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Conserved domains on  [gi|7710012|ref|NP_057878|]
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ketimine reductase mu-crystallin [Mus musculus]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 5-312 3.07e-134

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member pfam02423:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 313  Bit Score: 383.35  E-value: 3.07e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012      5 PAFLSAEEVQDHLRSSsLLIPPLEAALANFSkgpDGGVMQPVRTVVPVAKHRGFLGVMPAYSAAEDALTTKLVTFYEGHS 84
Cdd:pfam02423   2 TMVLLAVDVEEELFMD-DLAGYVEEAFRRWS---LGTFDKPPRVASHSRDGDGVLEAMPAYLGGRKLYGVKWVNSHPGNP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012     85 NTAVPSHQASVLLFDPSNGSLLAVMDGNVITAKRTAAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVR 164
Cdd:pfam02423  78 DSGLPTVTATGVLNDPSTGYPLALMDATLLTALRTAAVSAVAAKYLAPKDASVLAIIGNGVQAEFQAEAFRAVFGIDEVR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    165 MWNRTRENAEKFASTVQG---DVRVCSSVQEAVTGADVIITVTMATE--PILFGEWVKPGAHINAVGASRPDWRELDDEL 239
Cdd:pfam02423 158 IYDRDPRATEKFARNAQEpgfEVRACTSPEEAVEGADIIITVTADKAnaPILKDEWVKPGAHINAVGADRPGKTELDDDI 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7710012    240 MRQAVLYVDSrEAALKESGDV-LLSGADIFAELGEVISGAKP--AHCEKTTVFKSLGMAVEDLVAAKLVYDSWSSG 312
Cdd:pfam02423 238 LKRADIFVEY-EAQAREEGEIqQLLVDDPVAELGEVITGKKPgrTSDEEITLFDSVGMAIEDVAAARYVYERALSK 312
 
Name Accession Description Interval E-value
OCD_Mu_crystall pfam02423
Ornithine cyclodeaminase/mu-crystallin family; This family contains the bacterial Ornithine ...
 5-312 3.07e-134

Ornithine cyclodeaminase/mu-crystallin family; This family contains the bacterial Ornithine cyclodeaminase enzyme EC:4.3.1.12, which catalyzes the deamination of ornithine to proline. This family also contains mu-Crystallin the major component of the eye lens in several Australian marsupials, mRNA for this protein has also been found in human retina.


Pssm-ID: 426766 [Multi-domain]  Cd Length: 313  Bit Score: 383.35  E-value: 3.07e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012      5 PAFLSAEEVQDHLRSSsLLIPPLEAALANFSkgpDGGVMQPVRTVVPVAKHRGFLGVMPAYSAAEDALTTKLVTFYEGHS 84
Cdd:pfam02423   2 TMVLLAVDVEEELFMD-DLAGYVEEAFRRWS---LGTFDKPPRVASHSRDGDGVLEAMPAYLGGRKLYGVKWVNSHPGNP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012     85 NTAVPSHQASVLLFDPSNGSLLAVMDGNVITAKRTAAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVR 164
Cdd:pfam02423  78 DSGLPTVTATGVLNDPSTGYPLALMDATLLTALRTAAVSAVAAKYLAPKDASVLAIIGNGVQAEFQAEAFRAVFGIDEVR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    165 MWNRTRENAEKFASTVQG---DVRVCSSVQEAVTGADVIITVTMATE--PILFGEWVKPGAHINAVGASRPDWRELDDEL 239
Cdd:pfam02423 158 IYDRDPRATEKFARNAQEpgfEVRACTSPEEAVEGADIIITVTADKAnaPILKDEWVKPGAHINAVGADRPGKTELDDDI 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7710012    240 MRQAVLYVDSrEAALKESGDV-LLSGADIFAELGEVISGAKP--AHCEKTTVFKSLGMAVEDLVAAKLVYDSWSSG 312
Cdd:pfam02423 238 LKRADIFVEY-EAQAREEGEIqQLLVDDPVAELGEVITGKKPgrTSDEEITLFDSVGMAIEDVAAARYVYERALSK 312
OCDMu COG2423
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid ...
 7-309 3.04e-120

Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid transport and metabolism]; Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 441972 [Multi-domain]  Cd Length: 322  Bit Score: 348.29  E-value: 3.04e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    7 FLSAEEVQDHLrSSSLLIPPLEAALANFSkgpDGGVMQPVRTVVPVAKHRGFLGVMPAYSAAEDALTTKLVTFYEGHSNT 86
Cdd:COG2423   3 ILSAEDVAALL-DMDDAIDAVEEAFRALA---RGRVVMPPRTVLDLPEAGGTLLLMPAYIPGGGAFGVKVVSVFPGNPAR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   87 AVPSHQASVLLFDPSNGSLLAVMDGNVITAKRTAAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVRMW 166
Cdd:COG2423  79 GLPTVQGTVLLFDAETGEPLALLDGTLLTALRTAAASALAARYLARPDARTLGIIGAGVQARTQLRALAAVRPIERVRVW 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012  167 NRTRENAEKFASTVQG---DVRVCSSVQEAVTGADVIITVTMATEPILFGEWVKPGAHINAVGASRPDWRELDDELMRQA 243
Cdd:COG2423 159 GRDPEKAEAFAARLAAeglPVEAADDLEEAVADADIIVTATPSREPVLRGEWLRPGTHINAVGADTPGKRELDPALLARA 238

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7710012  244 VLYVDSREAALKESGDV-------LLSGADIFAELGEVISGAKPAHC--EKTTVFKSLGMAVEDLVAAKLVYDSW 309
Cdd:COG2423 239 RVVVDSREQALAEAGELqhalaagLISEDDIVAELGEVLAGRAPGRTsdDEITVFKSVGLALQDLAAARLVYERA 313
PRK08618 PRK08618
ornithine cyclodeaminase family protein;
7-307 1.35e-76

ornithine cyclodeaminase family protein;


Pssm-ID: 236313 [Multi-domain]  Cd Length: 325  Bit Score: 237.27  E-value: 1.35e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012     7 FLSAEEVQDhLRSSSLLIPPLEAALANFSKGPdggVMQPVRTVVPVAKHRGFLGVMPAYSAAEDALTTKLVTFYEGHSNT 86
Cdd:PRK08618   3 VLSAEDQKK-LFNMNEAIEADKEALKAYSEGK---TITPLRTNLPFPNENNTSLIMPGYAEGLEALGLKIVSVVPENKKK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    87 AVPSHQASVLLFDPSNGSLLAVMDGNVITAKRTAAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVRMW 166
Cdd:PRK08618  79 GKPTIPGTVILSDFETGEVLAILDGTYLTQIRTGALSGVATKYLAREDAKTLCLIGTGGQAKGQLEAVLAVRDIERVRVY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   167 NRTRENAEKFASTVQG----DVRVCSSVQEAVTGADVIITVTMATEPIlFGEWVKPGAHINAVGASRPDWRELDDELMRQ 242
Cdd:PRK08618 159 SRTFEKAYAFAQEIQSkfntEIYVVNSADEAIEEADIIVTVTNAKTPV-FSEKLKKGVHINAVGSFMPDMQELPSEAIAR 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7710012   243 A-VLYVDSREAALKESGDV-------LLSGADIFAELGEVISGAKPAHC--EKTTVFKSLGMAVEDLVAAKLVYD 307
Cdd:PRK08618 238 AnKVVVESKEAALEETGDLivplkegLISKDDIHGELGQIISGEIAGREsdEEITVFKSVGLAVVDIVVAKYIYE 312
ala_DH_arch TIGR02371
alanine dehydrogenase, Archaeoglobus fulgidus type; This enzyme, a homolog of bacterial ...
 40-307 2.43e-54

alanine dehydrogenase, Archaeoglobus fulgidus type; This enzyme, a homolog of bacterial ornithine cyclodeaminases and marsupial mu-crystallins, is a homodimeric, NAD-dependent alanine dehydrogenase found in Archaeoglobus fulgidus and several other Archaea. For a number of close homologs, scoring between trusted and noise cutoffs, it is not clear at present what is the enzymatic activity.


