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Conserved domains on  [gi|363652690|gb|EHL91723|]
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glutamyl-tRNA reductase [Campylobacter sp. 10_1_50]

Protein Classification

glutamyl-tRNA reductase( domain architecture ID 11477807)

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

CATH:  3.40.50.720|3.30.460.30|1.10.1200.70
EC:  1.2.1.70
Gene Ontology:  GO:0008883|GO:0050661
SCOP:  4000132

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 1-417 2.97e-164

glutamyl-tRNA reductase; Reviewed


:

Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 468.51  E-value: 2.97e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690   1 MHYLDISFTYKNTDISVREKLAFdSDEKKEQILKLINSNKNIKESMVLNTCNRVEIIASVEDVKVATAHIIRCMSIFSGV 80
Cdd:PRK00045   1 MSLLAVGLNHKTAPVELREKLAF-SEDELEEALESLLASPSVLEAVILSTCNRTEIYAVVDQFHAGREAIIRWLAEYHGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  81 FEDELYERADIYENSGAAHHLFAVASSLDSLVVGETQIVGQLKNAFKFAYDNNSCSEDISKIIHYACKCAAKVRNETQIS 160
Cdd:PRK00045  80 DLEELRPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYALAQEAGTVGTILNRLFQKAFSVAKRVRTETGIG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 161 KNPISVSSVAVAKAKEIFGTLEGKTAIVVGAGEMGELAAKHLISSGA-EVIIINRSSERVEQLVDSLGDNAswDSILKLK 239
Cdd:PRK00045 160 AGAVSVASAAVELAKQIFGDLSGKKVLVIGAGEMGELVAKHLAEKGVrKITVANRTLERAEELAEEFGGEA--IPLDELP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 240 EYVNNYDLIFSSTAAPHAIITGEIIEPREFHRY-----FFDIAVPRDIDLLNTEL--ISVYTVDSLEEIVRKNLALREEQ 312
Cdd:PRK00045 238 EALAEADIVISSTGAPHPIIGKGMVERALKARRhrpllLVDLAVPRDIEPEVGELpgVYLYDVDDLQEIVEENLAQRQEA 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 313 AQKAYSIVGQDTSEFLKTLKEDMSVPLIKSIRKQAEICAKNELEKAIKKGYLKHSDYDEAQKLIHQVFKAFLHQPTMKLK 392
Cdd:PRK00045 318 AEKAEAIVEEEVAEFMEWLRSLEVVPTIRALREQAEEIREEELERALKKLGPGEDEEEVLEKLARSLVNKLLHAPTVRLK 397

                        410       420
                 ....*....|....*....|....*
gi 363652690 393 GLAYEERAsELSNGVKFLFDIKDEQ 417
Cdd:PRK00045 398 EAAEEGDD-EYLEALRELFGLDPES 421
 
Name Accession Description Interval E-value
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 1-417 2.97e-164

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 468.51  E-value: 2.97e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690   1 MHYLDISFTYKNTDISVREKLAFdSDEKKEQILKLINSNKNIKESMVLNTCNRVEIIASVEDVKVATAHIIRCMSIFSGV 80
Cdd:PRK00045   1 MSLLAVGLNHKTAPVELREKLAF-SEDELEEALESLLASPSVLEAVILSTCNRTEIYAVVDQFHAGREAIIRWLAEYHGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  81 FEDELYERADIYENSGAAHHLFAVASSLDSLVVGETQIVGQLKNAFKFAYDNNSCSEDISKIIHYACKCAAKVRNETQIS 160
Cdd:PRK00045  80 DLEELRPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYALAQEAGTVGTILNRLFQKAFSVAKRVRTETGIG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 161 KNPISVSSVAVAKAKEIFGTLEGKTAIVVGAGEMGELAAKHLISSGA-EVIIINRSSERVEQLVDSLGDNAswDSILKLK 239
Cdd:PRK00045 160 AGAVSVASAAVELAKQIFGDLSGKKVLVIGAGEMGELVAKHLAEKGVrKITVANRTLERAEELAEEFGGEA--IPLDELP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 240 EYVNNYDLIFSSTAAPHAIITGEIIEPREFHRY-----FFDIAVPRDIDLLNTEL--ISVYTVDSLEEIVRKNLALREEQ 312
Cdd:PRK00045 238 EALAEADIVISSTGAPHPIIGKGMVERALKARRhrpllLVDLAVPRDIEPEVGELpgVYLYDVDDLQEIVEENLAQRQEA 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 313 AQKAYSIVGQDTSEFLKTLKEDMSVPLIKSIRKQAEICAKNELEKAIKKGYLKHSDYDEAQKLIHQVFKAFLHQPTMKLK 392
Cdd:PRK00045 318 AEKAEAIVEEEVAEFMEWLRSLEVVPTIRALREQAEEIREEELERALKKLGPGEDEEEVLEKLARSLVNKLLHAPTVRLK 397

