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Conserved domains on  [gi|1766409864|gb|KAB7169090|]
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adenosylhomocysteinase [Bifidobacterium longum]

Protein Classification

adenosylhomocysteinase( domain architecture ID 11481026)

adenosylhomocysteinase 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 83-494 2.03e-165

S-adenosyl-L-homocysteine hydrolase; Provisional


:

Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 474.23  E-value: 2.03e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  83 ITDMRKA-SGLEAMEYAEQHMPVLRDTMDSLTTRVDFSGIRIAVCLILEPKTAILLRKLKAAGAIVGV-YCGPDSTDPRV 160
Cdd:PRK05476   10 VADISLAdWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWaSCNPFSTQDDV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 161 AEQLRREGITVESSRDWTAEQAHEAALHLLDEIQPDIIIDDGASFARLASLERPELTANLIGVAEETTSGVRAFQQMQEA 240
Cdd:PRK05476   90 AAALAAAGIPVFAWKGETLEEYWECIERALDGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGVHRLYAMAKD 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 241 GALTYPVVAVNDSVLKTGFDNAHGTGETCVTTMQRILgEHAFDGKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVAS 320
Cdd:PRK05476  170 GALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRAT-NVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVDPICA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 321 LKAVFDGFAAQDIDEALPCADMVVSATGVRHTVTLEHMRAMHEGAALAVIGGIANEIALDEVSDF-------TPQVNrdt 393
Cdd:PRK05476  249 LQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELavkwreiKPQVD--- 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 394 vQLNVPDGPTLTLIADGDGVNYTVGGGNPIEIMDLSFAVQASAVAYLLEHRGTLDHTLIRLDAATDQRIAASALKARGYR 473
Cdd:PRK05476  326 -EYTLPDGKRIILLAEGRLVNLGAATGHPSEVMDMSFANQALAQIELFTNRGKLEPGVYVLPKELDEEVARLKLKALGVK 404

                         410       420
                  ....*....|....*....|.
gi 1766409864 474 ASHAVEDNGYNWRLTRFAEND 494
Cdd:PRK05476  405 LDELTEEQAEYIGVWVEGPFK 425
 
Name Accession Description Interval E-value
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 83-494 2.03e-165

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 474.23  E-value: 2.03e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  83 ITDMRKA-SGLEAMEYAEQHMPVLRDTMDSLTTRVDFSGIRIAVCLILEPKTAILLRKLKAAGAIVGV-YCGPDSTDPRV 160
Cdd:PRK05476   10 VADISLAdWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWaSCNPFSTQDDV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 161 AEQLRREGITVESSRDWTAEQAHEAALHLLDEIQPDIIIDDGASFARLASLERPELTANLIGVAEETTSGVRAFQQMQEA 240
Cdd:PRK05476   90 AAALAAAGIPVFAWKGETLEEYWECIERALDGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGVHRLYAMAKD 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 241 GALTYPVVAVNDSVLKTGFDNAHGTGETCVTTMQRILgEHAFDGKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVAS 320
Cdd:PRK05476  170 GALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRAT-NVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVDPICA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 321 LKAVFDGFAAQDIDEALPCADMVVSATGVRHTVTLEHMRAMHEGAALAVIGGIANEIALDEVSDF-------TPQVNrdt 393
Cdd:PRK05476  249 LQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELavkwreiKPQVD--- 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 394 vQLNVPDGPTLTLIADGDGVNYTVGGGNPIEIMDLSFAVQASAVAYLLEHRGTLDHTLIRLDAATDQRIAASALKARGYR 473
Cdd:PRK05476  326 -EYTLPDGKRIILLAEGRLVNLGAATGHPSEVMDMSFANQALAQIELFTNRGKLEPGVYVLPKELDEEVARLKLKALGVK 404

                         410       420
                  ....*....|....*....|.
gi 1766409864 474 ASHAVEDNGYNWRLTRFAEND 494
Cdd:PRK05476  405 LDELTEEQAEYIGVWVEGPFK 425
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 89-471 1.33e-104

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: 318.25  E-value: 1.33e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  89 ASGLEAMEYAEQHMPVLRDTMDSLTTRVDFSGIRIAVCLILEPKTAILLRKLKAAGAIVGVY-CGPDSTDPRVAEQLRRE 167
Cdd:cd00401     1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCsCNPLSTQDDVAAALAEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 168 GITVESSRDWTAE---QAHEAALhlldEIQPDIIIDDGASFARLASLERPELTANLIGVAEETTSGVRAFQQMQEAGALT 244
Cdd:cd00401    81 GIPVFAWKGETEEeywWCIEQAL----DHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 245 YPVVAVNDSVLKTGFDNAHGTGETCVTTMQR---ILgehaFDGKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASL 321
Cdd:cd00401   157 FPAIAVNDAVTKHKFDNRYGTGQSTIDGIKRatnVL----IAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICAL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 322 KAVFDGFAAQDIDEALPCADMVVSATGVRHTVTLEHMRAMHEGAALAVIGGIANEIALDEVSDftPQVNRDTVQLNV--- 398
Cdd:cd00401   233 QAAMDGFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEE--LAVEKREIRPQVdey 310

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1766409864 399 --PDGPTLTLIADGDGVNYTVGGGNPIEIMDLSFAVQASAVAYLLEHRGTLDHTLIRLDAATDQRIAASALKARG 471
Cdd:cd00401   311 tlPDGRRIILLAEGRLVNLACATGHPSFVMDMSFANQALAQIELWKNRDKLEPGVYVLPKELDEEVARLKLEALG 385
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
95-471 5.83e-104

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 317.38  E-value: 5.83e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  95 MEYAEQHMPVLRDTMDSLTTRVDFSGIRIAVCLILEPKTAILLRKLKAAGA---IVGvyCGPDSTDPRVAEQLRREGITV 171
Cdd:COG0499    21 IEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAevrWAS--CNPLSTQDDVAAALAAAGIPV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 172 ESSRDWTAEQAHEAALHLLDeIQPDIIIDDGASFARLASLERPELTANLIGVAEETTSGVRAFQQMQEAGALTYPVVAVN 251
Cdd:COG0499    99 FAWKGETLEEYYWCIEQALD-HGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHRLRAMAKEGALKFPAIAVN 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 252 DSVLKTGFDNAHGTGETCVTTMQRilgehAFD----GKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDG 327
Cdd:COG0499   178 DAVTKSLFDNRYGTGQSLLDGIKR-----ATNvliaGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVDPICALEAAMDG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 328 FAAQDIDEALPCADMVVSATGVRHTVTLEHMRAMHEGAALAVIGGIANEIALDEVSDFT-------PQVnrDTVQLnvPD 400
Cdd:COG0499   253 FRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAvekreirPQV--DEYTL--PD 328

