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Conserved domains on  [gi|15217924|ref|NP_176125|]
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Glutamyl-tRNA reductase family protein [Arabidopsis thaliana]

Protein Classification

glutamyl-tRNA reductase( domain architecture ID 11476472)

glutamyl-tRNA reductase catalyzes conversion of glutamyl-tRNA to glutamate-1-semialdehyde

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00203 PLN00203
glutamyl-tRNA reductase
 1-530 0e+00

glutamyl-tRNA reductase


:

Pssm-ID: 215101 [Multi-domain]  Cd Length: 519  Bit Score: 971.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924    1 MAVSSAFVGCPKLETLLNHHNLspsssssssvsqTPLGLNGVRVLPKNNRTRRGLIQKARCELSASSDSASNAASISALE 80
Cdd:PLN00203   1 MAVSAAAALAPAAETSSAPPSS------------SSSSSSATRRGLKSNVTLPSVVGSAAGLATAVDSASSKAASASALE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   81 QLKNSAADRYTKERSSIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCGLNHIEEAAVLSTCNRMEIYVLALSQHRGV 160
Cdd:PLN00203  69 QLKNSAADRYTKEKSSIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCSLNHIEEAAVLSTCNRMEIYVVALSWHRGV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  161 KEVTEWMSKTSGIPVSEICQHRFLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAI 240
Cdd:PLN00203 149 KEVTEWMSKTSGIPVSELRQHLFLLYDKDATQHLFEVSGGLDSLVLGEGQILAQVKQVVKVGQGVDGFGRNLSGLFKHAI 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  241 TVGKRVRTETNIASGAVSVSSAAVELALMKLPQSSNVSARMCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIRE 320
Cdd:PLN00203 229 TAGKRVRTETNIASGAVSVSSAAVELALMKLPESSHASARVLVIGAGKMGKLLVKHLVSKGCTKMVVVNRSEERVAALRE 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  321 EMPGIEIIYRPLDEMLACASEADVVFTSTASETPLFLKEHVENLPQASPEVGGLRHFVDISVPRNVGSCVGEVETARVYN 400
Cdd:PLN00203 309 EFPDVEIIYKPLDEMLACAAEADVVFTSTSSETPLFLKEHVEALPPASDTVGGKRLFVDISVPRNVGACVSELESARVYN 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  401 VDDLKEVVAANKEDRMRKAMEAQTIITEESTQFEAWRDSLETVPTIKKLRAYAERIRVAELEKCMSKMGDDINKKTTRAV 480
Cdd:PLN00203 389 VDDLKEVVAANKEDRLRKAMEAQTIIREESKNFEAWRDSLETVPTIKKLRSYAERIRAAELEKCLSKMGDDLTKKQRKAV 468

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 15217924  481 DDLSRGIVNRFLHGPMQHLRCDGSDSRTLSETLENMHALNRMYGLEKDIL 530
Cdd:PLN00203 469 EDLSRGIVNKLLHGPMQHLRCDGSDSRTVSETLENMHALNRMFDLETEIA 518
 
Name Accession Description Interval E-value
PLN00203 PLN00203
glutamyl-tRNA reductase
 1-530 0e+00

glutamyl-tRNA reductase


Pssm-ID: 215101 [Multi-domain]  Cd Length: 519  Bit Score: 971.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924    1 MAVSSAFVGCPKLETLLNHHNLspsssssssvsqTPLGLNGVRVLPKNNRTRRGLIQKARCELSASSDSASNAASISALE 80
Cdd:PLN00203   1 MAVSAAAALAPAAETSSAPPSS------------SSSSSSATRRGLKSNVTLPSVVGSAAGLATAVDSASSKAASASALE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   81 QLKNSAADRYTKERSSIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCGLNHIEEAAVLSTCNRMEIYVLALSQHRGV 160
Cdd:PLN00203  69 QLKNSAADRYTKEKSSIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCSLNHIEEAAVLSTCNRMEIYVVALSWHRGV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  161 KEVTEWMSKTSGIPVSEICQHRFLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAI 240
Cdd:PLN00203 149 KEVTEWMSKTSGIPVSELRQHLFLLYDKDATQHLFEVSGGLDSLVLGEGQILAQVKQVVKVGQGVDGFGRNLSGLFKHAI 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  241 TVGKRVRTETNIASGAVSVSSAAVELALMKLPQSSNVSARMCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIRE 320
Cdd:PLN00203 229 TAGKRVRTETNIASGAVSVSSAAVELALMKLPESSHASARVLVIGAGKMGKLLVKHLVSKGCTKMVVVNRSEERVAALRE 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  321 EMPGIEIIYRPLDEMLACASEADVVFTSTASETPLFLKEHVENLPQASPEVGGLRHFVDISVPRNVGSCVGEVETARVYN 400
Cdd:PLN00203 309 EFPDVEIIYKPLDEMLACAAEADVVFTSTSSETPLFLKEHVEALPPASDTVGGKRLFVDISVPRNVGACVSELESARVYN 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  401 VDDLKEVVAANKEDRMRKAMEAQTIITEESTQFEAWRDSLETVPTIKKLRAYAERIRVAELEKCMSKMGDDINKKTTRAV 480
Cdd:PLN00203 389 VDDLKEVVAANKEDRLRKAMEAQTIIREESKNFEAWRDSLETVPTIKKLRSYAERIRAAELEKCLSKMGDDLTKKQRKAV 468

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 15217924  481 DDLSRGIVNRFLHGPMQHLRCDGSDSRTLSETLENMHALNRMYGLEKDIL 530
Cdd:PLN00203 469 EDLSRGIVNKLLHGPMQHLRCDGSDSRTVSETLENMHALNRMFDLETEIA 518
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 96-528 1.43e-154