Pssm-ID: 131424  Cd Length: 325  Bit Score: 180.11  E-value: 2.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012     40 GGVMQPVRTVVPVAKHRGFLGVMPAYSAAEDALTTKLVTFYEGHSNTAVPSHQASVLLFDPSNGSLLAVMDGNVITAKRT 119
Cdd:TIGR02371  33 GKVQMPPKMYLFFRRYNGDLRVMPAYLEELEMAGVKCVNVHPGNPDRHLPTVMALIILVSPETGFPIALMDGTYITDMRT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    120 AAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVRMWNRTRENAEKFASTVQgDVRVCSSV----QEAVT 195
Cdd:TIGR02371 113 GAAGGVAAKYLARKDSSVLGIIGAGRQAWTQLEALSRVFDLEEVSVYCRTPSTREKFALRAS-DYEVPVRAatdpREAVE 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    196 GADVIITVTMATEPILFGEWVKPGAHINAVGASRPDWRELDDELMRQAVLYVDSREAAlKESGDV-------LLSGADIF 268
Cdd:TIGR02371 192 GCDILVTTTPSRKPVVKADWVSEGTHINAIGADAPGKQELDPEILKNAKIFVDDLEQA-THSGEInvpiskgIIRVDDLH 270

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 7710012    269 AELGEVISGAKPAHC--EKTTVFKSLGMAVEDLVAAKLVYD 307
Cdd:TIGR02371 271 ASLGEVITGLKEGRTspEEITIFDSTGLAIQDVATAWMVYE 311
 
Name Accession Description Interval E-value
OCD_Mu_crystall pfam02423
Ornithine cyclodeaminase/mu-crystallin family; This family contains the bacterial Ornithine ...
 5-312 3.07e-134

Ornithine cyclodeaminase/mu-crystallin family; This family contains the bacterial Ornithine cyclodeaminase enzyme EC:4.3.1.12, which catalyzes the deamination of ornithine to proline. This family also contains mu-Crystallin the major component of the eye lens in several Australian marsupials, mRNA for this protein has also been found in human retina.


Pssm-ID: 426766 [Multi-domain]  Cd Length: 313  Bit Score: 383.35  E-value: 3.07e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012      5 PAFLSAEEVQDHLRSSsLLIPPLEAALANFSkgpDGGVMQPVRTVVPVAKHRGFLGVMPAYSAAEDALTTKLVTFYEGHS 84
Cdd:pfam02423   2 TMVLLAVDVEEELFMD-DLAGYVEEAFRRWS---LGTFDKPPRVASHSRDGDGVLEAMPAYLGGRKLYGVKWVNSHPGNP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012     85 NTAVPSHQASVLLFDPSNGSLLAVMDGNVITAKRTAAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVR 164
Cdd:pfam02423  78 DSGLPTVTATGVLNDPSTGYPLALMDATLLTALRTAAVSAVAAKYLAPKDASVLAIIGNGVQAEFQAEAFRAVFGIDEVR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    165 MWNRTRENAEKFASTVQG---DVRVCSSVQEAVTGADVIITVTMATE--PILFGEWVKPGAHINAVGASRPDWRELDDEL 239
Cdd:pfam02423 158 IYDRDPRATEKFARNAQEpgfEVRACTSPEEAVEGADIIITVTADKAnaPILKDEWVKPGAHINAVGADRPGKTELDDDI 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7710012    240 MRQAVLYVDSrEAALKESGDV-LLSGADIFAELGEVISGAKP--AHCEKTTVFKSLGMAVEDLVAAKLVYDSWSSG 312
Cdd:pfam02423 238 LKRADIFVEY-EAQAREEGEIqQLLVDDPVAELGEVITGKKPgrTSDEEITLFDSVGMAIEDVAAARYVYERALSK 312
OCDMu COG2423
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid ...
 7-309 3.04e-120

Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid transport and metabolism]; Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 441972 [Multi-domain]  Cd Length: 322  Bit Score: 348.29  E-value: 3.04e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    7 FLSAEEVQDHLrSSSLLIPPLEAALANFSkgpDGGVMQPVRTVVPVAKHRGFLGVMPAYSAAEDALTTKLVTFYEGHSNT 86
Cdd:COG2423   3 ILSAEDVAALL-DMDDAIDAVEEAFRALA---RGRVVMPPRTVLDLPEAGGTLLLMPAYIPGGGAFGVKVVSVFPGNPAR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   87 AVPSHQASVLLFDPSNGSLLAVMDGNVITAKRTAAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVRMW 166
Cdd:COG2423  79 GLPTVQGTVLLFDAETGEPLALLDGTLLTALRTAAASALAARYLARPDARTLGIIGAGVQARTQLRALAAVRPIERVRVW 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012  167 NRTRENAEKFASTVQG---DVRVCSSVQEAVTGADVIITVTMATEPILFGEWVKPGAHINAVGASRPDWRELDDELMRQA 243
Cdd:COG2423 159 GRDPEKAEAFAARLAAeglPVEAADDLEEAVADADIIVTATPSREPVLRGEWLRPGTHINAVGADTPGKRELDPALLARA 238

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7710012  244 VLYVDSREAALKESGDV-------LLSGADIFAELGEVISGAKPAHC--EKTTVFKSLGMAVEDLVAAKLVYDSW 309
Cdd:COG2423 239 RVVVDSREQALAEAGELqhalaagLISEDDIVAELGEVLAGRAPGRTsdDEITVFKSVGLALQDLAAARLVYERA 313
PRK08618 PRK08618
ornithine cyclodeaminase family protein;
7-307 1.35e-76

ornithine cyclodeaminase family protein;


Pssm-ID: 236313 [Multi-domain]  Cd Length: 325  Bit Score: 237.27  E-value: 1.35e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012     7 FLSAEEVQDhLRSSSLLIPPLEAALANFSKGPdggVMQPVRTVVPVAKHRGFLGVMPAYSAAEDALTTKLVTFYEGHSNT 86
Cdd:PRK08618   3 VLSAEDQKK-LFNMNEAIEADKEALKAYSEGK---TITPLRTNLPFPNENNTSLIMPGYAEGLEALGLKIVSVVPENKKK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    87 AVPSHQASVLLFDPSNGSLLAVMDGNVITAKRTAAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVRMW 166
Cdd:PRK08618  79 GKPTIPGTVILSDFETGEVLAILDGTYLTQIRTGALSGVATKYLAREDAKTLCLIGTGGQAKGQLEAVLAVRDIERVRVY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   167 NRTRENAEKFASTVQG----DVRVCSSVQEAVTGADVIITVTMATEPIlFGEWVKPGAHINAVGASRPDWRELDDELMRQ 242
Cdd:PRK08618 159 SRTFEKAYAFAQEIQSkfntEIYVVNSADEAIEEADIIVTVTNAKTPV-FSEKLKKGVHINAVGSFMPDMQELPSEAIAR 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7710012   243 A-VLYVDSREAALKESGDV-------LLSGADIFAELGEVISGAKPAHC--EKTTVFKSLGMAVEDLVAAKLVYD 307
Cdd:PRK08618 238 AnKVVVESKEAALEETGDLivplkegLISKDDIHGELGQIISGEIAGREsdEEITVFKSVGLAVVDIVVAKYIYE 312
PRK06141 PRK06141
ornithine cyclodeaminase family protein;
7-307 6.44e-68

ornithine cyclodeaminase family protein;


Pssm-ID: 180421  Cd Length: 314  Bit Score: 214.38  E-value: 6.44e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012     7 FLSAEEVQDHLRSSSLlIPPLEAALAnfskgpdGGVMQPVRTVVPVA---KHRGFLGVMPAYSAaEDALTTKLVTFYEGH 83
Cdd:PRK06141   3 VIDAEQTRQALPFPAL-IEALRDAFA-------RGCVMPVRHVHSLEvpgEAQATLLLMPAWNE-GRYIGVKAVTVFPGN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    84 SNTAVPSHQASVLLFDPSNGSLLAVMDGNVITAKRTAAVSAIATKLLKPPGSDVLCILGAG------VQAYShyeiftEQ 157
Cdd:PRK06141  74 PARGLPGLHSTYLLFDGRTGEPLALVDGTELTARRTAAASALAASYLARKDASRLLVVGTGrlasllALAHA------SV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   158 FSFKEVRMWNRTRENAEKFASTV--QG-DVRVCSSVQEAVTGADVIITVTMATEPILFGEWVKPGAHINAVGASRPDWRE 234
Cdd:PRK06141 148 RPIKQVRVWGRDPAKAEALAAELraQGfDAEVVTDLEAAVRQADIISCATLSTEPLVRGEWLKPGTHLDLVGNFTPDMRE 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   235 LDDELMRQAVLYVDSREAALKESGDVL-------LSGADIFAELGEVISGAKPAHC--EKTTVFKSLGMAVEDLVAAKLV 305
Cdd:PRK06141 228 CDDEAIRRASVYVDTRAGALAEAGDLLipiaegvFSPDDIRGELAELCRGQHKGRTsdDEITLFKSVGTALEDLAAAILV 307


