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Conserved domains on  [gi|489534381|ref|WP_003439110|]
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ornithine cyclodeaminase family protein [Clostridioides difficile]

Protein Classification

ornithine cyclodeaminase family protein( domain architecture ID 11483382)

ornithine cyclodeaminase family protein similar to Bacillus cereus delta(1)-pyrroline-2-carboxylate reductase, which catalyzes the reduction of delta(1)-pyrroline-2-carboxylate (Pyr2C) to L-proline, preferentially using NADPH over NADH as the electron donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08618 PRK08618
ornithine cyclodeaminase family protein;
1-329 0e+00

ornithine cyclodeaminase family protein;


:

Pssm-ID: 236313 [Multi-domain]  Cd Length: 325  Bit Score: 520.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381   1 MLLLKKDDIKKVFTMRDAIEADKEAFRIYCEGKSVNPLRTNISVPSQDASMLFMPGYVEELGCGGIKIVSVFPKNAQKGK 80
Cdd:PRK08618   1 MLVLSAEDQKKLFNMNEAIEADKEALKAYSEGKTITPLRTNLPFPNENNTSLIMPGYAEGLEALGLKIVSVVPENKKKGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  81 PVIPATVLLLDGETGEVSAVLDGTYVTQIRTGAASGAAIDVLAKKDSKIGALIGLGGQGEPQLEAMIEARNLDEVRVFSR 160
Cdd:PRK08618  81 PTIPGTVILSDFETGEVLAILDGTYLTQIRTGALSGVATKYLAREDAKTLCLIGTGGQAKGQLEAVLAVRDIERVRVYSR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 161 NKESREKFAEEMNlklSKYNTKIVAVESSDEAIDNADVIVLATPSKQPVLNgNLVKKGALISAVGSYMPDMQELCPNCLT 240
Cdd:PRK08618 161 TFEKAYAFAQEIQ---SKFNTEIYVVNSADEAIEEADIIVTVTNAKTPVFS-EKLKKGVHINAVGSFMPDMQELPSEAIA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 241 RASKIFFESTDAVLSESGDILIPLKEGKISKDDFSGDLGNVINGTIPGREDDDEIIVFKTVGIGVQDVVTAKRIYDKAKE 320
Cdd:PRK08618 237 RANKVVVESKEAALEETGDLIVPLKEGLISKDDIHGELGQIISGEIAGRESDEEITVFKSVGLAVVDIVVAKYIYEKAVE 316


                 ....*....
gi 489534381 321 NGIGIDWKW 329
Cdd:PRK08618 317 NGVGKEIEF 325
 
Name Accession Description Interval E-value
PRK08618 PRK08618
ornithine cyclodeaminase family protein;
1-329 0e+00

ornithine cyclodeaminase family protein;


Pssm-ID: 236313 [Multi-domain]  Cd Length: 325  Bit Score: 520.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381   1 MLLLKKDDIKKVFTMRDAIEADKEAFRIYCEGKSVNPLRTNISVPSQDASMLFMPGYVEELGCGGIKIVSVFPKNAQKGK 80
Cdd:PRK08618   1 MLVLSAEDQKKLFNMNEAIEADKEALKAYSEGKTITPLRTNLPFPNENNTSLIMPGYAEGLEALGLKIVSVVPENKKKGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  81 PVIPATVLLLDGETGEVSAVLDGTYVTQIRTGAASGAAIDVLAKKDSKIGALIGLGGQGEPQLEAMIEARNLDEVRVFSR 160
Cdd:PRK08618  81 PTIPGTVILSDFETGEVLAILDGTYLTQIRTGALSGVATKYLAREDAKTLCLIGTGGQAKGQLEAVLAVRDIERVRVYSR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 161 NKESREKFAEEMNlklSKYNTKIVAVESSDEAIDNADVIVLATPSKQPVLNgNLVKKGALISAVGSYMPDMQELCPNCLT 240
Cdd:PRK08618 161 TFEKAYAFAQEIQ---SKFNTEIYVVNSADEAIEEADIIVTVTNAKTPVFS-EKLKKGVHINAVGSFMPDMQELPSEAIA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 241 RASKIFFESTDAVLSESGDILIPLKEGKISKDDFSGDLGNVINGTIPGREDDDEIIVFKTVGIGVQDVVTAKRIYDKAKE 320
Cdd:PRK08618 237 RANKVVVESKEAALEETGDLIVPLKEGLISKDDIHGELGQIISGEIAGRESDEEITVFKSVGLAVVDIVVAKYIYEKAVE 316