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: 448.41  E-value: 1.43e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  96 SIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCGLNHIEEAAVLSTCNRMEIYVLALSQHRGVKEVTEWMSKTSGIPV 175
Cdd:COG0373   2 SLLVVGLNHKTAPVEIREKLAFSEEELEEALEELKAQPGVDEAVILSTCNRTEIYAVADDPHAGLEALIEFLAEYHGLDV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 176 SEICQHRFLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAITVGKRVRTETNIASG 255
Cdd:COG0373  82 EELEPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYELAREAGTTGPVLNRLFQKAFSVAKRVRTETGIGEG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 256 AVSVSSAAVELALMKLPQSSNVSArmCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEMPGieiIYRPLDEM 335
Cdd:COG0373 162 AVSVSSAAVELAKKIFGDLSGKTV--LVIGAGEMGELAARHLAAKGVKRITVANRTLERAEELAEEFGG---EAVPLEEL 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 336 LACASEADVVFTSTASETPLFLKEHVENLPQASPevGGLRHFVDISVPRNVGSCVGEVETARVYNVDDLKEVVAANKEDR 415
Cdd:COG0373 237 PEALAEADIVISSTGAPHPVITKEMVERALKKRR--HRPLFLIDLAVPRDIEPEVGELPGVYLYDIDDLQEVVDENLEER 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 416 MRKAMEAQTIITEESTQFEAWRDSLETVPTIKKLRAYAERIRVAELEKCMSKMGdDINKKTTRAVDDLSRGIVNRFLHGP 495
Cdd:COG0373 315 QAAAPKAEAIIEEEVEEFLEWLKSREVVPTIRALREKAEAIREEELERALKKLP-DLGEDEREVLEKLTRSLVNKLLHAP 393

                       410       420       430
                ....*....|....*....|....*....|....*.
gi 15217924 496 MQHLR---CDGSDSRTLsetlenmHALNRMYGLEKD 528
Cdd:COG0373 394 TVRLKeaaAEGEDDEYL-------EALRRLFDLEEE 422
hemA TIGR01035
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ...
 97-500 4.91e-110

glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase (TIGR00713), leads to the production of delta-amino-levulinic acid from Glu-tRNA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273407 [Multi-domain]  Cd Length: 417  Bit Score: 334.36  E-value: 4.91e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924    97 IVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCGLNHIEEAAVLSTCNRMEIYVLALSQHRGVKEVTEWMSKTSGIPVS 176
Cdd:TIGR01035   1 ILVLGVSHKSAPVEVREKLSIDEIKLKKALDTLKAEPSIEEAMVLSTCNRVEIYAVVDNLHEGKSALLQILAENKNMSNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   177 EICQHRFLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAITVGKRVRTETNIASGA 256
Cdd:TIGR01035  81 DLEKYLYILTGESAVEHLFRVASGLDSMVVGETQILGQVKNAYKVAQEEKTVGKVLERLFQKAFSVGKRVRTETDISAGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   257 VSVSSAAVELALMKLPQSSNVSArmCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEMPGIEIIYRPLDEML 336
Cdd:TIGR01035 161 VSISSAAVELAERIFGSLKGKKA--LLIGAGEMGELVAKHLLRKGVGKILIANRTYERAEDLAKELGGEAVKFEDLEEYL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   337 AcasEADVVFTSTASETPLFLKEHVENlpqASPEVGGLRHFVDISVPRNVGSCVGEVETARVYNVDDLKEVVAANKEDRM 416
Cdd:TIGR01035 239 A---EADIVISSTGAPHPIVSKEDVER---ALRERTRPLFIIDIAVPRDVDPAVARLEGVFLYDVDDLQPVVEENLAERR 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   417 RKAMEAQTIITEESTQFEAWRDSLETVPTIKKLRAYAERIRVAELEKCMSKMGdDINKKTTRAVDDLSRGIVNRFLHGPM 496
Cdd:TIGR01035 313 EEAEKAEEIVEEETAEFKQWLRSLEVEPTIKALRSLAEIVREKELEKALKKLP-GLSKDVEEVLEDLARKLINKLLHAPT 391


                  ....
gi 15217924   497 QHLR 500
Cdd:TIGR01035 392 VRLK 395
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 97-419 3.30e-101

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 307.66  E-value: 3.30e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  97 IVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCGLNHIEEAAVLSTCNRMEIYVLALSQHRGVKEVTEWMSKTSGIPvs 176
Cdd:cd05213   1 ILVIGLSHKTAPVELREKLAFSEEELKEALRRLLEKPGISEAVLLSTCNRVELYLVGDNFHKLADELEELLAELLNEP-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 177 EICQHRFLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAITVGKRVRTETNIASGA 256
Cdd:cd05213  79 ELREYLYVGRGQDAVRHLFRVASGLDSMVVGETQILGQVKNAYKLAKEAGTSGKLLNRLFQKAIKVGKRVRTETGISRGA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 257 VSVSSAAVELALMKLPQSSNvsARMCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEMPGieiIYRPLDEML 336
Cdd:cd05213 159 VSISSAAVELAEKIFGNLKG--KKVLVIGAGEMGELAAKHLAAKGVAEITIANRTYERAEELAKELGG---NAVPLDELL 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 337 ACASEADVVFTSTASETPLFLKEHVENLPQASPEVgglrhFVDISVPRNVGSCVGEVETARVYNVDDLKEVVAANKEDRM 416
Cdd:cd05213 234 ELLNEADVVISATGAPHYAKIVERAMKKRSGKPRL-----IVDLAVPRDIEPEVGELEGVRLYTIDDLEEVVEENLERRE 308