                 ..
gi 7710012   306 YD 307
Cdd:PRK06141 308 YE 309
ala_DH_arch TIGR02371
alanine dehydrogenase, Archaeoglobus fulgidus type; This enzyme, a homolog of bacterial ...
 40-307 2.43e-54

alanine dehydrogenase, Archaeoglobus fulgidus type; This enzyme, a homolog of bacterial ornithine cyclodeaminases and marsupial mu-crystallins, is a homodimeric, NAD-dependent alanine dehydrogenase found in Archaeoglobus fulgidus and several other Archaea. For a number of close homologs, scoring between trusted and noise cutoffs, it is not clear at present what is the enzymatic activity.


Pssm-ID: 131424  Cd Length: 325  Bit Score: 180.11  E-value: 2.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012     40 GGVMQPVRTVVPVAKHRGFLGVMPAYSAAEDALTTKLVTFYEGHSNTAVPSHQASVLLFDPSNGSLLAVMDGNVITAKRT 119
Cdd:TIGR02371  33 GKVQMPPKMYLFFRRYNGDLRVMPAYLEELEMAGVKCVNVHPGNPDRHLPTVMALIILVSPETGFPIALMDGTYITDMRT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    120 AAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVRMWNRTRENAEKFASTVQgDVRVCSSV----QEAVT 195
Cdd:TIGR02371 113 GAAGGVAAKYLARKDSSVLGIIGAGRQAWTQLEALSRVFDLEEVSVYCRTPSTREKFALRAS-DYEVPVRAatdpREAVE 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    196 GADVIITVTMATEPILFGEWVKPGAHINAVGASRPDWRELDDELMRQAVLYVDSREAAlKESGDV-------LLSGADIF 268
Cdd:TIGR02371 192 GCDILVTTTPSRKPVVKADWVSEGTHINAIGADAPGKQELDPEILKNAKIFVDDLEQA-THSGEInvpiskgIIRVDDLH 270

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 7710012    269 AELGEVISGAKPAHC--EKTTVFKSLGMAVEDLVAAKLVYD 307
Cdd:TIGR02371 271 ASLGEVITGLKEGRTspEEITIFDSTGLAIQDVATAWMVYE 311
PRK07340 PRK07340
delta(1)-pyrroline-2-carboxylate reductase family protein;
21-304 3.74e-51

delta(1)-pyrroline-2-carboxylate reductase family protein;


Pssm-ID: 235996  Cd Length: 304  Bit Score: 170.91  E-value: 3.74e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    21 SLLIPPLEAALANFSkgpDGGVMQPVRTVVPVAkHRGFLGVMPAysAAEDALTTKLVTFYEGHSNTAVPSHQASVLLFDP 100
Cdd:PRK07340  17 PALADALAAALLDYA---AGRIQSPERLVVPLQ-GGGVLLSMPA--SAADLAITKLVTVCPGNAARGLPTIQGEVVVADA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   101 SNGSLLAVMDGNVITAKRTAAVSAIATKLLKP-PGSDVLcILGAGVQAYSHYEIFTEQFSFKEVRMWNRTRENAEKFAST 179
Cdd:PRK07340  91 ATGERLFLLDGPTVTGRRTAAVSLLAARTLAPaPPGDLL-LIGTGVQARAHLEAFAAGLPVRRVWVRGRTAASAAAFCAH 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   180 VQG---DVRVcSSVQEAVTGADVIITVTMATEPILfGEWVKPGAHINAVGASRPDWRELDDELMRQAVLYVDSREAALKE 256
Cdd:PRK07340 170 ARAlgpTAEP-LDGEAIPEAVDLVVTATTSRTPVY-PEAARAGRLVVAVGAFTPDMAELAPRTVRGSRLYVDDPAGARHE 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 7710012   257 SGDVLLSGADI--FAELGEVISGAKPAHcEKTTVFKSLGMAVEDLVAAKL 304
Cdd:PRK07340 248 AGDLIQAGVDWsrVRPLADALRGAWPAR-GGPVLFKSVGCAAWDLAACRL 296
PRK08291 PRK08291
cyclodeaminase;
28-280 1.23e-34