                 ....*....
gi 489534381 321 NGIGIDWKW 329
Cdd:PRK08618 317 NGVGKEIEF 325
OCDMu COG2423
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid ...
 1-327 2.40e-146

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: 414.93  E-value: 2.40e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381   1 MLLLKKDDIKKVFTMRDAIEADKEAFRIYCEGKSVNPLRTNISVPSQDASMLFMPGYVEELGCGGIKIVSVFPKNAQKGK 80
Cdd:COG2423    1 MLILSAEDVAALLDMDDAIDAVEEAFRALARGRVVMPPRTVLDLPEAGGTLLLMPAYIPGGGAFGVKVVSVFPGNPARGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  81 PVIPATVLLLDGETGEVSAVLDGTYVTQIRTGAASGAAIDVLAKKDSKIGALIGLGGQGEPQLEAMIEARNLDEVRVFSR 160
Cdd:COG2423   81 PTVQGTVLLFDAETGEPLALLDGTLLTALRTAAASALAARYLARPDARTLGIIGAGVQARTQLRALAAVRPIERVRVWGR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 161 NKESREKFAEEMnlklSKYNTKIVAVESSDEAIDNADVIVLATPSKQPVLNGNLVKKGALISAVGSYMPDMQELCPNCLT 240
Cdd:COG2423  161 DPEKAEAFAARL----AAEGLPVEAADDLEEAVADADIIVTATPSREPVLRGEWLRPGTHINAVGADTPGKRELDPALLA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 241 RAsKIFFESTDAVLSESGDILIPLKEGKISKDDFSGDLGNVINGTIPGREDDDEIIVFKTVGIGVQDVVTAKRIYDKAKE 320
Cdd:COG2423  237 RA-RVVVDSREQALAEAGELQHALAAGLISEDDIVAELGEVLAGRAPGRTSDDEITVFKSVGLALQDLAAARLVYERARA 315


                 ....*..
gi 489534381 321 NGIGIDW 327
Cdd:COG2423  316 AGLGTEV 322
OCD_Mu_crystall pfam02423
Ornithine cyclodeaminase/mu-crystallin family; This family contains the bacterial Ornithine ...
 15-322 4.60e-72

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: 225.81  E-value: 4.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381   15 MRDAIEADKEAFRIYCEGKSVNPLRTNISVPSQDASMLFMPGYVEELGCGGIKIVSVFPKNAQKGKPVIPATVLLLDGET 94
Cdd:pfam02423  16 MDDLAGYVEEAFRRWSLGTFDKPPRVASHSRDGDGVLEAMPAYLGGRKLYGVKWVNSHPGNPDSGLPTVTATGVLNDPST 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381   95 GEVSAVLDGTYVTQIRTGAASGAAIDVLAKKDSKIGALIGLGGQGEPQLEAMIEARNLDEVRVFSRNKESREKFAeemnL 174
Cdd:pfam02423  96 GYPLALMDATLLTALRTAAVSAVAAKYLAPKDASVLAIIGNGVQAEFQAEAFRAVFGIDEVRIYDRDPRATEKFA----R 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  175 KLSKYNTKIVAVESSDEAIDNADVIVLATPSKQ--PVLNGNLVKKGALISAVGSYMPDMQELCPNCLTRAsKIFFEStDA 252
Cdd:pfam02423 172 NAQEPGFEVRACTSPEEAVEGADIIITVTADKAnaPILKDEWVKPGAHINAVGADRPGKTELDDDILKRA-DIFVEY-EA 249

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  253 VLSESGDILIplkegkISKDDFSGDLGNVINGTIPGREDDDEIIVFKTVGIGVQDVVTAKRIYDKAKENG 322
Cdd:pfam02423 250 QAREEGEIQQ------LLVDDPVAELGEVITGKKPGRTSDEEITLFDSVGMAIEDVAAARYVYERALSKG 313
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 112-225 6.85e-04

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. 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: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 40.07  E-value: 6.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 112 GAASGAAIDVLAK-----KDSKIGALIGLGGQGepQLEAMIEARNLDEVRVFSRNKESREKFAEEMNlklSKYNTKIVAV 186
Cdd:cd01078    9 AAAVAAAGKALELmgkdlKGKTAVVLGGTGPVG--QRAAVLLAREGARVVLVGRDLERAQKAADSLR---ARFGEGVGAV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489534381 187 ESSD-----EAIDNADVIVLATPS--KQPVLNGNLVKKGALISAVG 225
Cdd:cd01078   84 ETSDdaaraAAIKGADVVFAAGAAgvELLEKLAWAPKPLAVAADVN 129
 