                ...
gi 15217924 417 RKA 419
Cdd:cd05213 309 KEA 311
GlutR_N pfam05201
Glutamyl-tRNAGlu reductase, N-terminal domain;
103-250 1.41e-58

Glutamyl-tRNAGlu reductase, N-terminal domain;


Pssm-ID: 461585  Cd Length: 144  Bit Score: 191.18  E-value: 1.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   103 SIHTAPVEMREKLAIPEAEWPRAIAELCGlnhIEEAAVLSTCNRMEIYVLALSQHRGVKEVTEWMSKTSGiPVSEICQHR 182
Cdd:pfam05201   1 NHKTAPVEIREKLAFSEEELEEALQELRG---IDEAVILSTCNRTEIYAVADDFHAALEAVIEFLAEHSG-DLEELRPYL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15217924   183 FLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAITVGKRVRTET 250
Cdd:pfam05201  77 YVYEGEEAVRHLFRVASGLDSMVLGEDQILGQVKDAYELAREAGTTGPVLNRLFQKAITVAKRVRTET 144
 
Name Accession Description Interval E-value
PLN00203 PLN00203
glutamyl-tRNA reductase
 1-530 0e+00

glutamyl-tRNA reductase


Pssm-ID: 215101 [Multi-domain]  Cd Length: 519  Bit Score: 971.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924    1 MAVSSAFVGCPKLETLLNHHNLspsssssssvsqTPLGLNGVRVLPKNNRTRRGLIQKARCELSASSDSASNAASISALE 80
Cdd:PLN00203   1 MAVSAAAALAPAAETSSAPPSS------------SSSSSSATRRGLKSNVTLPSVVGSAAGLATAVDSASSKAASASALE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   81 QLKNSAADRYTKERSSIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCGLNHIEEAAVLSTCNRMEIYVLALSQHRGV 160
Cdd:PLN00203  69 QLKNSAADRYTKEKSSIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCSLNHIEEAAVLSTCNRMEIYVVALSWHRGV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  161 KEVTEWMSKTSGIPVSEICQHRFLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAI 240
Cdd:PLN00203 149 KEVTEWMSKTSGIPVSELRQHLFLLYDKDATQHLFEVSGGLDSLVLGEGQILAQVKQVVKVGQGVDGFGRNLSGLFKHAI 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  241 TVGKRVRTETNIASGAVSVSSAAVELALMKLPQSSNVSARMCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIRE 320
Cdd:PLN00203 229 TAGKRVRTETNIASGAVSVSSAAVELALMKLPESSHASARVLVIGAGKMGKLLVKHLVSKGCTKMVVVNRSEERVAALRE 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  321 EMPGIEIIYRPLDEMLACASEADVVFTSTASETPLFLKEHVENLPQASPEVGGLRHFVDISVPRNVGSCVGEVETARVYN 400
Cdd:PLN00203 309 EFPDVEIIYKPLDEMLACAAEADVVFTSTSSETPLFLKEHVEALPPASDTVGGKRLFVDISVPRNVGACVSELESARVYN 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  401 VDDLKEVVAANKEDRMRKAMEAQTIITEESTQFEAWRDSLETVPTIKKLRAYAERIRVAELEKCMSKMGDDINKKTTRAV 480
Cdd:PLN00203 389 VDDLKEVVAANKEDRLRKAMEAQTIIREESKNFEAWRDSLETVPTIKKLRSYAERIRAAELEKCLSKMGDDLTKKQRKAV 468

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 15217924  481 DDLSRGIVNRFLHGPMQHLRCDGSDSRTLSETLENMHALNRMYGLEKDIL 530
Cdd:PLN00203 469 EDLSRGIVNKLLHGPMQHLRCDGSDSRTVSETLENMHALNRMFDLETEIA 518
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 96-528 1.43e-154

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: 448.41  E-value: 1.43e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  96 SIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCGLNHIEEAAVLSTCNRMEIYVLALSQHRGVKEVTEWMSKTSGIPV 175
Cdd:COG0373   2 SLLVVGLNHKTAPVEIREKLAFSEEELEEALEELKAQPGVDEAVILSTCNRTEIYAVADDPHAGLEALIEFLAEYHGLDV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 176 SEICQHRFLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAITVGKRVRTETNIASG 255
Cdd:COG0373  82 EELEPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYELAREAGTTGPVLNRLFQKAFSVAKRVRTETGIGEG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 256 AVSVSSAAVELALMKLPQSSNVSArmCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEMPGieiIYRPLDEM 335
Cdd:COG0373 162 AVSVSSAAVELAKKIFGDLSGKTV--LVIGAGEMGELAARHLAAKGVKRITVANRTLERAEELAEEFGG---EAVPLEEL 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 336 LACASEADVVFTSTASETPLFLKEHVENLPQASPevGGLRHFVDISVPRNVGSCVGEVETARVYNVDDLKEVVAANKEDR 415
Cdd:COG0373 237 PEALAEADIVISSTGAPHPVITKEMVERALKKRR--HRPLFLIDLAVPRDIEPEVGELPGVYLYDIDDLQEVVDENLEER 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 416 MRKAMEAQTIITEESTQFEAWRDSLETVPTIKKLRAYAERIRVAELEKCMSKMGdDINKKTTRAVDDLSRGIVNRFLHGP 495
Cdd:COG0373 315 QAAAPKAEAIIEEEVEEFLEWLKSREVVPTIRALREKAEAIREEELERALKKLP-DLGEDEREVLEKLTRSLVNKLLHAP 393