                        410       420
                 ....*....|....*....|....*
gi 363652690 393 GLAYEERAsELSNGVKFLFDIKDEQ 417
Cdd:PRK00045 398 EAAEEGDD-EYLEALRELFGLDPES 421
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 1-418 3.99e-145

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: 419.90  E-value: 3.99e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690   1 MHYLDISFTYKNTDISVREKLAFdSDEKKEQILKLINSNKNIKESMVLNTCNRVEIIASVEDVKVATAHIIRCMSIFSGV 80
Cdd:COG0373    1 MSLLVVGLNHKTAPVEIREKLAF-SEEELEEALEELKAQPGVDEAVILSTCNRTEIYAVADDPHAGLEALIEFLAEYHGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  81 FEDELYERADIYENSGAAHHLFAVASSLDSLVVGETQIVGQLKNAFKFAYDNNSCSEDISKIIHYACKCAAKVRNETQIS 160
Cdd:COG0373   80 DVEELEPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYELAREAGTTGPVLNRLFQKAFSVAKRVRTETGIG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 161 KNPISVSSVAVAKAKEIFGTLEGKTAIVVGAGEMGELAAKHLISSGA-EVIIINRSSERVEQLVDSLGDNA-SWDsilKL 238
Cdd:COG0373  160 EGAVSVSSAAVELAKKIFGDLSGKTVLVIGAGEMGELAARHLAAKGVkRITVANRTLERAEELAEEFGGEAvPLE---EL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 239 KEYVNNYDLIFSSTAAPHAIITGEIIEPREFHR-----YFFDIAVPRDIDLLNTEL--ISVYTVDSLEEIVRKNLALREE 311
Cdd:COG0373  237 PEALAEADIVISSTGAPHPVITKEMVERALKKRrhrplFLIDLAVPRDIEPEVGELpgVYLYDIDDLQEVVDENLEERQA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 312 QAQKAYSIVGQDTSEFLKTLKEDMSVPLIKSIRKQAEICAKNELEKAIKK-GYLKHSDYDEAQKLIHQVFKAFLHQPTMK 390
Cdd:COG0373  317 AAPKAEAIIEEEVEEFLEWLKSREVVPTIRALREKAEAIREEELERALKKlPDLGEDEREVLEKLTRSLVNKLLHAPTVR 396

                        410       420
                 ....*....|....*....|....*...
gi 363652690 391 LKGLAYEERASELSNGVKFLFDIKDEQN 418
Cdd:COG0373  397 LKEAAAEGEDDEYLEALRRLFDLEEEEE 424
hemA TIGR01035
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ...
 3-414 1.52e-116