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1766409864 401 GPTLTLIADGDGVNYTVGGGNPIEIMDLSFAVQASAVAYLLEHRGTLDHTLIRLDAATDQRIAASALKARG 471
Cdd:COG0499   329 GRRIYLLAEGRLVNLAAATGHPSEVMDMSFANQALAQIYLVKNGDKLEPGVYVLPKELDEEVARLKLEALG 399
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 89-473 2.44e-91

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: 284.30  E-value: 2.44e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  89 ASGLEAMEYAEQHMPVLRDTMDSLTTRVDFSGIRIAVCLILEPKTAILLRKLKAAGAIVGVY-CGPDSTDPRVAEQLRRE 167
Cdd:TIGR00936   1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTsCNPLSTQDDVAAALAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 168 -GITVESSRDWTAEQAHEAALHLLDeIQPDIIIDDGASFARLASLERPELTANLIGVAEETTSGVRAFQQMQEAGALTYP 246
Cdd:TIGR00936  81 aGIPVFAWRGETNEEYYWAIEQVLD-HEPNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLKFP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 247 VVAVNDSVLKTGFDNAHGTGETCVTTMQRilgehAFD----GKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLK 322
Cdd:TIGR00936 160 AINVNDAYTKSLFDNRYGTGQSTIDGILR-----ATNlliaGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 323 AVFDGFAAQDIDEALPCADMVVSATGVRHTVTLEHMRAMHEGAALAVIGGIANEI---ALDEVSDFTPQVNRDTVQLNVP 399
Cdd:TIGR00936 235 AAMDGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIdvkALEELAVEKVNVRPQVDEYILK 314

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1766409864 400 DGPTLTLIADGDGVNYTVGGGNPIEIMDLSFAVQASAVAYLLEHRGTLDHTLIRLDAATDQRIAASALKARGYR 473
Cdd:TIGR00936 315 DGRRIYLLAEGRLVNLAAAEGHPSEVMDMSFANQALAAEYLWKNHDKLEPGVYRLPKELDEMVARLKLEAMGIE 388
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
83-471 4.04e-57

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 195.45  E-value: 4.04e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864   83 ITDMRKAS-GLEAMEYAEQHMPVLrdtmdsLTTRVDFS------GIRIAVCLILEPKTAILLRKLKAAGAIVG-VYCGPD 154
Cdd:smart00996   2 VADISLADwGRKEIEIAETEMPGL------MALREEYGaekplkGARIAGCLHMTIQTAVLIETLVALGAEVRwASCNIF 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  155 STDPRVAEQLRREGITV-----ESSRD--WTAEQAheaaLHLLDEIQPDIIIDDGASFARLASLERPELTANLIGVAEET 227
Cdd:smart00996  76 STQDHAAAAIAAAGVPVfawkgETLEEywWCIEQT----LTWPDGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEET 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  228 TSGVRAFQQMQEAGALTYPVVAVNDSVLKTGFDNAHGTGETCVTTMQRILgEHAFDGKNVTVIGYGPVGQGFARRIRALG 307
Cdd:smart00996 152 TTGVHRLYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRAT-DVMIAGKVAVVCGYGDVGKGCAQSLRGQG 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  308 AEVTICDIDPVASLKAVFDGFAAQDIDEALPCADMVVSATGVRHTVTLEHMRAMHEGAALAVIGGIANEI---ALDEVSD 384
Cdd:smart00996 231 ARVIVTEIDPICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIdvaSLRNNPG 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  385 FT-----PQVNRDTvqlnVPDGPTLTLIADGDGVNYTVGGGNPIEIMDLSFAVQASAVAYLLEHRGTLDHTLIRLDAATD 459
Cdd:smart00996 311 LKwenikPQVDHIT----FPDGKRIILLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELFTKPGKYKNGVYVLPKKLD 386

                          410
                   ....*....|..
gi 1766409864  460 QRIAASALKARG 471
Cdd:smart00996 387 EKVARLHLEKLG 398
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
95-436 2.08e-46

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 166.85  E-value: 2.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  95 MEYAEQHMPVLrdtMdslTTRVDFS------GIRIAVCLILEPKTAILLRKLKAAGAIVG-VYCGPDSTDPRVAEQLRRE 167
Cdd:pfam05221  17 IEIAEHEMPGL---M---ALREEYGaskplkGARIAGSLHMTIQTAVLIETLVALGAEVRwASCNIFSTQDHAAAAIAAA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 168 GITV-----ESSRD--WTAEQAheaALHLLDEIQPDIIIDDGASFARLASLERPELTANLIGVAEETTSGVRAFQQMQEA 240
Cdd:pfam05221  91 GVPVfawkgETLEEywWCTEQA---LTWPPDGGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHRLYQMAKK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 241 GALTYPVVAVNDSVLKTGFDNAHGTGETCVTTMQRilgehAFD----GKNVTVIGYGPVGQGFARRIRALGAEVTICDID 316
Cdd:pfam05221 168 GKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKR-----ATDvmiaGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEID 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 317 PVASLKAVFDGFAAQDIDEALPCADMVVSATGVRHTVTLEHMRAMHEGAALAVIGGIANEIALDEVSDFT--------PQ 388
Cdd:pfam05221 243 PICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNIGHFDNEIDEIVLALLKgvkwvnikPQ 322

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1766409864 389 VNRDTvqlnVPDGPTLTLIADGDGVNYTVGGGNPIEIMDLSFAVQASA 436
Cdd:pfam05221 323 VDDIT----FPDGKSIIVLAEGRLVNLGCATGHPSFVMSNSFTNQVLA 366
 
Name Accession Description Interval E-value
PRK05476 PRK05476
S-adenosyl-L-homocysteine hydrolase; Provisional
 83-494 2.03e-165

