 NEVAAALAEGGFSVFAWKGESEDDFWWCIDRCVnvEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLY 324
Cdd:PRK05476  87 DDVAAALAAAGIPVFAWKGETLEEYWECIERAL--DGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGVHRLY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  325 QLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEID 404
Cdd:PRK05476 165 AMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVD 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  405 PICALQACMDGFRLVKLSEVIRQVDIVITCTGNKNVVVREYMDRMKNGCIVCNMGHSNTEIDVASLRTPELTWERVRSQV 484
Cdd:PRK05476 245 PICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKPQV 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  485 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 563
Cdd:PRK05476 325 DEYTLPDGKRIILLAEGRLVNLGAATgHPSEVMDMSFANQALAQIELFTNR-GKLEPGVYVLPKELDEEVARLKLKALGV 403

                        410       420
                 ....*....|....*....|..
gi 41386739  564 HLTELSDEQAKYLGLNKNGPFK 585
Cdd:PRK05476 404 KLDELTEEQAEYIGVWVEGPFK 425
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
165-583 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 670.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 165 DFCIKNIKQADFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYSTQ 244
Cdd:COG0499   5 DYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNPLSTQ 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 245 NEVAAALAEGGFSVFAWKGESEDDFWWCIDRCVNvegWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLY 324
Cdd:COG0499  85 DDVAAALAAAGIPVFAWKGETLEEYYWCIEQALD---HGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHRLR 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 325 QLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEID 404
Cdd:COG0499 162 AMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVD 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 405 PICALQACMDGFRLVKLSEVIRQVDIVITCTGNKNVVVREYMDRMKNGCIVCNMGHSNTEIDVASLRTPELTWERVRSQV 484
Cdd:COG0499 242 PICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRPQV 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 485 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 563
Cdd:COG0499 322 DEYTLPDGRRIYLLAEGRLVNLAAATgHPSEVMDMSFANQALAQIYLVKNG-DKLEPGVYVLPKELDEEVARLKLEALGV 400

                       410       420
                ....*....|....*....|
gi 41386739 564 HLTELSDEQAKYLGLNKNGP 583
Cdd:COG0499 401 KIDTLTEEQAEYLGSWVEGP 420
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 175-583 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 41386739   175 DFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYSTQNEVAAALAEG 254
Cdd:TIGR00936   1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAALAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   255 -GFSVFAWKGESEDDFWWCIDRCVNVEgwqPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLC 333
Cdd:TIGR00936  81 aGIPVFAWRGETNEEYYWAIEQVLDHE---PNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   334 VPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACM 413
Cdd:TIGR00936 158 FPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   414 DGFRLVKLSEVIRQVDIVITCTGNKNVVVREYMDRMKNGCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGK 493
Cdd:TIGR00936 238 DGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   494 RIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELSDEQ 572
Cdd:TIGR00936 318 RIYLLAEGRLVNLAAAEgHPSEVMDMSFANQALAAEYLWKNH-DKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQ 396

                         410
                  ....*....|.
gi 41386739   573 AKYLGLNKNGP 583
Cdd:TIGR00936 397 KEYLGSWEEGT 407
 
Name Accession Description Interval E-value
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
167-590 0e+00

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 876.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    167 CIKNIKQADFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYSTQNE 246
Cdd:smart00996   1 KVADISLADWGRKEIEIAETEMPGLMALREEYGAEKPLKGARIAGCLHMTIQTAVLIETLVALGAEVRWASCNIFSTQDH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    247 VAAALAEGGFSVFAWKGESEDDFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQ 325
Cdd:smart00996  81 AAAAIAAAGVPVFAWKGETLEEYWWCIEQTLTWPdGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEETTTGVHRLYQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    326 LSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDP 405
Cdd:smart00996 161 MAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEIDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    406 ICALQACMDGFRLVKLSEVIRQVDIVITCTGNKNVVVREYMDRMKNGCIVCNMGHSNTEIDVASLRT-PELTWERVRSQV 484
Cdd:smart00996 241 ICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIDVASLRNnPGLKWENIKPQV 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    485 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 563
Cdd:smart00996 321 DHITFPDGKRIILLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELFTKP-GKYKNGVYVLPKKLDEKVARLHLEKLGA 399