                       410       420       430
                ....*....|....*....|....*....|....*.
gi 15217924 496 MQHLR---CDGSDSRTLsetlenmHALNRMYGLEKD 528
Cdd:COG0373 394 TVRLKeaaAEGEDDEYL-------EALRRLFDLEEE 422
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 96-528 2.68e-152

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 442.32  E-value: 2.68e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   96 SIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCGLNHIEEAAVLSTCNRMEIYVLALSQHRGVKEVTEWMSKTSGIPV 175
Cdd:PRK00045   2 SLLAVGLNHKTAPVELREKLAFSEDELEEALESLLASPSVLEAVILSTCNRTEIYAVVDQFHAGREAIIRWLAEYHGLDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  176 SEICQHRFLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAITVGKRVRTETNIASG 255
Cdd:PRK00045  82 EELRPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYALAQEAGTVGTILNRLFQKAFSVAKRVRTETGIGAG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  256 AVSVSSAAVELALMKLPQSSNVSArmCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEMPGieiIYRPLDEM 335
Cdd:PRK00045 162 AVSVASAAVELAKQIFGDLSGKKV--LVIGAGEMGELVAKHLAEKGVRKITVANRTLERAEELAEEFGG---EAIPLDEL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  336 LACASEADVVFTSTASETPLFLKEHVENLPQAspEVGGLRHFVDISVPRNVGSCVGEVETARVYNVDDLKEVVAANKEDR 415
Cdd:PRK00045 237 PEALAEADIVISSTGAPHPIIGKGMVERALKA--RRHRPLLLVDLAVPRDIEPEVGELPGVYLYDVDDLQEIVEENLAQR 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  416 MRKAMEAQTIITEESTQFEAWRDSLETVPTIKKLRAYAERIRVAELEKCMSKMGDDinKKTTRAVDDLSRGIVNRFLHGP 495
Cdd:PRK00045 315 QEAAEKAEAIVEEEVAEFMEWLRSLEVVPTIRALREQAEEIREEELERALKKLGPG--EDEEEVLEKLARSLVNKLLHAP 392

                        410       420       430
                 ....*....|....*....|....*....|...
gi 15217924  496 MQHLRCDGSDSRtlSETLEnmhALNRMYGLEKD 528
Cdd:PRK00045 393 TVRLKEAAEEGD--DEYLE---ALRELFGLDPE 420
hemA TIGR01035
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ...
 97-500 4.91e-110

glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase (TIGR00713), leads to the production of delta-amino-levulinic acid from Glu-tRNA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273407 [Multi-domain]  Cd Length: 417  Bit Score: 334.36  E-value: 4.91e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924    97 IVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCGLNHIEEAAVLSTCNRMEIYVLALSQHRGVKEVTEWMSKTSGIPVS 176
Cdd:TIGR01035   1 ILVLGVSHKSAPVEVREKLSIDEIKLKKALDTLKAEPSIEEAMVLSTCNRVEIYAVVDNLHEGKSALLQILAENKNMSNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   177 EICQHRFLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAITVGKRVRTETNIASGA 256
Cdd:TIGR01035  81 DLEKYLYILTGESAVEHLFRVASGLDSMVVGETQILGQVKNAYKVAQEEKTVGKVLERLFQKAFSVGKRVRTETDISAGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   257 VSVSSAAVELALMKLPQSSNVSArmCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEMPGIEIIYRPLDEML 336
Cdd:TIGR01035 161 VSISSAAVELAERIFGSLKGKKA--LLIGAGEMGELVAKHLLRKGVGKILIANRTYERAEDLAKELGGEAVKFEDLEEYL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   337 AcasEADVVFTSTASETPLFLKEHVENlpqASPEVGGLRHFVDISVPRNVGSCVGEVETARVYNVDDLKEVVAANKEDRM 416
Cdd:TIGR01035 239 A---EADIVISSTGAPHPIVSKEDVER---ALRERTRPLFIIDIAVPRDVDPAVARLEGVFLYDVDDLQPVVEENLAERR 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   417 RKAMEAQTIITEESTQFEAWRDSLETVPTIKKLRAYAERIRVAELEKCMSKMGdDINKKTTRAVDDLSRGIVNRFLHGPM 496
Cdd:TIGR01035 313 EEAEKAEEIVEEETAEFKQWLRSLEVEPTIKALRSLAEIVREKELEKALKKLP-GLSKDVEEVLEDLARKLINKLLHAPT 391


                  ....
gi 15217924   497 QHLR 500
Cdd:TIGR01035 392 VRLK 395
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 97-419 3.30e-101

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 307.66  E-value: 3.30e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  97 IVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCGLNHIEEAAVLSTCNRMEIYVLALSQHRGVKEVTEWMSKTSGIPvs 176
Cdd:cd05213   1 ILVIGLSHKTAPVELREKLAFSEEELKEALRRLLEKPGISEAVLLSTCNRVELYLVGDNFHKLADELEELLAELLNEP-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 177 EICQHRFLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAITVGKRVRTETNIASGA 256
Cdd:cd05213  79 ELREYLYVGRGQDAVRHLFRVASGLDSMVVGETQILGQVKNAYKLAKEAGTSGKLLNRLFQKAIKVGKRVRTETGISRGA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 257 VSVSSAAVELALMKLPQSSNvsARMCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEMPGieiIYRPLDEML 336
Cdd:cd05213 159 VSISSAAVELAEKIFGNLKG--KKVLVIGAGEMGELAAKHLAAKGVAEITIANRTYERAEELAKELGG---NAVPLDELL 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 337 ACASEADVVFTSTASETPLFLKEHVENLPQASPEVgglrhFVDISVPRNVGSCVGEVETARVYNVDDLKEVVAANKEDRM 416
Cdd:cd05213 234 ELLNEADVVISATGAPHYAKIVERAMKKRSGKPRL-----IVDLAVPRDIEPEVGELEGVRLYTIDDLEEVVEENLERRE 308