cyclodeaminase;


Pssm-ID: 236221 [Multi-domain]  Cd Length: 330  Bit Score: 128.54  E-value: 1.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    28 EAALANFSKGPdggVMQPVRTVVPVAKHRGFLGVMPAYSAAEDALTTKLVTFYEGHSNTAVPSHQASVLLFDPSNGSLLA 107
Cdd:PRK08291  27 EAAFAALATGA---VAMPPILRLDIPEHRGEVDVKTAYIPGLDSFAIKVSPGFFDNPKLGLPSLNGLMVVLSARTGLVEA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   108 VM-DGNVITAKRTAAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVRMWNRTRENAEKFASTVQG---- 182
Cdd:PRK08291 104 LLlDNGYLTDVRTAAAGAVAARHLAREDASRAAVIGAGEQARLQLEALTLVRPIREVRVWARDAAKAEAYAADLRAelgi 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   183 DVRVCSSVQEAVTGADVIITVTMATEPILFGEWVKPGAHINAVGASRPDWRELDDELMRQAVLYV-DS-----REAALKE 256
Cdd:PRK08291 184 PVTVARDVHEAVAGADIIVTTTPSEEPILKAEWLHPGLHVTAMGSDAEHKNEIAPAVFAAADLYVcDRlsqtrRLGELHH 263

                        250       260
                 ....*....|....*....|....*
gi 7710012   257 SGDVLLSGAD-IFAELGEVISGAKP 280
Cdd:PRK08291 264 AIAAGLVAADaVFPELGQVIAGRRP 288
PRK07589 PRK07589
ornithine cyclodeaminase; Validated
 105-307 1.23e-32

ornithine cyclodeaminase; Validated


Pssm-ID: 236064  Cd Length: 346  Bit Score: 123.46  E-value: 1.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   105 LLAVMdgNVITAKRTAAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVRMWNRTRENAEKFASTVQG-- 182
Cdd:PRK07589 101 LLSEM--TLLTALRTAATSALAAKYLARPDSRTMALIGNGAQSEFQALAFKALLGIEEIRLYDIDPAATAKLARNLAGpg 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   183 -DVRVCSSVQEAVTGADVIITVTM----ATepILFGEWVKPGAHINAVGASRPDWRELDDELMRQAVLYVDSREAALKEs 257
Cdd:PRK07589 179 lRIVACRSVAEAVEGADIITTVTAdktnAT--ILTDDMVEPGMHINAVGGDCPGKTELHPDILRRARVFVEYEPQTRIE- 255

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 7710012   258 GDVLLSGAD-IFAELGEVISGAKP--AHCEKTTVFKSLGMAVEDLVAAKLVYD 307
Cdd:PRK07589 256 GEIQQLPADfPVTELWRVLTGEAPgrESADQITLFDSVGFALEDFSALRYVRD 308
PRK06407 PRK06407
ornithine cyclodeaminase; Provisional
 7-305 3.03e-32