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: 346.68  E-value: 1.52e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690    3 YLDISFTYKNTDISVREKLAFDSDEKKEqILKLINSNKNIKESMVLNTCNRVEIIASVEDVKVATAHIIRCMSIFSGVFE 82
Cdd:TIGR01035   1 ILVLGVSHKSAPVEVREKLSIDEIKLKK-ALDTLKAEPSIEEAMVLSTCNRVEIYAVVDNLHEGKSALLQILAENKNMSN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690   83 DELYERADIYENSGAAHHLFAVASSLDSLVVGETQIVGQLKNAFKFAYDNNSCSEDISKIIHYACKCAAKVRNETQISKN 162
Cdd:TIGR01035  80 EDLEKYLYILTGESAVEHLFRVASGLDSMVVGETQILGQVKNAYKVAQEEKTVGKVLERLFQKAFSVGKRVRTETDISAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  163 PISVSSVAVAKAKEIFGTLEGKTAIVVGAGEMGELAAKHLISSGA-EVIIINRSSERVEQLVDSLGDNASwdSILKLKEY 241
Cdd:TIGR01035 160 AVSISSAAVELAERIFGSLKGKKALLIGAGEMGELVAKHLLRKGVgKILIANRTYERAEDLAKELGGEAV--KFEDLEEY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  242 VNNYDLIFSSTAAPHAIITGEIIEPREFHRY----FFDIAVPRDID--LLNTELISVYTVDSLEEIVRKNLALREEQAQK 315
Cdd:TIGR01035 238 LAEADIVISSTGAPHPIVSKEDVERALRERTrplfIIDIAVPRDVDpaVARLEGVFLYDVDDLQPVVEENLAERREEAEK 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  316 AYSIVGQDTSEFLKTLKEDMSVPLIKSIRKQAEICAKNELEKAIKKGYLKHSDYDEA-QKLIHQVFKAFLHQPTMKLKGL 394
Cdd:TIGR01035 318 AEEIVEEETAEFKQWLRSLEVEPTIKALRSLAEIVREKELEKALKKLPGLSKDVEEVlEDLARKLINKLLHAPTVRLKQL 397

                         410       420
                  ....*....|....*....|
gi 363652690  395 AYEERASELSNGVKFLFDIK 414
Cdd:TIGR01035 398 ADKEESEVCLEALKNLFGLE 417
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 3-313 4.79e-99

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: 298.03  E-value: 4.79e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690   3 YLDISFTYKNTDISVREKLAFDSDEKKEqILKLINSNKNIKESMVLNTCNRVEIIASVEDVKVATAHIIRcmsiFSGVFE 82
Cdd:cd05213    1 ILVIGLSHKTAPVELREKLAFSEEELKE-ALRRLLEKPGISEAVLLSTCNRVELYLVGDNFHKLADELEE----LLAELL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  83 DELYERADIY--ENSGAAHHLFAVASSLDSLVVGETQIVGQLKNAFKFAYDNNSCSEDISKIIHYACKCAAKVRNETQIS 160
Cdd:cd05213   76 NEPELREYLYvgRGQDAVRHLFRVASGLDSMVVGETQILGQVKNAYKLAKEAGTSGKLLNRLFQKAIKVGKRVRTETGIS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 161 KNPISVSSVAVAKAKEIFGTLEGKTAIVVGAGEMGELAAKHLISSG-AEVIIINRSSERVEQLVDSLGDNA-SWDsilKL 238
Cdd:cd05213  156 RGAVSISSAAVELAEKIFGNLKGKKVLVIGAGEMGELAAKHLAAKGvAEITIANRTYERAEELAKELGGNAvPLD---EL 232

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363652690 239 KEYVNNYDLIFSSTAAPH-AIITGEIIEPRE-FHRYFFDIAVPRDID--LLNTELISVYTVDSLEEIVRKNLALREEQA 313
Cdd:cd05213  233 LELLNEADVVISATGAPHyAKIVERAMKKRSgKPRLIVDLAVPRDIEpeVGELEGVRLYTIDDLEEVVEENLERREKEA 311
GlutR_N pfam05201
Glutamyl-tRNAGlu reductase, N-terminal domain;
9-157 2.94e-49

Glutamyl-tRNAGlu reductase, N-terminal domain;


Pssm-ID: 461585  Cd Length: 144  Bit Score: 164.21  E-value: 2.94e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690    9 TYKNTDISVREKLAFDSDEKKEQILKLinsnKNIKESMVLNTCNRVEIIASVEDVKVATAHIIRCMSIFSGVfEDELYER 88
Cdd:pfam05201   1 NHKTAPVEIREKLAFSEEELEEALQEL----RGIDEAVILSTCNRTEIYAVADDFHAALEAVIEFLAEHSGD-LEELRPY 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363652690   89 ADIYENSGAAHHLFAVASSLDSLVVGETQIVGQLKNAFKFAYDNNSCSEDISKIIHYACKCAAKVRNET 157
Cdd:pfam05201  76 LYVYEGEEAVRHLFRVASGLDSMVLGEDQILGQVKDAYELAREAGTTGPVLNRLFQKAITVAKRVRTET 144
 
Name Accession Description Interval E-value
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 1-417 2.97e-164