                ...
gi 15217924 417 RKA 419
Cdd:cd05213 309 KEA 311
GlutR_N pfam05201
Glutamyl-tRNAGlu reductase, N-terminal domain;
103-250 1.41e-58

Glutamyl-tRNAGlu reductase, N-terminal domain;


Pssm-ID: 461585  Cd Length: 144  Bit Score: 191.18  E-value: 1.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   103 SIHTAPVEMREKLAIPEAEWPRAIAELCGlnhIEEAAVLSTCNRMEIYVLALSQHRGVKEVTEWMSKTSGiPVSEICQHR 182
Cdd:pfam05201   1 NHKTAPVEIREKLAFSEEELEEALQELRG---IDEAVILSTCNRTEIYAVADDFHAALEAVIEFLAEHSG-DLEELRPYL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15217924   183 FLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAITVGKRVRTET 250
Cdd:pfam05201  77 YVYEGEEAVRHLFRVASGLDSMVLGEDQILGQVKDAYELAREAGTTGPVLNRLFQKAITVAKRVRTET 144
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 265-407 3.89e-51

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: 171.22  E-value: 3.89e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   265 ELALMKLPQSSnvSARMCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEMPGIEiiYRPLDEMLACASEADV 344
Cdd:pfam01488   1 ELAKKIFGDLK--DKKVLLIGAGEMGELVAKHLLAKGAKEVTIANRTIERAQELAEKFGGVE--ALPLDDLKEYLAEADI 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15217924   345 VFTSTASETPLFLKEHVEnlpQASPEVGGLRHFVDISVPRNVGSCVGEVETARVYNVDDLKEV 407
Cdd:pfam01488  77 VISATSSPTPIITKEMVE---RALKPRKKPLLFVDIAVPRDIEPEVGELEGVYLYTVDDLKEV 136
PRK13940 PRK13940
glutamyl-tRNA reductase; Provisional
 96-525 3.89e-37

glutamyl-tRNA reductase; Provisional


Pssm-ID: 172450 [Multi-domain]  Cd Length: 414  Bit Score: 142.08  E-value: 3.89e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   96 SIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCGLNHIEEAAVLSTCNRMEIYvLALSQHRGVKEVTEWMSKTSGIPV 175
Cdd:PRK13940   2 ALISLAIDYKKSPIEVRSEFALSGLDVSMLYRSILAIDNVVHAVILSTCNRTEVY-LEISDLRVVDDILVWWQGYVRNPN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  176 SEICQHRFLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAITVGKRVRTETNIASG 255
Cdd:PRK13940  81 YKIKDYFKLRQGTEVIMHLMKLACGLESMVLGEPQILGQVKDSYTLSKKNHAIGKELDRVFQKVFATAKRVRSETRIGHC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  256 AVSVSSAAVELALMKLPQSSnvSARMCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEMPGIEIIYrpLDEM 335
Cdd:PRK13940 161 PVSVAFSAITLAKRQLDNIS--SKNVLIIGAGQTGELLFRHVTALAPKQIMLANRTIEKAQKITSAFRNASAHY--LSEL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  336 LACASEADVVFTSTASETPLFLKEHVENLPqaspevgglRHFVDISVPRNVGSCVGEVETARVYNVDDLKEVVAANKEDR 415
Cdd:PRK13940 237 PQLIKKADIIIAAVNVLEYIVTCKYVGDKP---------RVFIDISIPQALDPKLGELEQNVYYCVDDINAVIEDNKDKR 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  416 MRKAMEAQTIITEESTQFEAWRDSLETVPTIKKLRAYAERIRVAELEKCMSKMGDdiNKKTTRAVDDLSRGIVNRFLHGP 495
Cdd:PRK13940 308 KYESSKAQKIIVKSLEEYLEKEKAIISNSAIKELFQKADGLVDLSLEKSLAKIRN--GKDAEEIIKRFAYEIKKKVLHYP 385

                        410       420       430
                 ....*....|....*....|....*....|
gi 15217924  496 MQHLRCDGSDSRTlsetlENMHALNRMYGL 525
Cdd:PRK13940 386 VVGMKEASKQGRS-----DCLVCMKRMFGL 410
GlutR_dimer pfam00745
Glutamyl-tRNAGlu reductase, dimerization domain;
421-522 1.93e-24

Glutamyl-tRNAGlu reductase, dimerization domain;


Pssm-ID: 459922 [Multi-domain]  Cd Length: 95  Bit Score: 97.26  E-value: 1.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   421 EAQTIITEESTQFEAWRDSLETVPTIKKLRAYAERIRVAELEKCMSKMGddINKKTTRAVDDLSRGIVNRFLHGPMQHLR 500
Cdd:pfam00745   1 KAEAIIEEEVEEFMAWLKSLEVVPTIRALREKAEEIREEELERALKKLG--LDGEDREELEKLTRSLVNKLLHDPTVRLK 78