Name Accession Description Interval E-value
PRK08618 PRK08618
ornithine cyclodeaminase family protein;
1-329 0e+00

ornithine cyclodeaminase family protein;


Pssm-ID: 236313 [Multi-domain]  Cd Length: 325  Bit Score: 520.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381   1 MLLLKKDDIKKVFTMRDAIEADKEAFRIYCEGKSVNPLRTNISVPSQDASMLFMPGYVEELGCGGIKIVSVFPKNAQKGK 80
Cdd:PRK08618   1 MLVLSAEDQKKLFNMNEAIEADKEALKAYSEGKTITPLRTNLPFPNENNTSLIMPGYAEGLEALGLKIVSVVPENKKKGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  81 PVIPATVLLLDGETGEVSAVLDGTYVTQIRTGAASGAAIDVLAKKDSKIGALIGLGGQGEPQLEAMIEARNLDEVRVFSR 160
Cdd:PRK08618  81 PTIPGTVILSDFETGEVLAILDGTYLTQIRTGALSGVATKYLAREDAKTLCLIGTGGQAKGQLEAVLAVRDIERVRVYSR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 161 NKESREKFAEEMNlklSKYNTKIVAVESSDEAIDNADVIVLATPSKQPVLNgNLVKKGALISAVGSYMPDMQELCPNCLT 240
Cdd:PRK08618 161 TFEKAYAFAQEIQ---SKFNTEIYVVNSADEAIEEADIIVTVTNAKTPVFS-EKLKKGVHINAVGSFMPDMQELPSEAIA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 241 RASKIFFESTDAVLSESGDILIPLKEGKISKDDFSGDLGNVINGTIPGREDDDEIIVFKTVGIGVQDVVTAKRIYDKAKE 320
Cdd:PRK08618 237 RANKVVVESKEAALEETGDLIVPLKEGLISKDDIHGELGQIISGEIAGRESDEEITVFKSVGLAVVDIVVAKYIYEKAVE 316


                 ....*....
gi 489534381 321 NGIGIDWKW 329
Cdd:PRK08618 317 NGVGKEIEF 325
OCDMu COG2423
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid ...
 1-327 2.40e-146

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: 414.93  E-value: 2.40e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381   1 MLLLKKDDIKKVFTMRDAIEADKEAFRIYCEGKSVNPLRTNISVPSQDASMLFMPGYVEELGCGGIKIVSVFPKNAQKGK 80
Cdd:COG2423    1 MLILSAEDVAALLDMDDAIDAVEEAFRALARGRVVMPPRTVLDLPEAGGTLLLMPAYIPGGGAFGVKVVSVFPGNPARGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  81 PVIPATVLLLDGETGEVSAVLDGTYVTQIRTGAASGAAIDVLAKKDSKIGALIGLGGQGEPQLEAMIEARNLDEVRVFSR 160
Cdd:COG2423   81 PTVQGTVLLFDAETGEPLALLDGTLLTALRTAAASALAARYLARPDARTLGIIGAGVQARTQLRALAAVRPIERVRVWGR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 161 NKESREKFAEEMnlklSKYNTKIVAVESSDEAIDNADVIVLATPSKQPVLNGNLVKKGALISAVGSYMPDMQELCPNCLT 240
Cdd:COG2423  161 DPEKAEAFAARL----AAEGLPVEAADDLEEAVADADIIVTATPSREPVLRGEWLRPGTHINAVGADTPGKRELDPALLA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 241 RAsKIFFESTDAVLSESGDILIPLKEGKISKDDFSGDLGNVINGTIPGREDDDEIIVFKTVGIGVQDVVTAKRIYDKAKE 320
Cdd:COG2423  237 RA-RVVVDSREQALAEAGELQHALAAGLISEDDIVAELGEVLAGRAPGRTSDDEITVFKSVGLALQDLAAARLVYERARA 315


                 ....*..
gi 489534381 321 NGIGIDW 327
Cdd:COG2423  316 AGLGTEV 322
OCD_Mu_crystall pfam02423
Ornithine cyclodeaminase/mu-crystallin family; This family contains the bacterial Ornithine ...
 15-322 4.60e-72