S-adenosyl-L-homocysteine hydrolase; Provisional


Pssm-ID: 235488 [Multi-domain]  Cd Length: 425  Bit Score: 474.23  E-value: 2.03e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  83 ITDMRKA-SGLEAMEYAEQHMPVLRDTMDSLTTRVDFSGIRIAVCLILEPKTAILLRKLKAAGAIVGV-YCGPDSTDPRV 160
Cdd:PRK05476   10 VADISLAdWGRKEIEWAETEMPGLMAIREEFAAEKPLKGARIAGCLHMTIQTAVLIETLKALGAEVRWaSCNPFSTQDDV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 161 AEQLRREGITVESSRDWTAEQAHEAALHLLDEIQPDIIIDDGASFARLASLERPELTANLIGVAEETTSGVRAFQQMQEA 240
Cdd:PRK05476   90 AAALAAAGIPVFAWKGETLEEYWECIERALDGHGPNMILDDGGDLTLLVHTERPELLANIKGVTEETTTGVHRLYAMAKD 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 241 GALTYPVVAVNDSVLKTGFDNAHGTGETCVTTMQRILgEHAFDGKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVAS 320
Cdd:PRK05476  170 GALKFPAINVNDSVTKSKFDNRYGTGESLLDGIKRAT-NVLIAGKVVVVAGYGDVGKGCAQRLRGLGARVIVTEVDPICA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 321 LKAVFDGFAAQDIDEALPCADMVVSATGVRHTVTLEHMRAMHEGAALAVIGGIANEIALDEVSDF-------TPQVNrdt 393
Cdd:PRK05476  249 LQAAMDGFRVMTMEEAAELGDIFVTATGNKDVITAEHMEAMKDGAILANIGHFDNEIDVAALEELavkwreiKPQVD--- 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 394 vQLNVPDGPTLTLIADGDGVNYTVGGGNPIEIMDLSFAVQASAVAYLLEHRGTLDHTLIRLDAATDQRIAASALKARGYR 473
Cdd:PRK05476  326 -EYTLPDGKRIILLAEGRLVNLGAATGHPSEVMDMSFANQALAQIELFTNRGKLEPGVYVLPKELDEEVARLKLKALGVK 404

                         410       420
                  ....*....|....*....|.
gi 1766409864 474 ASHAVEDNGYNWRLTRFAEND 494
Cdd:PRK05476  405 LDELTEEQAEYIGVWVEGPFK 425
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
 89-471 1.33e-104

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: 318.25  E-value: 1.33e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  89 ASGLEAMEYAEQHMPVLRDTMDSLTTRVDFSGIRIAVCLILEPKTAILLRKLKAAGAIVGVY-CGPDSTDPRVAEQLRRE 167
Cdd:cd00401     1 EFGRKEIEWAEQEMPVLMALRERYAKEKPLKGARIAGCLHMTAQTAVLIETLKALGAEVRWCsCNPLSTQDDVAAALAEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 168 GITVESSRDWTAE---QAHEAALhlldEIQPDIIIDDGASFARLASLERPELTANLIGVAEETTSGVRAFQQMQEAGALT 244
Cdd:cd00401    81 GIPVFAWKGETEEeywWCIEQAL----DHGPNLIIDDGGDLTHLLHTKRPDLLKKIIGGSEETTTGVHRLRAMEKEGKLL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 245 YPVVAVNDSVLKTGFDNAHGTGETCVTTMQR---ILgehaFDGKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASL 321
Cdd:cd00401   157 FPAIAVNDAVTKHKFDNRYGTGQSTIDGIKRatnVL----IAGKVVVVAGYGWVGKGCAMRARGLGARVIVTEVDPICAL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 322 KAVFDGFAAQDIDEALPCADMVVSATGVRHTVTLEHMRAMHEGAALAVIGGIANEIALDEVSDftPQVNRDTVQLNV--- 398
Cdd:cd00401   233 QAAMDGFEVMPMEEAAKIGDIFVTATGNKDVIRGEHFEKMKDGAILCNAGHFDVEIDVAALEE--LAVEKREIRPQVdey 310

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1766409864 399 --PDGPTLTLIADGDGVNYTVGGGNPIEIMDLSFAVQASAVAYLLEHRGTLDHTLIRLDAATDQRIAASALKARG 471
Cdd:cd00401   311 tlPDGRRIILLAEGRLVNLACATGHPSFVMDMSFANQALAQIELWKNRDKLEPGVYVLPKELDEEVARLKLEALG 385
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
95-471 5.83e-104

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 440265 [Multi-domain]  Cd Length: 420  Bit Score: 317.38  E-value: 5.83e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  95 MEYAEQHMPVLRDTMDSLTTRVDFSGIRIAVCLILEPKTAILLRKLKAAGA---IVGvyCGPDSTDPRVAEQLRREGITV 171
Cdd:COG0499    21 IEWAEREMPVLMAIREEFAKEKPLKGARIAGCLHMTAQTAVLIETLKAGGAevrWAS--CNPLSTQDDVAAALAAAGIPV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 172 ESSRDWTAEQAHEAALHLLDeIQPDIIIDDGASFARLASLERPELTANLIGVAEETTSGVRAFQQMQEAGALTYPVVAVN 251
Cdd:COG0499    99 FAWKGETLEEYYWCIEQALD-HGPNIILDDGGDLTLLLHKERPELLAGIIGGTEETTTGVHRLRAMAKEGALKFPAIAVN 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 252 DSVLKTGFDNAHGTGETCVTTMQRilgehAFD----GKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDG 327
Cdd:COG0499   178 DAVTKSLFDNRYGTGQSLLDGIKR-----ATNvliaGKTVVVAGYGWCGKGVAMRARGLGARVIVTEVDPICALEAAMDG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 328 FAAQDIDEALPCADMVVSATGVRHTVTLEHMRAMHEGAALAVIGGIANEIALDEVSDFT-------PQVnrDTVQLnvPD 400
Cdd:COG0499   253 FRVMPMEEAAKLGDIFVTATGNKDVITAEHFEAMKDGAILANAGHFDVEIDVAALEKLAvekreirPQV--DEYTL--PD 328

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1766409864 401 GPTLTLIADGDGVNYTVGGGNPIEIMDLSFAVQASAVAYLLEHRGTLDHTLIRLDAATDQRIAASALKARG 471
Cdd:COG0499   329 GRRIYLLAEGRLVNLAAATGHPSEVMDMSFANQALAQIYLVKNGDKLEPGVYVLPKELDEEVARLKLEALG 399
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
 89-473 2.44e-91

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: 284.30  E-value: 2.44e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  89 ASGLEAMEYAEQHMPVLRDTMDSLTTRVDFSGIRIAVCLILEPKTAILLRKLKAAGAIVGVY-CGPDSTDPRVAEQLRRE 167
Cdd:TIGR00936   1 AEGRKKIEWAEREMPVLMRIRERFSEEKPLKGARIAACLHVTVETAVLIETLVAGGAEVAWTsCNPLSTQDDVAAALAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 168 -GITVESSRDWTAEQAHEAALHLLDeIQPDIIIDDGASFARLASLERPELTANLIGVAEETTSGVRAFQQMQEAGALTYP 246
Cdd:TIGR00936  81 aGIPVFAWRGETNEEYYWAIEQVLD-HEPNIIIDDGADLIFLLHTERPELLEKIIGGSEETTTGVIRLRAMEAEGVLKFP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 247 VVAVNDSVLKTGFDNAHGTGETCVTTMQRilgehAFD----GKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLK 322
Cdd:TIGR00936 160 AINVNDAYTKSLFDNRYGTGQSTIDGILR-----ATNlliaGKTVVVAGYGWCGKGIAMRARGMGARVIVTEVDPIRALE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 323 AVFDGFAAQDIDEALPCADMVVSATGVRHTVTLEHMRAMHEGAALAVIGGIANEI---ALDEVSDFTPQVNRDTVQLNVP 399
Cdd:TIGR00936 235 AAMDGFRVMTMEEAAKIGDIFITATGNKDVIRGEHFENMKDGAIVANIGHFDVEIdvkALEELAVEKVNVRPQVDEYILK 314