                          410       420
                   ....*....|....*....|....*..
gi 41386739    564 HLTELSDEQAKYLGLNKNGPFKPNYYR 590
Cdd:smart00996 400 KLTKLTKEQADYIGVPVEGPFKPDHYR 426
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
165-590 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 41386739   165 DFCIKNIKQADFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYSTQ 244
Cdd:pfam05221   1 DYKVADISLADFGRKEIEIAEHEMPGLMALREEYGASKPLKGARIAGSLHMTIQTAVLIETLVALGAEVRWASCNIFSTQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   245 NEVAAALAEGGFSVFAWKGESEDDFWWCIDRCVN--VEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHR 322
Cdd:pfam05221  81 DHAAAAIAAAGVPVFAWKGETLEEYWWCTEQALTwpPDGGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   323 LYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTE 402
Cdd:pfam05221 161 LYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRATDVMIAGKVAVVCGYGDVGKGCAQSLRGQGARVIVTE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   403 IDPICALQACMDGFRLVKLSEVIRQVDIVITCTGNKNVVVREYMDRMK--NGCIVCNMGHSNTEIDVASLRTPELTWERV 480
Cdd:pfam05221 241 IDPICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKmmAIVCNIGHFDNEIDEIVLALLKGVKWVNIK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   481 RsQVDHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNaPEGRYKQDVYLLPKKMDEYVASLHLP 559
Cdd:pfam05221 321 P-QVDDITFPDGKSIIVLAEGRLVNLGCATgHPSFVMSNSFTNQVLAQIELWT-NDKEYENGVYVLPKKLDEKVARLHLE 398

                         410       420       430
                  ....*....|....*....|....*....|.
gi 41386739   560 TFDAHLTELSDEQAKYLGLNKNGPFKPNYYR 590
Cdd:pfam05221 399 KLGAKLTELTKEQADYIGVPVEGPFKPDHYR 429
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 175-579 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: 754.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 175 DFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYSTQNEVAAALAEG 254
Cdd:cd00401   1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCSCNPLSTQDDVAAALAEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 255 GFSVFAWKGESEDDFWWCIDRCVnveGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCV 334
Cdd:cd00401  81 GIPVFAWKGETEEEYWWCIEQAL---DHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLLF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 335 PAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACMD 414
Cdd:cd00401 158 PAIAVNDAVTKHKFDNRYGTGQSTIDGIKRATNVLIAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICALQAAMD 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 415 GFRLVKLSEVIRQVDIVITCTGNKNVVVREYMDRMKNGCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKR 494
Cdd:cd00401 238 GFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEELAVEKREIRPQVDEYTLPDGRR 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 495 IVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELSDEQA 573
Cdd:cd00401 318 IILLAEGRLVNLACATgHPSFVMDMSFANQALAQIELWKNR-DKLEPGVYVLPKELDEEVARLKLEALGIKLDKLTEEQA 396


                ....*.
gi 41386739 574 KYLGLN 579
Cdd:cd00401 397 EYLGSW 402
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 165-585 0e+00

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 678.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  165 DFCIKNIKQADFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYSTQ 244
Cdd:PRK05476   7 DYKVADISLADWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWASCNPFSTQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  245 NEVAAALAEGGFSVFAWKGESEDDFWWCIDRCVnvEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLY 324
Cdd:PRK05476  87 DDVAAALAAAGIPVFAWKGETLEEYWECIERAL--DGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGVHRLY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  325 QLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEID 404
Cdd:PRK05476 165 AMAKDGALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRATNVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVD 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  405 PICALQACMDGFRLVKLSEVIRQVDIVITCTGNKNVVVREYMDRMKNGCIVCNMGHSNTEIDVASLRTPELTWERVRSQV 484
Cdd:PRK05476 245 PICALQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELAVKWREIKPQV 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  485 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 563
Cdd:PRK05476 325 DEYTLPDGKRIILLAEGRLVNLGAATgHPSEVMDMSFANQALAQIELFTNR-GKLEPGVYVLPKELDEEVARLKLKALGV 403

                        410       420
                 ....*....|....*....|..
gi 41386739  564 HLTELSDEQAKYLGLNKNGPFK 585
Cdd:PRK05476 404 KLDELTEEQAEYIGVWVEGPFK 425
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
165-583 0e+00