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: 225.81  E-value: 4.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381   15 MRDAIEADKEAFRIYCEGKSVNPLRTNISVPSQDASMLFMPGYVEELGCGGIKIVSVFPKNAQKGKPVIPATVLLLDGET 94
Cdd:pfam02423  16 MDDLAGYVEEAFRRWSLGTFDKPPRVASHSRDGDGVLEAMPAYLGGRKLYGVKWVNSHPGNPDSGLPTVTATGVLNDPST 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381   95 GEVSAVLDGTYVTQIRTGAASGAAIDVLAKKDSKIGALIGLGGQGEPQLEAMIEARNLDEVRVFSRNKESREKFAeemnL 174
Cdd:pfam02423  96 GYPLALMDATLLTALRTAAVSAVAAKYLAPKDASVLAIIGNGVQAEFQAEAFRAVFGIDEVRIYDRDPRATEKFA----R 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  175 KLSKYNTKIVAVESSDEAIDNADVIVLATPSKQ--PVLNGNLVKKGALISAVGSYMPDMQELCPNCLTRAsKIFFEStDA 252
Cdd:pfam02423 172 NAQEPGFEVRACTSPEEAVEGADIIITVTADKAnaPILKDEWVKPGAHINAVGADRPGKTELDDDILKRA-DIFVEY-EA 249

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  253 VLSESGDILIplkegkISKDDFSGDLGNVINGTIPGREDDDEIIVFKTVGIGVQDVVTAKRIYDKAKENG 322
Cdd:pfam02423 250 QAREEGEIQQ------LLVDDPVAELGEVITGKKPGRTSDEEITLFDSVGMAIEDVAAARYVYERALSKG 313
PRK06141 PRK06141
ornithine cyclodeaminase family protein;
1-321 3.50e-70

ornithine cyclodeaminase family protein;


Pssm-ID: 180421  Cd Length: 314  Bit Score: 220.93  E-value: 3.50e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381   1 MLLLKKDDIKKVFTMRDAIEADKEAFRIYCegksVNPLRT--NISVPSQ-DASMLFMPGYVEELGCGgIKIVSVFPKNAQ 77
Cdd:PRK06141   1 MLVIDAEQTRQALPFPALIEALRDAFARGC----VMPVRHvhSLEVPGEaQATLLLMPAWNEGRYIG-VKAVTVFPGNPA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  78 KGKPVIPATVLLLDGETGEVSAVLDGTYVTQIRTGAASGAAIDVLAKKDSKIGALIGLGGQGEPQLEAMIEARNLDEVRV 157
Cdd:PRK06141  76 RGLPGLHSTYLLFDGRTGEPLALVDGTELTARRTAAASALAASYLARKDASRLLVVGTGRLASLLALAHASVRPIKQVRV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 158 FSRNKESREKFAEEmnlkLSKYNTKIVAVESSDEAIDNADVIVLATPSKQPVLNGNLVKKGALISAVGSYMPDMQELCPN 237
Cdd:PRK06141 156 WGRDPAKAEALAAE----LRAQGFDAEVVTDLEAAVRQADIISCATLSTEPLVRGEWLKPGTHLDLVGNFTPDMRECDDE 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 238 CLTRASkIFFESTDAVLSESGDILIPLKEGKISKDDFSGDLGNVINGTIPGREDDDEIIVFKTVGIGVQDVVTAKRIYDK 317
Cdd:PRK06141 232 AIRRAS-VYVDTRAGALAEAGDLLIPIAEGVFSPDDIRGELAELCRGQHKGRTSDDEITLFKSVGTALEDLAAAILVYEA 310


                 ....
gi 489534381 318 AKEN 321
Cdd:PRK06141 311 LNGR 314
PRK08291 PRK08291
cyclodeaminase;
1-324 1.49e-49

cyclodeaminase;