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1766409864 400 DGPTLTLIADGDGVNYTVGGGNPIEIMDLSFAVQASAVAYLLEHRGTLDHTLIRLDAATDQRIAASALKARGYR 473
Cdd:TIGR00936 315 DGRRIYLLAEGRLVNLAAAEGHPSEVMDMSFANQALAAEYLWKNHDKLEPGVYRLPKELDEMVARLKLEAMGIE 388
AdoHcyase smart00996
S-adenosyl-L-homocysteine hydrolase;
83-471 4.04e-57

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 214963 [Multi-domain]  Cd Length: 426  Bit Score: 195.45  E-value: 4.04e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864   83 ITDMRKAS-GLEAMEYAEQHMPVLrdtmdsLTTRVDFS------GIRIAVCLILEPKTAILLRKLKAAGAIVG-VYCGPD 154
Cdd:smart00996   2 VADISLADwGRKEIEIAETEMPGL------MALREEYGaekplkGARIAGCLHMTIQTAVLIETLVALGAEVRwASCNIF 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  155 STDPRVAEQLRREGITV-----ESSRD--WTAEQAheaaLHLLDEIQPDIIIDDGASFARLASLERPELTANLIGVAEET 227
Cdd:smart00996  76 STQDHAAAAIAAAGVPVfawkgETLEEywWCIEQT----LTWPDGWGPNMILDDGGDATLLVHKKYPRMLKKIRGVSEET 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  228 TSGVRAFQQMQEAGALTYPVVAVNDSVLKTGFDNAHGTGETCVTTMQRILgEHAFDGKNVTVIGYGPVGQGFARRIRALG 307
Cdd:smart00996 152 TTGVHRLYQMAKKGKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKRAT-DVMIAGKVAVVCGYGDVGKGCAQSLRGQG 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  308 AEVTICDIDPVASLKAVFDGFAAQDIDEALPCADMVVSATGVRHTVTLEHMRAMHEGAALAVIGGIANEI---ALDEVSD 384
Cdd:smart00996 231 ARVIVTEIDPICALQAAMDGFEVVTMEEVAPQADIFVTTTGNKDVITREHMRAMKDGAIVCNIGHFDNEIdvaSLRNNPG 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  385 FT-----PQVNRDTvqlnVPDGPTLTLIADGDGVNYTVGGGNPIEIMDLSFAVQASAVAYLLEHRGTLDHTLIRLDAATD 459
Cdd:smart00996 311 LKwenikPQVDHIT----FPDGKRIILLAEGRLVNLGCATGHPSFVMSNSFTNQVLAQIELFTKPGKYKNGVYVLPKKLD 386

                          410
                   ....*....|..
gi 1766409864  460 QRIAASALKARG 471
Cdd:smart00996 387 EKVARLHLEKLG 398
PTZ00075 PTZ00075
Adenosylhomocysteinase; Provisional
 91-471 3.24e-56

Adenosylhomocysteinase; Provisional


Pssm-ID: 240258  Cd Length: 476  Bit Score: 194.49  E-value: 3.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  91 GLEAMEYAEQHMPVLRDTMDSLTTRVDFSGIRIAVCLILEPKTAILLRKLKAAGAIVG-VYCGPDST-DPRVAEQLRREG 168
Cdd:PTZ00075   16 GRKEIELAENEMPGLMALREEYGPSKPLKGARITGCLHMTVQTAVLIETLKALGAEVRwCSCNIFSTqDHAAAAIAKAGS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 169 ITV-----ESSRD--WTAEQAheaaLHLLDEIQPDIIIDDGASF--------------------------------ARLA 209
Cdd:PTZ00075   96 VPVfawkgETLEEywWCTEQA----LKWPNGDGPNLIVDDGGDAtllvhegvkaeklyeekgilpdpldpsnedekCLLT 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 210 SLER---------PELTANLIGVAEETTSGVRAFQQMQEAGALTYPVVAVNDSVLKTGFDNAHGTGETCVTTMQR----I 276
Cdd:PTZ00075  172 VLKKlltknpdkwTNLVKKIVGVSEETTTGVHRLYKMLKKGELLFPAINVNDSVTKSKFDNIYGCRHSLIDGIFRatdvM 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 277 LGehafdGKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDGFAAQDIDEALPCADMVVSATGVRHTVTLE 356
Cdd:PTZ00075  252 IA-----GKTVVVCGYGDVGKGCAQALRGFGARVVVTEIDPICALQAAMEGYQVVTLEDVVETADIFVTATGNKDIITLE 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 357 HMRAMHEGAALAVIGGIANEIALD--------EVSDFTPQVNRDTvqlnVPDGPTLTLIADGDGVNYTVGGGNPIEIMDL 428
Cdd:PTZ00075  327 HMRRMKNNAIVGNIGHFDNEIQVAeleaypgiEIVEIKPQVDRYT----FPDGKGIILLAEGRLVNLGCATGHPSFVMSN 402

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1766409864 429 SFAVQASAVAYLLEHR--GTLDHTLIRLDAATDQRIAASALKARG 471
Cdd:PTZ00075  403 SFTNQVLAQIELWENRdtGKYPNGVYKLPKELDEKVARLHLKKLG 447
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
261-420 7.58e-53

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


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 175.72  E-value: 7.58e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  261 NAHGTGETCVTTMQRILGeHAFDGKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDGFAAQDIDEALPCA 340
Cdd:smart00997   1 NRYGTGESLLDGILRATN-VLLAGKNVVVAGYGDVGKGVAARLRGLGARVIVTEIDPIRALEAAMDGFEVMKMEEAAKRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  341 DMVVSATGVRHTVTLEHMRAMHEGAALAVIGGIANEIALDEVSDFT-------PQVNRDTvqlnVPDGPTLTLIADGDGV 413
Cdd:smart00997  80 DIFVTATGNKDVITREHFRAMKDGAILANAGHFDVEIDVAALEELAvekrevrPQVDEYT----LPDGKRIYLLAEGRLV 155