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 670.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 165 DFCIKNIKQADFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYSTQ 244
Cdd:COG0499   5 DYKVKDISLAEWGRKEIEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAEVRWASCNPLSTQ 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 245 NEVAAALAEGGFSVFAWKGESEDDFWWCIDRCVNvegWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLY 324
Cdd:COG0499  85 DDVAAALAAAGIPVFAWKGETLEEYYWCIEQALD---HGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHRLR 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 325 QLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEID 404
Cdd:COG0499 162 AMAKEGALKFPAIAVNDAVTKSLFDNRYGTGQSLLDGIKRATNVLIAGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVD 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 405 PICALQACMDGFRLVKLSEVIRQVDIVITCTGNKNVVVREYMDRMKNGCIVCNMGHSNTEIDVASLRTPELTWERVRSQV 484
Cdd:COG0499 242 PICALEAAMDGFRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAVEKREIRPQV 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 485 DHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDA 563
Cdd:COG0499 322 DEYTLPDGRRIYLLAEGRLVNLAAATgHPSEVMDMSFANQALAQIYLVKNG-DKLEPGVYVLPKELDEEVARLKLEALGV 400

                       410       420
                ....*....|....*....|
gi 41386739 564 HLTELSDEQAKYLGLNKNGP 583
Cdd:COG0499 401 KIDTLTEEQAEYLGSWVEGP 420
PTZ00075 PTZ00075
Adenosylhomocysteinase; Provisional
 165-591 0e+00

Adenosylhomocysteinase; Provisional


Pssm-ID: 240258  Cd Length: 476  Bit Score: 603.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  165 DFCIKNIKQADFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYSTQ 244
Cdd:PTZ00075   4 DYKVKDISLAEFGRKEIELAENEMPGLMALREEYGPSKPLKGARITGCLHMTVQTAVLIETLKALGAEVRWCSCNIFSTQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  245 NEVAAALAE-GGFSVFAWKGESEDDFWWCIDRCVNvegWQ----PNMILDDGGDLTHWIYK------------------- 300
Cdd:PTZ00075  84 DHAAAAIAKaGSVPVFAWKGETLEEYWWCTEQALK---WPngdgPNLIVDDGGDATLLVHEgvkaeklyeekgilpdpld 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  301 ----------------------KYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESI 358
Cdd:PTZ00075 161 psnedekclltvlkklltknpdKWTNLVKKIVGVSEETTTGVHRLYKMLKKGELLFPAINVNDSVTKSKFDNIYGCRHSL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  359 LDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACMDGFRLVKLSEVIRQVDIVITCTGNK 438
Cdd:PTZ00075 241 IDGIFRATDVMIAGKTVVVCGYGDVGKGCAQALRGFGARVVVTEIDPICALQAAMEGYQVVTLEDVVETADIFVTATGNK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  439 NVVVREYMDRMKNGCIVCNMGHSNTEIDVASLRT-PELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCST-VPTFVL 516
Cdd:PTZ00075 321 DIITLEHMRRMKNNAIVGNIGHFDNEIQVAELEAyPGIEIVEIKPQVDRYTFPDGKGIILLAEGRLVNLGCATgHPSFVM 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41386739  517 SITATTQALALIELY-NAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELSDEQAKYLGLNKNGPFKPNYYRY 591
Cdd:PTZ00075 401 SNSFTNQVLAQIELWeNRDTGKYPNGVYKLPKELDEKVARLHLKKLGAKLTKLTDKQAEYIGVPVDGPYKSDHYRY 476
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 175-583 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 41386739   175 DFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYSTQNEVAAALAEG 254
Cdd:TIGR00936   1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTSCNPLSTQDDVAAALAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   255 -GFSVFAWKGESEDDFWWCIDRCVNVEgwqPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLC 333
Cdd:TIGR00936  81 aGIPVFAWRGETNEEYYWAIEQVLDHE---PNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   334 VPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACM 413
Cdd:TIGR00936 158 FPAINVNDAYTKSLFDNRYGTGQSTIDGILRATNLLIAGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALEAAM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   414 DGFRLVKLSEVIRQVDIVITCTGNKNVVVREYMDRMKNGCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGK 493
Cdd:TIGR00936 238 DGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIDVKALEELAVEKVNVRPQVDEYILKDGR 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   494 RIVLLAEGRLLNLSCST-VPTFVLSITATTQALALIELYNAPeGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELSDEQ 572
Cdd:TIGR00936 318 RIYLLAEGRLVNLAAAEgHPSEVMDMSFANQALAAEYLWKNH-DKLEPGVYRLPKELDEMVARLKLEAMGIEIDELTEEQ 396