                          90       100
                  ....*....|....*....|..
gi 15217924   501 CDGSDsrtlsETLENMHALNRM 522
Cdd:pfam00745  79 EAEEG-----DGDEYLEALRRL 95
hemA PRK00676
glutamyl-tRNA reductase; Validated
 141-384 2.81e-13

glutamyl-tRNA reductase; Validated


Pssm-ID: 234810 [Multi-domain]  Cd Length: 338  Bit Score: 71.04  E-value: 2.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  141 LSTCNRMEIYVLALSQHRGVKEVTEWMSKTSGIPvseicqhrFLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVK 220
Cdd:PRK00676  48 LLTCHRAELYYYSVSPAELQSSLLSEITSLGVRP--------YFYRGLDCFTHLFCVTSGMDSLILGETEIQGQVKRAYL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  221 VGQGVNGFGRNISGLFKHAITVGKRVRTETNIASGAVSVSSaAVELALMKlpQSSNVSARMCVIGAGKMGKLVIKHLMAK 300
Cdd:PRK00676 120 KAARERKLPFALHFLFQKALKEGKVFRSKGGAPYAEVTIES-VVQQELRR--RQKSKKASLLFIGYSEINRKVAYYLQRQ 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  301 GCTKVVVVNRSEervsaireempgIEIIYRPL-DEMLACASEADVVF---TSTASETPLFLKEHVENLPQaspevgglRH 376
Cdd:PRK00676 197 GYSRITFCSRQQ------------LTLPYRTVvREELSFQDPYDVIFfgsSESAYAFPHLSWESLADIPD--------RI 256


                 ....*...
gi 15217924  377 FVDISVPR 384
Cdd:PRK00676 257 VFDFNVPR 264
OCDMu COG2423
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid ...
 278-361 9.56e-10

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: 60.16  E-value: 9.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 278 SARMCVIGAGKMGKLVIKHLMA-KGCTKVVVVNRSEERVSAIREEMPGIEIIYRPLDEMLACASEADVVFTSTASETPLF 356
Cdd:COG2423 127 ARTLGIIGAGVQARTQLRALAAvRPIERVRVWGRDPEKAEAFAARLAAEGLPVEAADDLEEAVADADIIVTATPSREPVL 206


                ....*
gi 15217924 357 LKEHV 361
Cdd:COG2423 207 RGEWL 211
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 280-362 8.03e-08

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: 51.89  E-value: 8.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 280 RMCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEMPGIEIIYRPLDeMLACASEADVVfTSTaseTPLFLKE 359
Cdd:cd01065  21 KVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELGIAIAYLD-LEELLAEADLI-INT---TPVGMKP 95


                ...
gi 15217924 360 HVE 362
Cdd:cd01065  96 GDE 98
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
282-383 7.29e-07

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 47.23  E-value: 7.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924   282 CVIGAGKMGKLVIKHLMAKGCTKVVVVN-RSEERVSAIREEMpGIEIIYRPLDEmlaCASEADVVFTSTAsetPLFLKEH 360
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGPHEVVVANsRNPEKAEELAEEY-GVGATAVDNEE---AAEEADVVFLAVK---PEDAPDV 73

                          90       100
                  ....*....|....*....|...
gi 15217924   361 VENLPQASPEVGglrhFVDISVP 383
Cdd:pfam03807  74 LSELSDLLKGKI----VISIAAG 92
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
 279-345 1.13e-06

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: 50.14  E-value: 1.13e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15217924 279 ARMCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEmpgIEIIYRPLDEMLACASEADVV 345
Cdd:COG0169 122 KRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPERAEALAAR---LGVRAVPLDDLAAALAGADLV 185
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 280-346 8.58e-06

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: 47.37  E-value: 8.58e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15217924 280 RMCVIGAGKMGKLVIKHLMAKGCTK--VVVVNRSEERVSAIREEmPGIEIIyrplDEMLACASEADVVF 346
Cdd:COG0345   4 KIGFIGAGNMGSAIIKGLLKSGVPPedIIVSDRSPERLEALAER-YGVRVT----TDNAEAAAQADVVV 67
PRK08618 PRK08618
ornithine cyclodeaminase family protein;
282-356 1.97e-05

ornithine cyclodeaminase family protein;


Pssm-ID: 236313 [Multi-domain]  Cd Length: 325  Bit Score: 46.59  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  282 CVIGAGKMGKLVIKHLMA-KGCTKVVVVNRSEERVSAIREEMP---GIEII-YRPLDEmlaCASEADVVFTSTASETPLF 356
Cdd:PRK08618 131 CLIGTGGQAKGQLEAVLAvRDIERVRVYSRTFEKAYAFAQEIQskfNTEIYvVNSADE---AIEEADIIVTVTNAKTPVF 207
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 257-353 2.99e-05

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 46.45  E-value: 2.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 257 VSVSSAAVELALMKLPQSSnvsarmCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEmpGIEIIYRPLDEML 336
Cdd:cd08236 145 AAVALHAVRLAGITLGDTV------VVIGAGTIGLLAIQWLKILGAKRVIAVDIDDEKLAVAREL--GADDTINPKEEDV 216

                        90       100
                ....*....|....*....|....
gi 15217924 337 ACASE------ADVVF-TSTASET 353
Cdd:cd08236 217 EKVREltegrgADLVIeAAGSPAT 240
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 283-348 6.18e-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: 43.61  E-value: 6.18e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15217924   283 VIGAGKMGKLVIKHLMAKGCTkVVVVNRSEERVSAIREEmpGIEIIYRPLDemlaCASEADVVFTS 348
Cdd:pfam03446   4 FIGLGVMGSPMALNLLKAGYT-VTVYNRTPEKVEELVAA--GAIAAASPAE----FVAGLDVVITM 62
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 190-355 1.78e-04