                   ....*..
gi 1766409864  414 NYTVGGG 420
Cdd:smart00997 156 NLAAATG 162
AdoHcyase pfam05221
S-adenosyl-L-homocysteine hydrolase;
95-436 2.08e-46

S-adenosyl-L-homocysteine hydrolase;


Pssm-ID: 461594  Cd Length: 429  Bit Score: 166.85  E-value: 2.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  95 MEYAEQHMPVLrdtMdslTTRVDFS------GIRIAVCLILEPKTAILLRKLKAAGAIVG-VYCGPDSTDPRVAEQLRRE 167
Cdd:pfam05221  17 IEIAEHEMPGL---M---ALREEYGaskplkGARIAGSLHMTIQTAVLIETLVALGAEVRwASCNIFSTQDHAAAAIAAA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 168 GITV-----ESSRD--WTAEQAheaALHLLDEIQPDIIIDDGASFARLASLERPELTANLIGVAEETTSGVRAFQQMQEA 240
Cdd:pfam05221  91 GVPVfawkgETLEEywWCTEQA---LTWPPDGGGPNMILDDGGDATLLVHKKYPRIAKGIKGVSEETTTGVHRLYQMAKK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 241 GALTYPVVAVNDSVLKTGFDNAHGTGETCVTTMQRilgehAFD----GKNVTVIGYGPVGQGFARRIRALGAEVTICDID 316
Cdd:pfam05221 168 GKLLFPAINVNDSVTKSKFDNLYGCRESLVDGIKR-----ATDvmiaGKVAVVCGYGDVGKGCAQSLRGQGARVIVTEID 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 317 PVASLKAVFDGFAAQDIDEALPCADMVVSATGVRHTVTLEHMRAMHEGAALAVIGGIANEIALDEVSDFT--------PQ 388
Cdd:pfam05221 243 PICALQAAMEGYEVVTMEDVVGEADIFITTTTNTNVITVEHMDHMKMMAIVCNIGHFDNEIDEIVLALLKgvkwvnikPQ 322

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1766409864 389 VNRDTvqlnVPDGPTLTLIADGDGVNYTVGGGNPIEIMDLSFAVQASA 436
Cdd:pfam05221 323 VDDIT----FPDGKSIIVLAEGRLVNLGCATGHPSFVMSNSFTNQVLA 366
PLN02494 PLN02494
adenosylhomocysteinase
 83-480 4.75e-46

adenosylhomocysteinase


Pssm-ID: 178111 [Multi-domain]  Cd Length: 477  Bit Score: 167.35  E-value: 4.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  83 ITDMRKAS-GLEAMEYAEQHMPVLRDTMDSLTTRVDFSGIRIAVCLILEPKTAILLRKLKAAGAIVG-VYCGPDSTDPRV 160
Cdd:PLN02494    8 VKDMSQADfGRLEIELAEVEMPGLMACRTEFGPSQPFKGARITGSLHMTIQTAVLIETLTALGAEVRwCSCNIFSTQDHA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 161 AEQLRREGITVESSRDWTAEQAHEAALHLLD---EIQPDIIIDDGAS--------------FARLASLERPELTAN---- 219
Cdd:PLN02494   88 AAAIARDSAAVFAWKGETLQEYWWCTERALDwgpGGGPDLIVDDGGDatllihegvkaeeeFEKDGTLPDPTSTDNaefk 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 220 -----------------------LIGVAEETTSGVRAFQQMQEAGALTYPVVAVNDSVLKTGFDNAHGTGETCVTTMQRi 276
Cdd:PLN02494  168 ivltiikdglkvdpkkyhkmkerLVGVSEETTTGVKRLYQMQKNGTLLFPAINVNDSVTKSKFDNLYGCRHSLPDGLMR- 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 277 lgehAFD----GKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDGFAAQDIDEALPCADMVVSATGVRHT 352
Cdd:PLN02494  247 ----ATDvmiaGKVAVICGYGDVGKGCAAAMKAAGARVIVTEIDPICALQALMEGYQVLTLEDVVSEADIFVTTTGNKDI 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 353 VTLEHMRAMHEGAALAVIGGIANEIALDEVSDFtPQVNRDTVQLNV-----PD-GPTLTLIADGDGVNYTVGGGNPIEIM 426
Cdd:PLN02494  323 IMVDHMRKMKNNAIVCNIGHFDNEIDMLGLETY-PGVKRITIKPQTdrwvfPDtGSGIIVLAEGRLMNLGCATGHPSFVM 401

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1766409864 427 DLSFAVQASAVAYLLEHR--GTLDHTLIRLDAATDQRIAASALKARGYRASHAVED 480
Cdd:PLN02494  402 SCSFTNQVIAQLELWNEKksGKYEKKVYVLPKHLDEKVAALHLGKLGAKLTKLSKD 457
AdoHcyase_NAD pfam00670
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
282-414 9.41e-26

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


Pssm-ID: 395543 [Multi-domain]  Cd Length: 162  Bit Score: 103.20  E-value: 9.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 282 FDGKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDGFAAQDIDEALPCADMVVSATGVRHTVTLEHMRAM 361
Cdd:pfam00670  21 IAGKVAVVCGYGDVGKGCAASLKGQGARVIVTEIDPICALQAAMEGFQVVTLEEVVDKADIFVTTTGNKDIITGEHMAKM 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1766409864 362 HEGAALAVIGGIANEIALDEVsdFTPQVNRDTVQLNV-----PDGPTLTLIADGDGVN 414
Cdd:pfam00670 101 KNDAIVCNIGHFDNEIDVAWL--EANGKKKENIKPQVdrytlPDGKHIILLAEGRLVN 156
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 177-367 2.82e-12

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: 67.64  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 177 WTAEQAHEAALHlldeiQPDIIIDDGASFARlASLERPELtANLIGVAEETTSGVRAFQQMQeAGALTYPVVAVNDSVLK 256
Cdd:cd12154    52 GAIVVTLAKALW-----SLDVVLKVKEPLTN-AEYALIQK-LGDRLLFTYTIGADHRDLTEA-LARAGLTAIAVEGVELP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 257 TGFDNAHGTGETCVTTMQRIL---------GEHAFDGKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVA-SLKAVFD 326
Cdd:cd12154   124 LLTSNSIGAGELSVQFIARFLevqqpgrlgGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEAlEQLEELG 203

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1766409864 327 GFAAQDIDEALPCADMVVSATGV----RH-TVTLEHMRAMHEGAAL 367
Cdd:cd12154   204 GKNVEELEEALAEADVIVTTTLLpgkrAGiLVPEELVEQMKPGSVI 249
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 284-371 6.48e-09