                         410
                  ....*....|.
gi 41386739   573 AKYLGLNKNGP 583
Cdd:TIGR00936 397 KEYLGSWEEGT 407
PLN02494 PLN02494
adenosylhomocysteinase
 164-591 0e+00

adenosylhomocysteinase


Pssm-ID: 178111 [Multi-domain]  Cd Length: 477  Bit Score: 524.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  164 GDFCIKNIKQADFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLSALGAQCRWAACNIYST 243
Cdd:PLN02494   4 REYKVKDMSQADFGRLEIELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNIFST 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  244 QNEVAAALAEGGFSVFAWKGESEDDFWWCIDRCVNVE-GWQPNMILDDGGDLTHWIY----------------------- 299
Cdd:PLN02494  84 QDHAAAAIARDSAAVFAWKGETLQEYWWCTERALDWGpGGGPDLIVDDGGDATLLIHegvkaeeefekdgtlpdptstdn 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  300 ------------------KKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDG 361
Cdd:PLN02494 164 aefkivltiikdglkvdpKKYHKMKERLVGVSEETTTGVKRLYQMQKNGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDG 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  362 LKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACMDGFRLVKLSEVIRQVDIVITCTGNKNVV 441
Cdd:PLN02494 244 LMRATDVMIAGKVAVICGYGDVGKGCAAAMKAAGARVIVTEIDPICALQALMEGYQVLTLEDVVSEADIFVTTTGNKDII 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  442 VREYMDRMKNGCIVCNMGHSNTEIDVASLRT-PELTWERVRSQVDHVIWPDGKR-IVLLAEGRLLNLSCST-VPTFVLSI 518
Cdd:PLN02494 324 MVDHMRKMKNNAIVCNIGHFDNEIDMLGLETyPGVKRITIKPQTDRWVFPDTGSgIIVLAEGRLMNLGCATgHPSFVMSC 403

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41386739  519 TATTQALALIELYNAPE-GRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELSDEQAKYLGLNKNGPFKPNYYRY 591
Cdd:PLN02494 404 SFTNQVIAQLELWNEKKsGKYEKKVYVLPKHLDEKVAALHLGKLGAKLTKLSKDQADYINVPVEGPYKPAHYRY 477
AdoHcyase_NAD pfam00670
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
350-510 5.17e-103

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


Pssm-ID: 395543 [Multi-domain]  Cd Length: 162  Bit Score: 308.13  E-value: 5.17e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   350 NLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACMDGFRLVKLSEVIRQVD 429
Cdd:pfam00670   1 NLYGCRESLIDGIKRATDVMIAGKVAVVCGYGDVGKGCAASLKGQGARVIVTEIDPICALQAAMEGFQVVTLEEVVDKAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   430 IVITCTGNKNVVVREYMDRMKNGCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCS 509
Cdd:pfam00670  81 IFVTTTGNKDIITGEHMAKMKNDAIVCNIGHFDNEIDVAWLEANGKKKENIKPQVDRYTLPDGKHIILLAEGRLVNLGCA 160


                  .
gi 41386739   510 T 510
Cdd:pfam00670 161 T 161
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
350-511 7.16e-102

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


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 305.14  E-value: 7.16e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    350 NLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACMDGFRLVKLSEVIRQVD 429
Cdd:smart00997   1 NRYGTGESLLDGILRATNVLLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPIRALEAAMDGFEVMKMEEAAKRAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    430 IVITCTGNKNVVVREYMDRMKNGCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCS 509
Cdd:smart00997  81 IFVTATGNKDVITREHFRAMKDGAILANAGHFDVEIDVAALEELAVEKREVRPQVDEYTLPDGKRIYLLAEGRLVNLAAA 160


                   ..
gi 41386739    510 TV 511
Cdd:smart00997 161 TG 162
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 209-530 4.94e-37

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: 140.06  E-value: 4.94e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 209 IVGCTHITAQTA------VLMETLSALGAQCRWAACNIYSTQNEVAAALAEggfsvfawkgeseddfwWCIDRCVNVEGW 282
Cdd:cd12154   1 IAGPKEIKNEEFrvglspSVVATLVEAGHEVRVETGAGIGAGFADQAYVQA-----------------GAIVVTLAKALW 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 283 QPNMILDDGGDLTHWIYKkypnMFKK--IKGIVEESVTGVHRLY--QLSKAGklcVPAMNVNDSVTKQKFDNLYCCRESI 358
Cdd:cd12154  64 SLDVVLKVKEPLTNAEYA----LIQKlgDRLLFTYTIGADHRDLteALARAG---LTAIAVEGVELPLLTSNSIGAGELS 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 359 LDGLKRTTDVMFGG----------KQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACMDGFRLV-KLSEVIRQ 427
Cdd:cd12154 137 VQFIARFLEVQQPGrlggapdvagKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKNVeELEEALAE 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 428 VDIVIT---CTGNKNVVVR--EYMDRMKNGCIVCNMGHSNTEIDVASLRTPELtwervrsqvdhviwpDGKRIVLLAEGR 502
Cdd:cd12154 217 ADVIVTttlLPGKRAGILVpeELVEQMKPGSVIVNVAVGAVGCVQALHTQLLE---------------EGHGVVHYGDVN 281