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 468.51  E-value: 2.97e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690   1 MHYLDISFTYKNTDISVREKLAFdSDEKKEQILKLINSNKNIKESMVLNTCNRVEIIASVEDVKVATAHIIRCMSIFSGV 80
Cdd:PRK00045   1 MSLLAVGLNHKTAPVELREKLAF-SEDELEEALESLLASPSVLEAVILSTCNRTEIYAVVDQFHAGREAIIRWLAEYHGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  81 FEDELYERADIYENSGAAHHLFAVASSLDSLVVGETQIVGQLKNAFKFAYDNNSCSEDISKIIHYACKCAAKVRNETQIS 160
Cdd:PRK00045  80 DLEELRPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYALAQEAGTVGTILNRLFQKAFSVAKRVRTETGIG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 161 KNPISVSSVAVAKAKEIFGTLEGKTAIVVGAGEMGELAAKHLISSGA-EVIIINRSSERVEQLVDSLGDNAswDSILKLK 239
Cdd:PRK00045 160 AGAVSVASAAVELAKQIFGDLSGKKVLVIGAGEMGELVAKHLAEKGVrKITVANRTLERAEELAEEFGGEA--IPLDELP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 240 EYVNNYDLIFSSTAAPHAIITGEIIEPREFHRY-----FFDIAVPRDIDLLNTEL--ISVYTVDSLEEIVRKNLALREEQ 312
Cdd:PRK00045 238 EALAEADIVISSTGAPHPIIGKGMVERALKARRhrpllLVDLAVPRDIEPEVGELpgVYLYDVDDLQEIVEENLAQRQEA 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 313 AQKAYSIVGQDTSEFLKTLKEDMSVPLIKSIRKQAEICAKNELEKAIKKGYLKHSDYDEAQKLIHQVFKAFLHQPTMKLK 392
Cdd:PRK00045 318 AEKAEAIVEEEVAEFMEWLRSLEVVPTIRALREQAEEIREEELERALKKLGPGEDEEEVLEKLARSLVNKLLHAPTVRLK 397

                        410       420
                 ....*....|....*....|....*
gi 363652690 393 GLAYEERAsELSNGVKFLFDIKDEQ 417
Cdd:PRK00045 398 EAAEEGDD-EYLEALRELFGLDPES 421
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 1-418 3.99e-145

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: 419.90  E-value: 3.99e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690   1 MHYLDISFTYKNTDISVREKLAFdSDEKKEQILKLINSNKNIKESMVLNTCNRVEIIASVEDVKVATAHIIRCMSIFSGV 80
Cdd:COG0373    1 MSLLVVGLNHKTAPVEIREKLAF-SEEELEEALEELKAQPGVDEAVILSTCNRTEIYAVADDPHAGLEALIEFLAEYHGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  81 FEDELYERADIYENSGAAHHLFAVASSLDSLVVGETQIVGQLKNAFKFAYDNNSCSEDISKIIHYACKCAAKVRNETQIS 160
Cdd:COG0373   80 DVEELEPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYELAREAGTTGPVLNRLFQKAFSVAKRVRTETGIG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 161 KNPISVSSVAVAKAKEIFGTLEGKTAIVVGAGEMGELAAKHLISSGA-EVIIINRSSERVEQLVDSLGDNA-SWDsilKL 238
Cdd:COG0373  160 EGAVSVSSAAVELAKKIFGDLSGKTVLVIGAGEMGELAARHLAAKGVkRITVANRTLERAEELAEEFGGEAvPLE---EL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 239 KEYVNNYDLIFSSTAAPHAIITGEIIEPREFHR-----YFFDIAVPRDIDLLNTEL--ISVYTVDSLEEIVRKNLALREE 311
Cdd:COG0373  237 PEALAEADIVISSTGAPHPVITKEMVERALKKRrhrplFLIDLAVPRDIEPEVGELpgVYLYDIDDLQEVVDENLEERQA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 312 QAQKAYSIVGQDTSEFLKTLKEDMSVPLIKSIRKQAEICAKNELEKAIKK-GYLKHSDYDEAQKLIHQVFKAFLHQPTMK 390
Cdd:COG0373  317 AAPKAEAIIEEEVEEFLEWLKSREVVPTIRALREKAEAIREEELERALKKlPDLGEDEREVLEKLTRSLVNKLLHAPTVR 396