Pssm-ID: 236221 [Multi-domain]  Cd Length: 330  Bit Score: 168.22  E-value: 1.49e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381   1 MLLLKKDDIKKVFTM-RDAIEADKEAFRIYCEGKSVNPLRTNISVPSQDASMLFMPGYVEELGCGGIKIVSVFPKNAQKG 79
Cdd:PRK08291   4 MTILTEAELRALVPLdLDAIDCVEAAFAALATGAVAMPPILRLDIPEHRGEVDVKTAYIPGLDSFAIKVSPGFFDNPKLG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  80 KPVIPATVLLLDGETGEVSAVL-DGTYVTQIRTGAASGAAIDVLAKKDSKIGALIGLGGQGEPQLEAMIEARNLDEVRVF 158
Cdd:PRK08291  84 LPSLNGLMVVLSARTGLVEALLlDNGYLTDVRTAAAGAVAARHLAREDASRAAVIGAGEQARLQLEALTLVRPIREVRVW 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 159 SRNKESREKFAEEMNLKLskyNTKIVAVESSDEAIDNADVIVLATPSKQPVLNGNLVKKGALISAVGSYMPDMQELCPNC 238
Cdd:PRK08291 164 ARDAAKAEAYAADLRAEL---GIPVTVARDVHEAVAGADIIVTTTPSEEPILKAEWLHPGLHVTAMGSDAEHKNEIAPAV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 239 LTRASKIFFEStdavLSES---GDILIPLKEGKISKDDFSGDLGNVINGTIPGREDDDEIIVFKTVGIGVQDVVTAKRIY 315
Cdd:PRK08291 241 FAAADLYVCDR----LSQTrrlGELHHAIAAGLVAADAVFPELGQVIAGRRPGRTSDDDITICDLTGTGVQDTAIATLAL 316


                 ....*....
gi 489534381 316 DKAKENGIG 324
Cdd:PRK08291 317 ARARAAGAG 325
PRK06407 PRK06407
ornithine cyclodeaminase; Provisional
 1-314 7.47e-41

ornithine cyclodeaminase; Provisional


Pssm-ID: 180556  Cd Length: 301  Bit Score: 144.70  E-value: 7.47e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381   1 MLLLKKDDIKKVFTMRDAIEADKEAFRIYCEGKSVNPLRTNISvpSQDASMLFMPGYVEELGCGGIKIVSVfpknaqkGK 80
Cdd:PRK06407   1 MYYISEDDVLRNLNMKECIGALREAFEEYGAGRANSSTRVRTF--SPGHVLNTMPAYMEKYHIAGLKTYIA-------GR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  81 PVIPATVLLLDGETGEVSAVLDGTYVTQIRTGAASGAAIDVLaKKDSKIGALIGLGGQGEPQLEAMIEARNLDEVRVFSR 160
Cdd:PRK06407  72 NGARFVVLLFDVNNPELVAIFEANRLGQIRTGAVTAYATSIL-HKNVENFTIIGSGFQAETQLEGMASVYNPKRIRVYSR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 161 NKESREKFAEEMNLklsKYNTKIVAVESSDEAIDNADVIVLATPSKQPVLNGNLVKKGALISAVGSYMPDMQELCPNCLT 240
Cdd:PRK06407 151 NFDHARAFAERFSK---EFGVDIRPVDNAEAALRDADTITSITNSDTPIFNRKYLGDEYHVNLAGSNYPNRREAEHSVLN 227

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489534381 241 RASKIFFESTDAVLSESGDILIPLKEGK--ISKDDFSGDlgnvingtiPGREDDDEIIVFKTVGIGVQDVVTAKRI 314
Cdd:PRK06407 228 DADIVVTEHMEQSLRESSEISEYVKKGGkpVELKDFAKN---------NGSYSGLRRTVFKSMGIGLEDIAAGYLV 294
PRK07340 PRK07340
delta(1)-pyrroline-2-carboxylate reductase family protein;
17-307 1.70e-40

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


Pssm-ID: 235996  Cd Length: 304  Bit Score: 143.56  E-value: 1.70e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  17 DAIEAdkeAFRIYCEGKSVNPLRTNISVPsQDASMLFMPGYVEELGCggIKIVSVFPKNAQKGKPVIPATVLLLDGETGE 96
Cdd:PRK07340  21 DALAA---ALLDYAAGRIQSPERLVVPLQ-GGGVLLSMPASAADLAI--TKLVTVCPGNAARGLPTIQGEVVVADAATGE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  97 VSAVLDGTYVTQIRTGAASGAAIDVLAKKDSKIGALIGLGGQGEPQLEAMIEARNLDEVRVFSRNKESREKFAEE---MN 173
Cdd:PRK07340  95 RLFLLDGPTVTGRRTAAVSLLAARTLAPAPPGDLLLIGTGVQARAHLEAFAAGLPVRRVWVRGRTAASAAAFCAHaraLG 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 174 LKLskyntkivAVESSDEAIDNADVIVLATPSKQPVLNGnLVKKGALISAVGSYMPDMQELCPNcLTRASKIFFESTDAV 253
Cdd:PRK07340 175 PTA--------EPLDGEAIPEAVDLVVTATTSRTPVYPE-AARAGRLVVAVGAFTPDMAELAPR-TVRGSRLYVDDPAGA 244