ornithine cyclodeaminase; Provisional


Pssm-ID: 180556  Cd Length: 301  Bit Score: 121.59  E-value: 3.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012     7 FLSAEEVQDHLRSSSLlIPPLEAALANFSKGPDGGVMQpVRTVVPvakhRGFLGVMPAYSAAEDALTTKlvTFYEGHSNT 86
Cdd:PRK06407   3 YISEDDVLRNLNMKEC-IGALREAFEEYGAGRANSSTR-VRTFSP----GHVLNTMPAYMEKYHIAGLK--TYIAGRNGA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    87 avpshQASVLLFDPSNGSLLAVMDGNVITAKRTAAVSAIATKLLKPPGsDVLCILGAGVQAYSHYEIFTEQFSFKEVRMW 166
Cdd:PRK06407  75 -----RFVVLLFDVNNPELVAIFEANRLGQIRTGAVTAYATSILHKNV-ENFTIIGSGFQAETQLEGMASVYNPKRIRVY 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   167 NRTRENAEKFASTVQ----GDVRVCSSVQEAVTGADVIITVTMATEPILFGEWVKPGAHINAVGASRPDWRELDDELMRQ 242
Cdd:PRK06407 149 SRNFDHARAFAERFSkefgVDIRPVDNAEAALRDADTITSITNSDTPIFNRKYLGDEYHVNLAGSNYPNRREAEHSVLND 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7710012   243 A-VLYVDSREAALKESGDVL----LSGADIfaELGEVISGAKPAHCEKTTVFKSLGMAVEDLVAAKLV 305
Cdd:PRK06407 229 AdIVVTEHMEQSLRESSEISeyvkKGGKPV--ELKDFAKNNGSYSGLRRTVFKSMGIGLEDIAAGYLV 294
PRK06823 PRK06823
ornithine cyclodeaminase family protein;
8-311 9.49e-30

ornithine cyclodeaminase family protein;


Pssm-ID: 136070  Cd Length: 315  Bit Score: 114.87  E-value: 9.49e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012     8 LSAEEVQDHLrSSSLLIPPLEAALANFSKGpdggvmqpvRTVVPVAKHRGFLG------VMPAYSAAEDALTTKLVTFYE 81
Cdd:PRK06823   4 LNKQKILAKF-DADRATLLLKEGFIAFSQG---------RVQMPPVQHLLFDQangdccIKSGYLQGDDQFVVKVSTGFY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    82 GHSNTAVPSHQASVLLFDPSNGSLLAVM-DGNVITAKRTAAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSF 160
Cdd:PRK06823  74 DNPAQGLPSNQGLMLAFSAKTGEPQALLlDEGWLTALRTALAGRIVARLLAPQHVSAIGIVGTGIQARMQLMYLKNVTDC 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   161 KEVRMWNRTRENAEK---FASTVQGDVRVCSSVQEAVTGADVIITVTMATEPILFGEWVKPGAHINAVGASRPDWRELDD 237
Cdd:PRK06823 154 RQLWVWGRSETALEEyrqYAQALGFAVNTTLDAAEVAHAANLIVTTTPSREPLLQAEDIQPGTHITAVGADSPGKQELDA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   238 ELMRQA-VLYVDSREAALkESGDV-------LLSGADIfAELGEVISGAKP--AHCEKTTVFKSLGMAVEDLVAAKLVYD 307
Cdd:PRK06823 234 ELVARAdKILVDSIAQCT-DFGEVshafkagLLAHHNL-TELGLALAQGIPfrENDQQITLADLTGVAIQDVQIAKGILG 311


                 ....
gi 7710012   308 SWSS 311
Cdd:PRK06823 312 DLKG 315
PRK06199 PRK06199
ornithine cyclodeaminase; Validated
 94-306 3.29e-18

ornithine cyclodeaminase; Validated


Pssm-ID: 235738  Cd Length: 379  Bit Score: 83.99  E-value: 3.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    94 SVLLF---DPSNGSLLAVMDGNVITAKRTAAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQF-SFKEVRMWNRT 169
Cdd:PRK06199 111 SILMFvlnDADTGAPLAIMSANLLSAYRTGAVPGVGARHLARKDSKVVGLLGPGVMGKTILAAFMAVCpGIDTIKIKGRG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   170 RENAEKFASTVQG------DVRVCSSVQEAVTGADVIITVT------MATEPILFGEWVKPGAHINAVGASRpdwreLDD 237
Cdd:PRK06199 191 QKSLDSFATWVAEtypqitNVEVVDSIEEVVRGSDIVTYCNsgetgdPSTYPYVKREWVKPGAFLLMPAACR-----IDE 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012   238 ELMRQAV-LYVDSR---EAALKESG---------------DVLLSG---ADIFAELGEVISGAKPA--HCEKTTVFKSLG 293
Cdd:PRK06199 266 GMEQGDVrKVVDNTglyEAWFEEVPkpahnlipvigvrfmDMIAEGkltLDQLEDIGDIVAGKAPGrqNDEEIIIMSVGG 345