                        410       420
                 ....*....|....*....|....*...
gi 363652690 391 LKGLAYEERASELSNGVKFLFDIKDEQN 418
Cdd:COG0373  397 LKEAAAEGEDDEYLEALRRLFDLEEEEE 424
hemA TIGR01035
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ...
 3-414 1.52e-116

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: 346.68  E-value: 1.52e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690    3 YLDISFTYKNTDISVREKLAFDSDEKKEqILKLINSNKNIKESMVLNTCNRVEIIASVEDVKVATAHIIRCMSIFSGVFE 82
Cdd:TIGR01035   1 ILVLGVSHKSAPVEVREKLSIDEIKLKK-ALDTLKAEPSIEEAMVLSTCNRVEIYAVVDNLHEGKSALLQILAENKNMSN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690   83 DELYERADIYENSGAAHHLFAVASSLDSLVVGETQIVGQLKNAFKFAYDNNSCSEDISKIIHYACKCAAKVRNETQISKN 162
Cdd:TIGR01035  80 EDLEKYLYILTGESAVEHLFRVASGLDSMVVGETQILGQVKNAYKVAQEEKTVGKVLERLFQKAFSVGKRVRTETDISAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  163 PISVSSVAVAKAKEIFGTLEGKTAIVVGAGEMGELAAKHLISSGA-EVIIINRSSERVEQLVDSLGDNASwdSILKLKEY 241
Cdd:TIGR01035 160 AVSISSAAVELAERIFGSLKGKKALLIGAGEMGELVAKHLLRKGVgKILIANRTYERAEDLAKELGGEAV--KFEDLEEY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  242 VNNYDLIFSSTAAPHAIITGEIIEPREFHRY----FFDIAVPRDID--LLNTELISVYTVDSLEEIVRKNLALREEQAQK 315
Cdd:TIGR01035 238 LAEADIVISSTGAPHPIVSKEDVERALRERTrplfIIDIAVPRDVDpaVARLEGVFLYDVDDLQPVVEENLAERREEAEK 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  316 AYSIVGQDTSEFLKTLKEDMSVPLIKSIRKQAEICAKNELEKAIKKGYLKHSDYDEA-QKLIHQVFKAFLHQPTMKLKGL 394
Cdd:TIGR01035 318 AEEIVEEETAEFKQWLRSLEVEPTIKALRSLAEIVREKELEKALKKLPGLSKDVEEVlEDLARKLINKLLHAPTVRLKQL 397

                         410       420
                  ....*....|....*....|
gi 363652690  395 AYEERASELSNGVKFLFDIK 414
Cdd:TIGR01035 398 ADKEESEVCLEALKNLFGLE 417
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 3-313 4.79e-99

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: 298.03  E-value: 4.79e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690   3 YLDISFTYKNTDISVREKLAFDSDEKKEqILKLINSNKNIKESMVLNTCNRVEIIASVEDVKVATAHIIRcmsiFSGVFE 82
Cdd:cd05213    1 ILVIGLSHKTAPVELREKLAFSEEELKE-ALRRLLEKPGISEAVLLSTCNRVELYLVGDNFHKLADELEE----LLAELL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  83 DELYERADIY--ENSGAAHHLFAVASSLDSLVVGETQIVGQLKNAFKFAYDNNSCSEDISKIIHYACKCAAKVRNETQIS 160
Cdd:cd05213   76 NEPELREYLYvgRGQDAVRHLFRVASGLDSMVVGETQILGQVKNAYKLAKEAGTSGKLLNRLFQKAIKVGKRVRTETGIS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 161 KNPISVSSVAVAKAKEIFGTLEGKTAIVVGAGEMGELAAKHLISSG-AEVIIINRSSERVEQLVDSLGDNA-SWDsilKL 238
Cdd:cd05213  156 RGAVSISSAAVELAEKIFGNLKGKKVLVIGAGEMGELAAKHLAAKGvAEITIANRTYERAEELAKELGGNAvPLD---EL 232