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489534381 254 LSESGDILiplkegkISKDDFS--GDLGNVINGTIPgreDDDEIIVFKTVGIGVQD 307
Cdd:PRK07340 245 RHEAGDLI-------QAGVDWSrvRPLADALRGAWP---ARGGPVLFKSVGCAAWD 290
PRK07589 PRK07589
ornithine cyclodeaminase; Validated
 65-326 4.35e-37

ornithine cyclodeaminase; Validated


Pssm-ID: 236064  Cd Length: 346  Bit Score: 135.79  E-value: 4.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  65 GIKIVSVFPKNAQKGKPVIPATVLLLDGETGEVSAVLDGTYVTQIRTGAASGAAIDVLAKKDSKIGALIGLGGQGEPQLE 144
Cdd:PRK07589  67 SFKYVNGHPKNTRRGLQTVMAFGVLADVDTGYPLLLSEMTLLTALRTAATSALAAKYLARPDSRTMALIGNGAQSEFQAL 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 145 AMIEARNLDEVRVFSRNKESREKFAEemnlKLSKYNTKIVAVESSDEAIDNADVIVLATPSKQ--PVLNGNLVKKGALIS 222
Cdd:PRK07589 147 AFKALLGIEEIRLYDIDPAATAKLAR----NLAGPGLRIVACRSVAEAVEGADIITTVTADKTnaTILTDDMVEPGMHIN 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 223 AVGSYMPDMQELCPNCLTRAsKIFFEstdavLSESGDIliplkEGKISK--DDFS-GDLGNVINGTIPGREDDDEIIVFK 299
Cdd:PRK07589 223 AVGGDCPGKTELHPDILRRA-RVFVE-----YEPQTRI-----EGEIQQlpADFPvTELWRVLTGEAPGRESADQITLFD 291

                        250       260
                 ....*....|....*....|....*..
gi 489534381 300 TVGIGVQDVVTAKRIYDKAKENGIGID 326
Cdd:PRK07589 292 SVGFALEDFSALRYVRDLAEDTGLGEQ 318
PRK06823 PRK06823
ornithine cyclodeaminase family protein;
1-315 1.15e-34

ornithine cyclodeaminase family protein;


Pssm-ID: 136070  Cd Length: 315  Bit Score: 128.74  E-value: 1.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381   1 MLLLKKDDIKKVFTMRDAIEADKEAFRIYCEGKSVNPLRTNISVPSQDASMLFMPGYVEELGCGGIKIVSVFPKNAQKGK 80
Cdd:PRK06823   1 MKILNKQKILAKFDADRATLLLKEGFIAFSQGRVQMPPVQHLLFDQANGDCCIKSGYLQGDDQFVVKVSTGFYDNPAQGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  81 PVIPATVLLLDGETGEVSAVL-DGTYVTQIRTGAASGAAIDVLAKKDSKIGALIGLGGQGEPQLEAMIEARNLDEVRVFS 159
Cdd:PRK06823  81 PSNQGLMLAFSAKTGEPQALLlDEGWLTALRTALAGRIVARLLAPQHVSAIGIVGTGIQARMQLMYLKNVTDCRQLWVWG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 160 RNKESREKFAEEMNLKLSKYNTKIVAVESSDEAidnaDVIVLATPSKQPVLNGNLVKKGALISAVGSYMPDMQELCPNCL 239
Cdd:PRK06823 161 RSETALEEYRQYAQALGFAVNTTLDAAEVAHAA----NLIVTTTPSREPLLQAEDIQPGTHITAVGADSPGKQELDAELV 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489534381 240 TRASKIFFESTdAVLSESGDILIPLKEGKISKDDFSgDLGNVINGTIPGREDDDEIIVFKTVGIGVQDVVTAKRIY 315
Cdd:PRK06823 237 ARADKILVDSI-AQCTDFGEVSHAFKAGLLAHHNLT-ELGLALAQGIPFRENDQQITLADLTGVAIQDVQIAKGIL 310
PRK06199 PRK06199
ornithine cyclodeaminase; Validated
 36-325 2.03e-34