                       330       340
                ....*....|....*....|....*....
gi 41386739 503 LLNLSC-STVPTFVLSITATTQALALIEL 530
Cdd:cd12154 282 MPGPGCaMGVPWDATLRLAANTLPALVKL 310
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 373-502 8.91e-07

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


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 50.84  E-value: 8.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 373 KQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACMDGFRLVK--------LSEV-IRQVDIVITCTGN--KNVV 441
Cdd:COG0569  96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVgdatdeevLEEAgIEDADAVIAATGDdeANIL 175

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41386739 442 VreymdrmkngCIVC-NMGHSNTeidVASLRTPELTWERVRSQVDHVIWPD---GKRIVLLAEGR 502
Cdd:COG0569 176 A----------CLLAkELGVPRI---IARANDPEYADLLERLGADVVISPErlaARRIARLLLRP 227
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 375-468 2.44e-05

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: 44.42  E-value: 2.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739    375 VVVCGYGEVGKGCSAALKAMGSIVYVTEIDP--ICALQACMDG-FRLVK-----LSEVIRQVDIVITC---TGNK--NVV 441
Cdd:smart01002  23 VVVIGAGVVGLGAAATAKGLGAEVTVLDVRParLRQLESLLGArFTTLYsqaelLEEAVKEADLVIGAvliPGAKapKLV 102

                           90       100
                   ....*....|....*....|....*..
gi 41386739    442 VREYMDRMKNGCIVCnmghsnteiDVA 468
Cdd:smart01002 103 TREMVKSMKPGSVIV---------DVA 120
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 356-446 1.82e-04

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 44.02  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  356 ESILDGLKrttdvmfgGKQVVVCGYGEVGKGCSAALKAMG-SIVYVT----EIDPICALQACMDGFRLVKLSEVIRQVDI 430
Cdd:PRK00045 174 KQIFGDLS--------GKKVLVIGAGEMGELVAKHLAEKGvRKITVAnrtlERAEELAEEFGGEAIPLDELPEALAEADI 245

                         90
                 ....*....|....*.
gi 41386739  431 VITCTGNKNVVVREYM 446
Cdd:PRK00045 246 VISSTGAPHPIIGKGM 261
PRK08306 PRK08306
dipicolinate synthase subunit DpsA;
366-469 6.05e-04

dipicolinate synthase subunit DpsA;


Pssm-ID: 181371 [Multi-domain]  Cd Length: 296  Bit Score: 42.13  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  366 TDVMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPicALQA-----CMDGFRLVKLSEVIRQVDIVItctgnkN- 439
Cdd:PRK08306 146 TPITIHGSNVLVLGFGRTGMTLARTLKALGANVTVGARKS--AHLAritemGLSPFHLSELAEEVGKIDIIF------Nt 217

                         90       100       110
                 ....*....|....*....|....*....|....
gi 41386739  440 ----VVVREYMDRMKNGCIVcnmghsnteIDVAS 469
Cdd:PRK08306 218 ipalVLTKEVLSKMPPEALI---------IDLAS 242
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 372-459 7.91e-04

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: 41.74  E-value: 7.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 372 GKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACMDGFRLVKLSEVIRQVDIVITC------TgnKNVVVREY 445
Cdd:cd05300 134 GKTVLIVGLGDIGREIARRAKAFGMRVIGVRRSGRPAPPVVDEVYTPDELDELLPEADYVVNAlpltpeT--RGLFNAER 211

                        90
                ....*....|....
gi 41386739 446 MDRMKNGCIVCNMG 459
Cdd:cd05300 212 FAAMKPGAVLINVG 225
PLN02928 PLN02928
oxidoreductase family protein
 372-459 1.22e-03