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: 57.15  E-value: 6.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 284 GKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDGFAAQDIDEALPCADMVVSA------TgvRHTVTLEH 357
Cdd:cd05300   134 GKTVLIVGLGDIGREIARRAKAFGMRVIGVRRSGRPAPPVVDEVYTPDELDELLPEADYVVNAlpltpeT--RGLFNAER 211

                          90
                  ....*....|....
gi 1766409864 358 MRAMHEGAALAVIG 371
Cdd:cd05300   212 FAAMKPGAVLINVG 225
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 284-379 1.19e-07

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: 51.73  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 284 GKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDGFAAQDIDEALPCADMVVSAT----GVRHTVTLEHMR 359
Cdd:pfam02826  36 GKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELGARYVSLDELLAESDVVSLHLpltpETRHLINAERLA 115

                          90       100
                  ....*....|....*....|....
gi 1766409864 360 AMHEGAALavI----GGIANEIAL 379
Cdd:pfam02826 116 LMKPGAIL--IntarGGLVDEDAL 137
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 284-381 8.71e-07

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: 50.65  E-value: 8.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 284 GKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDGFAAQDIDEALPCADMVV------SATgvRHTVTLEH 357
Cdd:cd12175   142 GKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFRDPEAEEKDLGVRYVELDELLAESDVVSlhvpltPET--RHLIGAEE 219

                          90       100
                  ....*....|....*....|....*.
gi 1766409864 358 MRAMHEGAALAVI--GGIANEIALDE 381
Cdd:cd12175   220 LAAMKPGAILINTarGGLVDEEALLA 245
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 287-374 9.13e-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: 48.27  E-value: 9.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864  287 VTVIGYGPVGQGFARRIRALGAEVTICDIDPvASLKAVFDGFAAQD---------IDEALPCADMVVSA---TGVR--HT 352
Cdd:smart01002  23 VVVIGAGVVGLGAAATAKGLGAEVTVLDVRP-ARLRQLESLLGARFttlysqaelLEEAVKEADLVIGAvliPGAKapKL 101

                           90       100
                   ....*....|....*....|..
gi 1766409864  353 VTLEHMRAMHEGaalAVIGGIA 374
Cdd:smart01002 102 VTREMVKSMKPG---SVIVDVA 120
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
 286-367 4.28e-06

Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440450 [Multi-domain]  Cd Length: 372  Bit Score: 48.85  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 286 NVTVIGYGPVGQGFARRIRALGAEVTICDIDP--VASLKAVFDG------FAAQDIDEALPCADMVVSA---TGVR--HT 352
Cdd:COG0686   170 KVVILGGGVVGTNAARMALGLGADVTVLDINLdrLRRLDDIFGGrvttlySNPANIEEALKEADLVIGAvliPGARapKL 249

                          90
                  ....*....|....*
gi 1766409864 353 VTLEHMRAMHEGAAL 367
Cdd:COG0686   250 VTREMVKRMKPGSVI 264
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 286-367 4.52e-06

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 48.56  E-value: 4.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 286 NVTVIGYGPVGQGFARRIRALGAEVTICDIDP--VASLKAVFDG------FAAQDIDEALPCADMVVSA---TGVR--HT 352
Cdd:cd05305   170 KVVILGAGVVGENAARVALGLGAEVTVLDINLerLRYLDDIFGGrvttlySNPANLEEALKEADLVIGAvliPGAKapKL 249

                          90
                  ....*....|....*
gi 1766409864 353 VTLEHMRAMHEGAAL 367
Cdd:cd05305   250 VTEEMVKTMKPGSVI 264
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 280-379 7.00e-06

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: 48.01  E-value: 7.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 280 HAFDGKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLkAVFDGFAAQDIDEALPCADMVVSATGV----RHTVTL 355
Cdd:cd05198   136 YELEGKTVGIVGLGRIGQRVAKRLQAFGMKVLYYDRTRKPEP-EEDLGFRVVSLDELLAQSDVVVLHLPLtpetRHLINE 214

                          90       100
                  ....*....|....*....|....*.
gi 1766409864 356 EHMRAMHEGAALAVI--GGIANEIAL 379
Cdd:cd05198   215 EELALMKPGAVLVNTarGGLVDEDAL 240
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 280-348 1.06e-05

Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 44.39  E-value: 1.06e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1766409864 280 HAFDGKNVTVIGYGPVGqgfARRIRAL---GAEVTICDIDPVASLKAVFDgFAAQDIDEALPCADMVVSATG 348
Cdd:pfam13241   3 LDLRGKRVLVVGGGEVA---ARKARKLleaGAKVTVVSPEITPFLEGLLD-LIRREFEGDLDGADLVIAATD 70
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 283-379 2.19e-05

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


Pssm-ID: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 46.47  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 283 DGKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDGFAAqDIDEALPCAD-MVVSATGVRHTVTL---EHM 358
Cdd:cd12165   136 RGKTVGILGYGHIGREIARLLKAFGMRVIGVSRSPKEDEGADFVGTLS-DLDEALEQADvVVVALPLTKQTRGLigaAEL 214

                          90       100
                  ....*....|....*....|...
gi 1766409864 359 RAMHEGAALAVI--GGIANEIAL 379
Cdd:cd12165   215 AAMKPGAILVNVgrGPVVDEEAL 237
PLN02928 PLN02928
oxidoreductase family protein
 256-371 2.56e-05

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 46.21  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 256 KTGfdNAHGTGETCVTTM---------------QRILGEHAFD---GKNVTVIGYGPVGQGFARRIRALGAEVTI----- 312
Cdd:PLN02928  115 GTG--NAASCAEMAIYLMlgllrkqnemqislkARRLGEPIGDtlfGKTVFILGYGAIGIELAKRLRPFGVKLLAtrrsw 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 313 -------CDIDPVASLKAVFDGFAAQDIDEALPCADMVVSA----TGVRHTVTLEHMRAMHEGAALAVIG 371
Cdd:PLN02928  193 tsepedgLLIPNGDVDDLVDEKGGHEDIYEFAGEADIVVLCctltKETAGIVNDEFLSSMKKGALLVNIA 262
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
 283-367 3.80e-05

Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. The D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD-binding domain.