ornithine cyclodeaminase; Validated


Pssm-ID: 235738  Cd Length: 379  Bit Score: 129.44  E-value: 2.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  36 NPLRTNISVPSQDASMLFMPGYveeLG----CGGIKIVSVFPKNAQKGKPVIPATVLLLDGETGEVSAVLDGTYVTQIRT 111
Cdd:PRK06199  63 NSPFPTMPKPTPDRRFMAMPAY---LGgrfrTAGVKWYGSNIANREKGLPRSILMFVLNDADTGAPLAIMSANLLSAYRT 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 112 GAASGAAIDVLAKKDSKIGALIGLGGQGEPQLEAMIEAR-NLDEVRVFSRNKESREKFAEEMNLKLsKYNTKIVAVESSD 190
Cdd:PRK06199 140 GAVPGVGARHLARKDSKVVGLLGPGVMGKTILAAFMAVCpGIDTIKIKGRGQKSLDSFATWVAETY-PQITNVEVVDSIE 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 191 EAIDNADVIVLAT------PSKQPVLNGNLVKKGALISavgsyMPDMQELCPNCLTRASKIFFEST---DAVLSESGD-- 259
Cdd:PRK06199 219 EVVRGSDIVTYCNsgetgdPSTYPYVKREWVKPGAFLL-----MPAACRIDEGMEQGDVRKVVDNTglyEAWFEEVPKpa 293

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489534381 260 -ILIPL---------KEGKISKDDFSgDLGNVINGTIPGREDDDEIIVFKTVGIGVQDVVTAKRIYDKAKENGIGI 325
Cdd:PRK06199 294 hNLIPVigvrfmdmiAEGKLTLDQLE-DIGDIVAGKAPGRQNDEEIIIMSVGGMPVEDVAWGTVVYRNALEKGIGV 368
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 107-217 4.47e-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: 47.80  E-value: 4.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 107 TQIRTGAAS--GAAIDvLAKK-----DSKIGALIGLGgqgepqleAMIE--ARNL-----DEVRVFSRNKESREKFAEEm 172
Cdd:COG0373  156 TGIGEGAVSvsSAAVE-LAKKifgdlSGKTVLVIGAG--------EMGElaARHLaakgvKRITVANRTLERAEELAEE- 225

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489534381 173 nlklskYNTKIVAVESSDEAIDNADVIVLATPSKQPVLNGNLVKK 217
Cdd:COG0373  226 ------FGGEAVPLEELPEALAEADIVISSTGAPHPVITKEMVER 264
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 107-217 1.04e-05

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 46.72  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 107 TQIRTGAAS--GAAIDvLAKK------DSKIgALIGLGgqgepqleAMIE-------ARNLDEVRVFSRNKESREKFAEE 171
Cdd:PRK00045 156 TGIGAGAVSvaSAAVE-LAKQifgdlsGKKV-LVIGAG--------EMGElvakhlaEKGVRKITVANRTLERAEELAEE 225

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489534381 172 mnlklskYNTKIVAVESSDEAIDNADVIVLATPSKQPVLNGNLVKK 217
Cdd:PRK00045 226 -------FGGEAIPLDELPEALAEADIVISSTGAPHPIIGKGMVER 264
MviM COG0673
Predicted dehydrogenase [General function prediction only];
131-204 2.66e-05

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 45.30  E-value: 2.66e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489534381 131 ALIGLGGQGEPQLEAMIEARNLDEVRVFSRNKESREKFAEEMNLKlskyntkivAVESSDEAIDNA--DVIVLATP 204
Cdd:COG0673    7 GIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVR---------VYTDYEELLADPdiDAVVIATP 73
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 125-221 1.55e-04

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 42.74  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 125 KDSKIGaLIGLGGQGEPQLEAMIEA-RNLDEVRVFSRNKESREKFAEEMNlklskyntkIVAVESSDEAIDNADVIVLAT 203
Cdd:COG0345    1 MSMKIG-FIGAGNMGSAIIKGLLKSgVPPEDIIVSDRSPERLEALAERYG---------VRVTTDNAEAAAQADVVVLAV 70

                         90       100
                 ....*....|....*....|..
gi 489534381 204 PSKQ--PVLN--GNLVKKGALI 221
Cdd:COG0345   71 KPQDlaEVLEelAPLLDPDKLV 92
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 145-206 1.87e-04

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 42.72  E-value: 1.87e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 145 AMIEARNLDEVRVFSRNKEsrekFAEEMN--------LKLSKYNTKIVAVESSDEAIDNADVIVLATPSK 206
Cdd:COG0240   16 AKVLARNGHEVTLWGRDPE----VAEEINetrenpryLPGVKLPENLRATSDLEEALAGADLVLLAVPSQ 81
NAD_Gly3P_dh_N pfam01210
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ...
 145-206 2.42e-04

NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the N-terminal NAD-binding domain.