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 41.20  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739  372 GKQVVVCGYGEVGKGCSAALKAMGSIVYVT------EIDPICALQACmDGFRLV-------KLSEVIRQVDIVITC---- 434
Cdd:PLN02928 159 GKTVFILGYGAIGIELAKRLRPFGVKLLATrrswtsEPEDGLLIPNG-DVDDLVdekggheDIYEFAGEADIVVLCctlt 237

                         90       100
                 ....*....|....*....|....*
gi 41386739  435 TGNKNVVVREYMDRMKNGCIVCNMG 459
Cdd:PLN02928 238 KETAGIVNDEFLSSMKKGALLVNIA 262
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 368-459 1.94e-03

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: 40.69  E-value: 1.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 368 VMFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACMDGFrLVKLSEVIRQVDIVITCT----GNKNVVVR 443
Cdd:cd12165 133 KELRGKTVGILGYGHIGREIARLLKAFGMRVIGVSRSPKEDEGADFVGT-LSDLDEALEQADVVVVALpltkQTRGLIGA 211

                        90
                ....*....|....*.
gi 41386739 444 EYMDRMKNGCIVCNMG 459
Cdd:cd12165 212 AELAAMKPGAILVNVG 227
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
 348-468 2.08e-03

Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 40.47  E-value: 2.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 348 FDNLYCCRESILDGL----KRTTDVMFGGK-----QVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACMDGFRL 418
Cdd:cd01620 129 PNSNIAGYAGVQLGAyelaRIQGGRMGGAGgvppaKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEKLKGVETLGGSR 208

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41386739 419 VKLS------EVIRQVDIVITCT----GNKNVVVREYM-DRMKNGCIVcnmghsnteIDVA 468
Cdd:cd01620 209 LRYSqkeeleKELKQTDILINAIlvdgPRAPILIMEELvGPMKRGAVI---------VDLA 260
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
 353-496 2.40e-03

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


Pssm-ID: 133448  Cd Length: 168  Bit Score: 39.08  E-value: 2.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 353 CCRESILDGLKRTtDVMFGGKQVVVCGYGE-VGKGCSAALKAMGSIVyvteidPICALQAcmdgfrlVKLSEVIRQVDIV 431
Cdd:cd01080  26 CTPAGILELLKRY-GIDLAGKKVVVVGRSNiVGKPLAALLLNRNATV------TVCHSKT-------KNLKEHTKQADIV 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41386739 432 ITCTGNKNVVVREYmdrMKNGCIVcnmghsnteIDVAslrtpeltwervrsqVDHVIWPDGKRIV 496
Cdd:cd01080  92 IVAVGKPGLVKGDM---VKPGAVV---------IDVG---------------INRVPDKSGGKLV 129
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 372-459 3.81e-03

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: 38.63  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739   372 GKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACMDGFRLVKLSEVIRQVDIV-ITCTGNK---NVVVREYMD 447
Cdd:pfam02826  36 GKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSLDELLAESDVVsLHLPLTPetrHLINAERLA 115

                          90
                  ....*....|..
gi 41386739   448 RMKNGCIVCNMG 459
Cdd:pfam02826 116 LMKPGAILINTA 127
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 355-459 7.05e-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: 38.71  E-value: 7.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 355 RESILDGLKRTTDV----MFGGKQVVVCGYGEVGKGCSAALKAMGSIVYVTEIDPICALQACMDGFRLVKLSEVIRQVDI 430
Cdd:cd12175 121 DRELRAGRWGRPEGrpsrELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFRDPEAEEKDLGVRYVELDELLAESDV 200

                        90       100       110
                ....*....|....*....|....*....|...
gi 41386739 431 VITCT----GNKNVVVREYMDRMKNGCIVCNMG 459
Cdd:cd12175 201 VSLHVpltpETRHLIGAEELAAMKPGAILINTA 233
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 372-458 7.06e-03

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240651 [Multi-domain]  Cd Length: 305  Bit Score: 38.70  E-value: 7.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41386739 372 GKQVVVCGYGEVGKGCSAALKAMGS--IVYVTEIDPICALQACMDGFRLVKLSEVIRQVDIV---ITCT-GNKNVVVREY 445
Cdd:cd12174 135 GKTLGVIGLGNIGRLVANAALALGMkvIGYDPYLSVEAAWKLSVEVQRVTSLEELLATADYItlhVPLTdETRGLINAEL 214

                        90
                ....*....|...
gi 41386739 446 MDRMKNGCIVCNM 458
Cdd:cd12174 215 LAKMKPGAILLNF 227
 
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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