                        250
                 ....*....|...
gi 7710012   294 MAVEDLVAAKLVY 306
Cdd:PRK06199 346 MPVEDVAWGTVVY 358
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 167-211 6.16e-06

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: 47.41  E-value: 6.16e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 7710012  167 NRTRENAEKFASTVQGDVRVCSSVQEAVTGADVIITVTMATEPIL 211
Cdd:COG0373 213 NRTLERAEELAEEFGGEAVPLEELPEALAEADIVISSTGAPHPVI 257
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 167-211 8.66e-06

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 46.72  E-value: 8.66e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 7710012   167 NRTRENAEKFASTVQGDVRVCSSVQEAVTGADVIITVTMATEPIL 211
Cdd:PRK00045 213 NRTLERAEELAEEFGGEAIPLDELPEALAEADIVISSTGAPHPII 257
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 162-249 1.04e-05

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 44.77  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012    162 EVRMWNRTRENAEKFastVQGDVRVCSSVQEAVTGADVIITVTMATEP---ILFGEWVKPGAHINAV-----GASRPDWR 233
Cdd:pfam03446  24 TVTVYNRTPEKVEEL---VAAGAIAAASPAEFVAGLDVVITMVPAGAAvdaVIFGEGLLPGLKPGDIiidgsTSSPEDAR 100

                          90
                  ....*....|....*.
gi 7710012    234 ELDDELMRQAVLYVDS 249
Cdd:pfam03446 101 RRAKELKEKGLHFLDA 116
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 162-283 3.04e-05

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 44.72  E-value: 3.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012  162 EVRMWNRTRENAEKFAStvQGdVRVCSSVQEAVTGADVIIT-VTM--ATEPILFGE-----WVKPGA-HINaVGASRPDW 232
Cdd:COG2084  26 EVTVWNRTPAKAEALVA--AG-ARVAASPAEAAAAADVVITmLPDdaAVEEVLLGEdgllaALRPGAvVVD-MSTISPET 101

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012  233 -RELDDELMRQAVLYVD-----SREAALKESGDVLLSG-ADIFAELGEVIS--GAKPAHC 283
Cdd:COG2084 102 aRELAAAAAARGVRYLDapvsgGPAGAEAGTLTIMVGGdEAAFERARPVLEamGKRIVHV 161
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 161-219 7.14e-05

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 41.79  E-value: 7.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7710012    161 KEVRMWNRTRENAEKFASTVQGdVRVC--SSVQEAVTGADVIITVTMATEPILFGEWVKPG 219
Cdd:pfam01488  37 KEVTIANRTIERAQELAEKFGG-VEALplDDLKEYLAEADIVISATSSPTPIITKEMVERA 96
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
168-231 6.13e-04

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 40.98  E-value: 6.13e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7710012  168 RTRENAEKFASTVQGDVRVCSSVQEAVTGADVIITVTMATEPILFGEWVKPGAHI----------NAVGASRPD 231
Cdd:COG5322 187 RLEELAEEILRNPGGKVTITTDIDEALREADIVVTVTSAVGAIIDPEDLKPGAVVcdvarprdvsRRVAEKRPD 260
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
 122-201 1.13e-03

Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439939 [Multi-domain]  Cd Length: 270  Bit Score: 39.74  E-value: 1.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710012  122 VSAIATKLLKPPGSDVLcILGAG-----VQAYSHyeifteQFSFKEVRMWNRTRENAEKFASTVQGDVRVCSSVQEAVTG 196
Cdd:COG0169 109 VRALREAGVDLAGKRVL-VLGAGgaaraVAAALA------EAGAAEITIVNRTPERAEALAARLGVRAVPLDDLAAALAG 181


                ....*
gi 7710012  197 ADVII 201
Cdd:COG0169 182 ADLVI 186
 
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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