Pssm-ID: 395967 [Multi-domain]  Cd Length: 158  Bit Score: 41.02  E-value: 2.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381  145 AMIEARNLDEVRVFSRnkesREKFAEEMN--------LKLSKYNTKIVAVESSDEAIDNADVIVLATPSK 206
Cdd:pfam01210  15 AKVLADNGHEVRLWGR----DEELIEEINtthenvryLPGIKLPENLKATTDLAEALKGADIIVIVVPSQ 80
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
131-204 2.63e-04

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 39.52  E-value: 2.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489534381  131 ALIGLGGQGEPQLEAMIEArNLDEVRV-FSRNKESREKFAEEMNLKlskyntkiVAVESSDEAIDNADVIVLATP 204
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAA-GPHEVVVaNSRNPEKAEELAEEYGVG--------ATAVDNEEAAEEADVVFLAVK 66
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 112-225 6.85e-04

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. 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: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 40.07  E-value: 6.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 112 GAASGAAIDVLAK-----KDSKIGALIGLGGQGepQLEAMIEARNLDEVRVFSRNKESREKFAEEMNlklSKYNTKIVAV 186
Cdd:cd01078    9 AAAVAAAGKALELmgkdlKGKTAVVLGGTGPVG--QRAAVLLAREGARVVLVGRDLERAQKAADSLR---ARFGEGVGAV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489534381 187 ESSD-----EAIDNADVIVLATPS--KQPVLNGNLVKKGALISAVG 225
Cdd:cd01078   84 ETSDdaaraAAIKGADVVFAAGAAgvELLEKLAWAPKPLAVAADVN 129
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 155-204 1.24e-03

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 39.80  E-value: 1.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489534381 155 VRVFSRNKESREKFAEEmnlklskynTKIVAVESSDEAIDNADVIVLATP 204
Cdd:COG5495   30 VGVYSRSPASAERAAAL---------LGAVPALDLEELAAEADLVLLAVP 70
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 131-204 2.59e-03

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. 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 DHs, 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: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 38.02  E-value: 2.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489534381 131 ALIGLGGQGEPQLEAMIEArNLDEVRVFSRNKESREKFAEEMNLKLSkyntkIVAVESSDEAIDNADVIVLATP 204
Cdd:cd01065   23 LILGAGGAARAVAYALAEL-GAAKIVIVNRTLEKAKALAERFGELGI-----AIAYLDLEELLAEADLIINTTP 90
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 154-226 3.69e-03

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


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 38.57  E-value: 3.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489534381 154 EVRVFSRNKESREKfAEEMNLklskyntkI-VAVESSDEAIDNADVIVLATPSKQ--PVL--NGNLVKKGALISAVGS 226
Cdd:COG0287   28 EVVGVDRSPETLER-ALELGV--------IdRAATDLEEAVADADLVVLAVPVGAtiEVLaeLAPHLKPGAIVTDVGS 96
PRK07502 PRK07502
prephenate/arogenate dehydrogenase family protein;
131-226 3.93e-03

prephenate/arogenate dehydrogenase family protein;


Pssm-ID: 236034 [Multi-domain]  Cd Length: 307  Bit Score: 38.41  E-value: 3.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489534381 131 ALIGLGGQGEPQLEAMIEARNLDEVRVFSRNKESREKfAEEMNLKLSkyntkivAVESSDEAIDNADVIVLATP--SKQP 208
Cdd:PRK07502  10 ALIGIGLIGSSLARAIRRLGLAGEIVGADRSAETRAR-ARELGLGDR-------VTTSAAEAVKGADLVILCVPvgASGA 81

                         90       100
                 ....*....|....*....|.
gi 489534381 209 V---LNGNLvKKGALISAVGS 226
Cdd:PRK07502  82 VaaeIAPHL-KPGAIVTDVGS 101
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 131-202 7.34e-03

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 37.43  E-value: 7.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489534381 131 ALIGLGGQGEPQLEAMIEA-RNLDEVRVFSRNKESREKFAEEMNlklskyntkIVAVESSDEAIDNADVIVLA 202
Cdd:PRK11880   6 GFIGGGNMASAIIGGLLASgVPAKDIIVSDPSPEKRAALAEEYG---------VRAATDNQEAAQEADVVVLA 69
 
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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