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 43.41  E-value: 1.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 190 ATQHIFEVSAGLDS-LVLGegqiLAQVKQVVKVGQGVNGF--GRNISGLFKHAItvgkRVRTETNIA---SGAVSVSSAA 263
Cdd:cd08255   7 ALEGLSTGTEKLPLpLPPG----YSSVGRVVEVGSGVTGFkpGDRVFCFGPHAE----RVVVPANLLvplPDGLPPERAA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 264 ----VELALMKLPQSS-NVSARMCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEMPGIEIIyrPLDEMLAC 338
Cdd:cd08255  79 ltalAATALNGVRDAEpRLGERVAVVGLGLVGLLAAQLAKAAGAREVVGVDPDAARRELAEALGPADPVA--ADTADEIG 156

                       170
                ....*....|....*..
gi 15217924 339 ASEADVVFTSTASETPL 355
Cdd:cd08255 157 GRGADVVIEASGSPSAL 173
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 253-391 2.20e-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: 42.38  E-value: 2.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 253 ASGAVSVSSAAVELAL--MKLPQSSNVSARMCVIGA-GKMGKlVIKHLMAKGCTKVVVVNRSEERVSAIREEM---PGI- 325
Cdd:cd01078   1 SNGSNTTAAAAVAAAGkaLELMGKDLKGKTAVVLGGtGPVGQ-RAAVLLAREGARVVLVGRDLERAQKAADSLrarFGEg 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15217924 326 --EIIYRPLDEMLACASEADVVFTSTAS--ETPLFLKEHVENL---------PQASPEVGGLRhfvDISVPRNVGSCVG 391
Cdd:cd01078  80 vgAVETSDDAARAAAIKGADVVFAAGAAgvELLEKLAWAPKPLavaadvnavPPVGIEGIDVP---DKGVDREGKVPYG 155
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 278-348 4.76e-04

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 42.41  E-value: 4.76e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15217924 278 SARMCVIGAGKMGKLVIKHLMAKGCTkVVVVNRSEERVSAIREEmpGIeiiyRPLDEMLACASEADVVFTS 348
Cdd:COG2084   1 MMKVGFIGLGAMGAPMARNLLKAGHE-VTVWNRTPAKAEALVAA--GA----RVAASPAEAAAAADVVITM 64
NmrA_like_SDR_a cd05251
NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) ...
 283-427 6.44e-04

NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) SDRs; NmrA and HSCARG like proteins. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187561 [Multi-domain]  Cd Length: 242  Bit Score: 41.49  E-value: 6.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 283 VIGA-GKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEMPGIEIIYRPLDE---MLACASEADVVFTSTASETPLFLK 358
Cdd:cd05251   3 VFGAtGKQGGSVVRALLKDPGFKVRALTRDPSSPAAKALAAPGVEVVQGDLDDpesLEAALKGVYGVFLVTDFWEAGGED 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15217924 359 E--HVENLPQASPEVgGLRHFVDISVPRnvgscvGEVETARVYNVDDLKEVvaankEDRMRKAMEAQTIIT 427
Cdd:cd05251  83 EiaQGKNVVDAAKRA-GVQHFVFSSVPD------VEKLTLAVPHFDSKAEV-----EEYIRASGLPATILR 141
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 256-351 6.89e-04

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


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 41.98  E-value: 6.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 256 AVSVSSAAVELALMKLPQSSNVSARMCVIGAGKMGKLVIKHLMAKGcTKVVVVNRSEERVSAIREEmpGIEIIY-RPLDE 334
Cdd:COG0569  73 VLFGGLLEALRRRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEG-HDVVVIDKDPERVERLAEE--DVLVIVgDATDE 149

                        90       100
                ....*....|....*....|
gi 15217924 335 ML---ACASEADVVFTSTAS 351
Cdd:COG0569 150 EVleeAGIEDADAVIAATGD 169
MviM COG0673
Predicted dehydrogenase [General function prediction only];
280-349 8.74e-04

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 41.45  E-value: 8.74e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15217924 280 RMCVIGAGKMGKLVIKHLMA-KGCTKVVVVNRSEERVSAIREEMpGIEiIYRPLDEMLAcASEADVVFTST 349
Cdd:COG0673   5 RVGIIGAGGIGRAHAPALAAlPGVELVAVADRDPERAEAFAEEY-GVR-VYTDYEELLA-DPDIDAVVIAT 72
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 279-355 8.77e-04

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family, including threonine dehydrogenase. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176204 [Multi-domain]  Cd Length: 319  Bit Score: 41.46  E-value: 8.77e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15217924 279 ARMCVIGAGKMGKLVIKHLMAKGCtKVVVVNRSEERVSAIREEmpGIEIIYrpLDEMLACASEADVVFTSTASETPL 355
Cdd:cd08242 157 DKVAVLGDGKLGLLIAQVLALTGP-DVVLVGRHSEKLALARRL--GVETVL--PDEAESEGGGFDVVVEATGSPSGL 228
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 283-346 1.08e-03

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 40.90  E-value: 1.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15217924  283 VIGAGKMGKLVIKHLMAKGC--TKVVVVNRSEERVSAIREEMpGIEIIYRPLDEmlacASEADVVF 346
Cdd:PRK11880   7 FIGGGNMASAIIGGLLASGVpaKDIIVSDPSPEKRAALAEEY-GVRAATDNQEA----AQEADVVV 67
PRK08291 PRK08291
cyclodeaminase;
246-362 1.54e-03

cyclodeaminase;


Pssm-ID: 236221 [Multi-domain]  Cd Length: 330  Bit Score: 40.72  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924  246 VRTEtniASGAVsvssAAVELAlmklpqsSNVSARMCVIGAGKMGKLVIKHLM-AKGCTKVVVVNRSEERVSAIREEMP- 323
Cdd:PRK08291 114 VRTA---AAGAV----AARHLA-------REDASRAAVIGAGEQARLQLEALTlVRPIREVRVWARDAAKAEAYAADLRa 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15217924  324 --GIEIIYrpLDEMLACASEADVVFTSTASETPLFLKEHVE 362
Cdd:PRK08291 180 elGIPVTV--ARDVHEAVAGADIIVTTTPSEEPILKAEWLH 218
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
 280-362 1.67e-03

N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.