Pssm-ID: 240634 [Multi-domain]  Cd Length: 318  Bit Score: 45.74  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 283 DGKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDGFAAQDIDEALPCADMVVSAT----GVRHTVTLEHM 358
Cdd:cd12157   143 DGKTVGILGMGALGRAIARRLSGFGATLLYYDPHPLDQAEEQALNLRRVELDELLESSDFLVLALpltpDTLHLINAEAL 222


                  ....*....
gi 1766409864 359 RAMHEGAAL 367
Cdd:cd12157   223 AKMKPGALL 231
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 283-381 6.08e-05

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


Pssm-ID: 240637  Cd Length: 310  Bit Score: 45.06  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 283 DGKNVTVIGYGPVGQGFARRIRALGAEVTicdidPVASLKAVFDGF---AAQDIDEALPCADMVVS---AT-GVRHTVTL 355
Cdd:cd12160   142 LGARVLIWGFGSIGQRLAPLLTALGARVT-----GVARSAGERAGFpvvAEDELPELLPETDVLVMilpATpSTAHALDA 216

                          90       100
                  ....*....|....*....|....*...
gi 1766409864 356 EHMRAMHEGAALAVI--GGIANEIALDE 381
Cdd:cd12160   217 EVLAALPKHAWVVNVgrGATVDEDALVA 244
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
 284-379 7.93e-05

Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, Coenzyme transport and metabolism, General function prediction only]; Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440672 [Multi-domain]  Cd Length: 316  Bit Score: 44.69  E-value: 7.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 284 GKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDGFAaqDIDEALPCADMVV------SATgvRHTVTLEH 357
Cdd:COG1052   143 GKTLGIIGLGRIGQAVARRAKGFGMKVLYYDRSPKPEVAELGAEYV--SLDELLAESDIVSlhcpltPET--RHLINAEE 218

                          90       100
                  ....*....|....*....|....*.
gi 1766409864 358 MRAMHEGAALavI----GGIANEIAL 379
Cdd:COG1052   219 LALMKPGAIL--IntarGGLVDEAAL 242
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 287-367 1.08e-04

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 43.64  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 287 VTVIGYGPVGQGFARRIRALGAEVTICDIDPvASLKAVFDGFAAQD----------IDEALPCADMVVSA---TGVR--H 351
Cdd:pfam01262  31 VLVIGGGVAGLNAAATAKGLGAIVTILDVRP-ARLEQLESILGAKFvetlysqaelIAEAVKEADLVIGTaliPGAKapK 109

                          90
                  ....*....|....*.
gi 1766409864 352 TVTLEHMRAMHEGAAL 367
Cdd:pfam01262 110 LVTREMVKSMKPGSVI 125
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
 284-379 1.15e-04

Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate dehydrogenase (PGDH) catalyzes the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDH comes in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. 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.


Pssm-ID: 240628 [Multi-domain]  Cd Length: 301  Bit Score: 44.07  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 284 GKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVaSLKAVFDGFAAQDIDEALPCADMV---VSATGV-RHTVTLEHMR 359
Cdd:cd05303   139 GKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPK-DEQAVELGVKTVSLEELLKNSDFIslhVPLTPEtKHMINKKELE 217

                          90       100
                  ....*....|....*....|..
gi 1766409864 360 AMHEGAAL--AVIGGIANEIAL 379
Cdd:cd05303   218 LMKDGAIIinTSRGGVIDEEAL 239
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 274-360 1.54e-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: 43.95  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 274 QRILGEhaFDGKNVTVIGYGPVGQGFARRIRALGA-EVTIC--DIDPVASLKAVFDGFAA--QDIDEALPCADMVVSATG 348
Cdd:COG0373   174 KKIFGD--LSGKTVLVIGAGEMGELAARHLAAKGVkRITVAnrTLERAEELAEEFGGEAVplEELPEALAEADIVISSTG 251

                          90
                  ....*....|...
gi 1766409864 349 VRH-TVTLEHMRA 360
Cdd:COG0373   252 APHpVITKEMVER 264
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
 284-379 1.96e-04

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. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. 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.


Pssm-ID: 240650 [Multi-domain]  Cd Length: 304  Bit Score: 43.56  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 284 GKNVTVIGYGPVGQGFARRIRALGAEVTICdiDPVASLKAVFDGFA-AQDIDEALPCADMVV------SATgvRHTVTLE 356
Cdd:cd12173   138 GKTLGIVGLGRIGREVARRARAFGMKVLAY--DPYISAERAAAGGVeLVSLDELLAEADFISlhtpltPET--RGLINAE 213

                          90       100
                  ....*....|....*....|....*..
gi 1766409864 357 HMRAMHEGAALavI----GGIANEIAL 379
Cdd:cd12173   214 ELAKMKPGAIL--IntarGGIVDEAAL 238
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
 261-345 2.26e-04

D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which 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.


Pssm-ID: 240635 [Multi-domain]  Cd Length: 343  Bit Score: 43.29  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 261 NAHGTGETCVTTMQRILGEHAFD--GKNVTVIGYGPVGQGFARRIRALGAEVTICdiDPVASLKAVFDGFAaqDIDEALP 338
Cdd:cd12158    90 NANSVAEYVLSALLVLAQRQGFSlkGKTVGIVGVGNVGSRLARRLEALGMNVLLC--DPPRAEAEGDPGFV--SLEELLA 165


                  ....*..
gi 1766409864 339 CADmVVS 345
Cdd:cd12158   166 EAD-IIT 171
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 284-379 2.68e-04

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: 240649 [Multi-domain]  Cd Length: 306  Bit Score: 42.86  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 284 GKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDGFAAqDIDEALPCADMV---VSAT-GVRHTVTLEHMR 359
Cdd:cd12172   142 GKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDEEFAKEHGVEFV-SLEELLKESDFIslhLPLTpETRHLINAAELA 220

                          90       100
                  ....*....|....*....|....
gi 1766409864 360 AMHEGAALavI----GGIANEIAL 379
Cdd:cd12172   221 LMKPGAIL--IntarGGLVDEEAL 242
NAD_bind_m-THF_DH_Cyclohyd cd01080
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ...
 274-367 2.77e-04

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


Pssm-ID: 133448  Cd Length: 168  Bit Score: 41.77  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 274 QRILGEHAFD--GKNVTVIGYGP-VGQGFARRIRALGAEVTICDIDpvaslkavfdgfaAQDIDEALPCADMVVSATGVR 350
Cdd:cd01080    32 LELLKRYGIDlaGKKVVVVGRSNiVGKPLAALLLNRNATVTVCHSK-------------TKNLKEHTKQADIVIVAVGKP 98

                          90
                  ....*....|....*..
gi 1766409864 351 HTVTLEHMRamhEGAAL 367
Cdd:cd01080    99 GLVKGDMVK---PGAVV 112
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 284-380 3.19e-04

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 42.82  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 284 GKNVTVIGYGPVGQGFARRIRALGA-EVTICDIDP-----VASLKA--VFDgFAAQDIDEAL------PCADMVVSATGV 349
Cdd:COG1063   162 GDTVLVIGAGPIGLLAALAARLAGAaRVIVVDRNPerlelARELGAdaVVN-PREEDLVEAVreltggRGADVVIEAVGA 240

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1766409864 350 RHTVTlEHMRAMHEGAALAVIGGIANEIALD 380
Cdd:COG1063   241 PAALE-QALDLVRPGGTVVLVGVPGGPVPID 270
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 280-343 4.46e-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: 240648 [Multi-domain]  Cd Length: 310  Bit Score: 42.14  E-value: 4.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1766409864 280 HAFDGKNVTVIGYGPVGQGFARRIRALGAEVTICD--IDPVaslKAVFDGFAAQDIDEALPCADMV 343
Cdd:cd12171   143 PELRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDpyVDPE---KIEADGVKKVSLEELLKRSDVV 205
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 274-353 9.90e-04

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 41.32  E-value: 9.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 274 QRILGEhaFDGKNVTVIGYGPVGQGFARRIRALGA-EVTIC--DIDPVASLKAVFDGFAA--QDIDEALPCADMVVSATG 348
Cdd:PRK00045  174 KQIFGD--LSGKKVLVIGAGEMGELVAKHLAEKGVrKITVAnrTLERAEELAEEFGGEAIplDELPEALAEADIVISSTG 251


                  ....*
gi 1766409864 349 VRHTV 353
Cdd:PRK00045  252 APHPI 256
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 283-371 1.89e-03

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 40.38  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 283 DGKNVTVIGYG-----PVGQGFARriRALGAEVTICDIdpvaslkavfdgfAAQDIDEALPCADMVVSATGVRHTVTLEH 357
Cdd:PRK14193  157 AGAHVVVIGRGvtvgrPIGLLLTR--RSENATVTLCHT-------------GTRDLAAHTRRADIIVAAAGVAHLVTADM 221

                          90
                  ....*....|....
gi 1766409864 358 MRamhEGAALAVIG 371
Cdd:PRK14193  222 VK---PGAAVLDVG 232
DpaA COG5842
Dipicolinate synthase subunit A (sporulation protein SpoVFA) [Cell cycle control, cell ...
 284-343 2.05e-03

Dipicolinate synthase subunit A (sporulation protein SpoVFA) [Cell cycle control, cell division, chromosome partitioning, Amino acid transport and metabolism];


Pssm-ID: 444544 [Multi-domain]  Cd Length: 288  Bit Score: 40.14  E-value: 2.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1766409864 284 GKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDGFAA---QDIDEALPCADMV 343
Cdd:COG5842   152 GSNVLVLGFGRCGKTLARKLKALGAKVTVGARKPADLARAYEMGYEPvhlSELAEYLGEADII 214
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
 282-348 2.20e-03

Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and metabolism]; Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 441254 [Multi-domain]  Cd Length: 211  Bit Score: 39.36  E-value: 2.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1766409864 282 FDGKNVTVIGYGPVGqgfARRIRAL---GAEVTICDIDPVASLKAVFD---------GFAAQDIDEalpcADMVVSATG 348
Cdd:COG1648    10 LEGRRVLVVGGGEVA---ARKARLLlkaGARVTVVAPEFSPELAALAEegrielikrAFEPEDLDG----AFLVIAATD 81
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 283-343 2.35e-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: 240656 [Multi-domain]  Cd Length: 306  Bit Score: 39.97  E-value: 2.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1766409864 283 DGKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASlkavfDGFAAQ-DIDEALPCADMV 343
Cdd:cd12179   137 MGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYDKYKNFG-----DAYAEQvSLETLFKEADIL 193
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 279-340 4.48e-03

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


Pssm-ID: 133444  Cd Length: 200  Bit Score: 38.34  E-value: 4.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1766409864 279 EHAFD-----GKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVfDGFAA----------QDIDEALPCA 340
Cdd:cd01075    18 EHLLGtdsleGKTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAA-ELFGAtvvapeeiysVDADVFAPCA 93
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
277-380 6.09e-03

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 39.05  E-value: 6.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 277 LGEHAF------DGKNVTVIGYGPVGQGFARRIRALGAE-VTICDIDP-----VASLKA--VFDG--FAAQDIDEALPCA 340
Cdd:PRK10309  148 VGLHAFhlaqgcEGKNVIIIGAGTIGLLAIQCAVALGAKsVTAIDINSeklalAKSLGAmqTFNSreMSAPQIQSVLREL 227

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1766409864 341 ---DMVVSATGVRHTVTLEhMRAMHEGAALAVIGGIANEIALD 380
Cdd:PRK10309  228 rfdQLILETAGVPQTVELA-IEIAGPRAQLALVGTLHHDLHLT 269
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 284-379 8.30e-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: 38.31  E-value: 8.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 284 GKNVTVIGYGPVGQGFARRIRALGAEVTICD--IDPVASLKAVFDGFAAQDIDEALPCADMV---VSAT-GVRHTVTLEH 357
Cdd:cd12174   135 GKTLGVIGLGNIGRLVANAALALGMKVIGYDpyLSVEAAWKLSVEVQRVTSLEELLATADYItlhVPLTdETRGLINAEL 214

                          90       100
                  ....*....|....*....|....*.
gi 1766409864 358 MRAMHEGAALavI----GGIANEIAL 379
Cdd:cd12174   215 LAKMKPGAIL--LnfarGEIVDEEAL 238
murD PRK14106
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
 282-349 9.31e-03

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional


Pssm-ID: 184511 [Multi-domain]  Cd Length: 450  Bit Score: 38.41  E-value: 9.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1766409864 282 FDGKNVTVIGYGPVGQGFARRIRALGAEVTICDIDPVASLKAVFDGFAAQDI--------DEALPCADMVVSATGV 349
Cdd:PRK14106    3 LKGKKVLVVGAGVSGLALAKFLKKLGAKVILTDEKEEDQLKEALEELGELGIelvlgeypEEFLEGVDLVVVSPGV 78
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 284-367 9.83e-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: 240643 [Multi-domain]  Cd Length: 300  Bit Score: 37.95  E-value: 9.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1766409864 284 GKNVTVIGYGPVGQGFARRIRALGAEVTIC-----DIDPVASLkavfdgfaaQDIDEALPCADMVVSAT----GVRHTVT 354
Cdd:cd12166   132 DRRVLIVGYGSIGRAIERRLAPFEVRVTRVartarPGEQVHGI---------DELPALLPEADVVVLIVpltdETRGLVD 202

                          90
                  ....*....|...
gi 1766409864 355 LEHMRAMHEGAAL 367
Cdd:cd12166   203 AEFLARMPDGALL 215
 
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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