Pssm-ID: 467611 [Multi-domain]  Cd Length: 139  Bit Score: 39.08  E-value: 1.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 280 RMCVIGA-GKMGKLVIKHLM-AKGCTKVVVVNRSE-ERVSAIREEMPGIEIIYRPLDEMLACASEADVV--FTstaseTP 354
Cdd:cd02274   2 KVAVAGAtGRMGRELVKAILeAPDLELVGAVDRPGsGLLGGDAGGLAGIGTGVIVSLDLELAAADADVVidFT-----TP 76


                ....*...
gi 15217924 355 LFLKEHVE 362
Cdd:cd02274  77 EATLENLE 84
NmrA_TMR_like_SDR_a cd08947
NmrA (a transcriptional regulator), HSCARG (an NADPH sensor), and triphenylmethane reductase ...
 283-372 1.84e-03

NmrA (a transcriptional regulator), HSCARG (an NADPH sensor), and triphenylmethane reductase (TMR) like proteins, atypical (a) SDRs; Atypical SDRs belonging to this subgroup include NmrA, HSCARG, and TMR, these proteins bind NAD(P) but they lack the usual catalytic residues of the SDRs. Atypical SDRs are distinct from classical SDRs. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. TMR, an NADP-binding protein, lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187651 [Multi-domain]  Cd Length: 224  Bit Score: 39.84  E-value: 1.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217924 283 VIGA-GKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIReeMPGIEIIYRP------LDEMLACASEADVVFTSTASEtPL 355
Cdd:cd08947   3 VTGAtGQQGGSVIRHLLAKGASQVRAVVRNVEKAATLA--DQGVEVRQGDynqpelLQKAFAGASKLFIITGPHYDN-TL 79

                        90
                ....*....|....*..
gi 15217924 356 FLKEHvENLPQASPEVG 372
Cdd:cd08947  80 EIKQG-KNVADAARRAG 95
aroE PRK00258
shikimate 5-dehydrogenase; Reviewed
 280-351 1.90e-03

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 234703 [Multi-domain]  Cd Length: 278  Bit Score: 40.17  E-value: 1.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15217924  280 RMCVIGAGKMGKLVIKHLMAKGCTKVVVVNRSEERVSAIREEMPGIEIIYRPLDEmLACASEADVVFTSTAS 351
Cdd:PRK00258 125 RILILGAGGAARAVILPLLDLGVAEITIVNRTVERAEELAKLFGALGKAELDLEL-QEELADFDLIINATSA 195
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 279-354 2.94e-03

UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 397677 [Multi-domain]  Cd Length: 186  Bit Score: 39.15  E-value: 2.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15217924   279 ARMCVIGAGKMGkLVIKHLMAKGCTKVVVVNRSEERVSAIREempGIEIIYRP-LDEMLACASEADVVFTSTASETP 354
Cdd:pfam03721   1 MKISVIGLGYVG-LPTAACLAEIGHDVIGVDIDEEKVDKLNS---GQIPIYEPgLDELVKANVSGRLSFTTDYSTAI 73
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 283-345 3.17e-03

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, aka Hydroxypyruvate Reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 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: 240638 [Multi-domain]  Cd Length: 315  Bit Score: 39.90  E-value: 3.17e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15217924 283 VIGAGKMGKLVIKHLMAKGCtKVVVVNRSEervsaiREEMPGIEIIYRPLDEMLAcasEADVV 345
Cdd:cd12161 149 IVGTGAIGLRVARLFKAFGC-KVLAYSRSE------KEEAKALGIEYVSLDELLA---ESDIV 201
PRK07680 PRK07680
late competence protein ComER; Validated
 283-346 3.69e-03

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 39.57  E-value: 3.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15217924  283 VIGAGKMGKLVIKHLMAKGCTK---VVVVNRSEERVSAIREEMPGIEIIYRPLDemlaCASEADVVF 346
Cdd:PRK07680   5 FIGTGNMGTILIEAFLESGAVKpsqLTITNRTPAKAYHIKERYPGIHVAKTIEE----VISQSDLIF 67
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 283-351 7.31e-03

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 37.52  E-value: 7.31e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15217924 283 VIGAGKMGKLVIKHLMAKGCTKVV-VVNRSEERV-----SAIREEMPGIeIIYRPLDEMLAcASEADVVFTSTAS 351
Cdd:cd24146   5 VWGLGAMGRGIARYLLEKPGLEIVgAVDRDPAKVgkdlgELGGGAPLGV-KVTDDLDAVLA-ATKPDVVVHATTS 77
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 283-351 8.67e-03

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 36.35  E-value: 8.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15217924   283 VIGAGKMGKLVIKHLMAKGctKVVVVNRSEERVSAIREEmpGIEIIY-RPLDEML---ACASEADVVFTSTAS 351
Cdd:pfam02254   3 IIGYGRVGRSLAEELSEGG--DVVVIDKDEERVEELREE--GVPVVVgDATDEEVleeAGIEEADAVIAATGD 71
 
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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