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363652690 239 KEYVNNYDLIFSSTAAPH-AIITGEIIEPRE-FHRYFFDIAVPRDID--LLNTELISVYTVDSLEEIVRKNLALREEQA 313
Cdd:cd05213  233 LELLNEADVVISATGAPHyAKIVERAMKKRSgKPRLIVDLAVPRDIEpeVGELEGVRLYTIDDLEEVVEENLERREKEA 311
PLN00203 PLN00203
glutamyl-tRNA reductase
 6-361 4.43e-63

glutamyl-tRNA reductase


Pssm-ID: 215101 [Multi-domain]  Cd Length: 519  Bit Score: 211.92  E-value: 4.43e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690   6 ISFTYKNTDISVREKLAFDSDEKKEQILKLINSNkNIKESMVLNTCNRVEIIASVEDVKVATAHIIRCMSIFSGVFEDEL 85
Cdd:PLN00203  88 IGLSIHTAPVEMREKLAIPEAEWPRAIAELCSLN-HIEEAAVLSTCNRMEIYVVALSWHRGVKEVTEWMSKTSGIPVSEL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  86 YERADIYENSGAAHHLFAVASSLDSLVVGETQIVGQLKNAFKFAYDNNSCSEDISKIIHYACKCAAKVRNETQISKNPIS 165
Cdd:PLN00203 167 RQHLFLLYDKDATQHLFEVSGGLDSLVLGEGQILAQVKQVVKVGQGVDGFGRNLSGLFKHAITAGKRVRTETNIASGAVS 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 166 VSSVAV--AKAKEIFGTLEGKTAIVVGAGEMGELAAKHLISSG-AEVIIINRSSERVEQLVDSLGD-NASWDSILKLKEY 241
Cdd:PLN00203 247 VSSAAVelALMKLPESSHASARVLVIGAGKMGKLLVKHLVSKGcTKMVVVNRSEERVAALREEFPDvEIIYKPLDEMLAC 326

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 242 VNNYDLIFSSTAAPHAIITGEIIEP-------REFHRYFFDIAVPRDIDLLNTELIS--VYTVDSLEEIVRKNLALREEQ 312
Cdd:PLN00203 327 AAEADVVFTSTSSETPLFLKEHVEAlppasdtVGGKRLFVDISVPRNVGACVSELESarVYNVDDLKEVVAANKEDRLRK 406

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 363652690 313 AQKAYSIVGQDTSEFlKTLKEDMS-VPLIKSIRKQAEICAKNELEKAIKK 361
Cdd:PLN00203 407 AMEAQTIIREESKNF-EAWRDSLEtVPTIKKLRSYAERIRAAELEKCLSK 455
GlutR_N pfam05201
Glutamyl-tRNAGlu reductase, N-terminal domain;
9-157 2.94e-49

Glutamyl-tRNAGlu reductase, N-terminal domain;


Pssm-ID: 461585  Cd Length: 144  Bit Score: 164.21  E-value: 2.94e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690    9 TYKNTDISVREKLAFDSDEKKEQILKLinsnKNIKESMVLNTCNRVEIIASVEDVKVATAHIIRCMSIFSGVfEDELYER 88
Cdd:pfam05201   1 NHKTAPVEIREKLAFSEEELEEALQEL----RGIDEAVILSTCNRTEIYAVADDFHAALEAVIEFLAEHSGD-LEELRPY 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363652690   89 ADIYENSGAAHHLFAVASSLDSLVVGETQIVGQLKNAFKFAYDNNSCSEDISKIIHYACKCAAKVRNET 157
Cdd:pfam05201  76 LYVYEGEEAVRHLFRVASGLDSMVLGEDQILGQVKDAYELAREAGTTGPVLNRLFQKAITVAKRVRTET 144
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 174-301 6.87e-39

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: 136.55  E-value: 6.87e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  174 AKEIFGTLEGKTAIVVGAGEMGELAAKHLISSGA-EVIIINRSSERVEQLVDSLGDNASwDSILKLKEYVNNYDLIFSST 252
Cdd:pfam01488   3 AKKIFGDLKDKKVLLIGAGEMGELVAKHLLAKGAkEVTIANRTIERAQELAEKFGGVEA-LPLDDLKEYLAEADIVISAT 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 363652690  253 AAPHAIITGEIIE----PREFHRYFFDIAVPRDIDLLNTEL--ISVYTVDSLEEI 301
Cdd:pfam01488  82 SSPTPIITKEMVEralkPRKKPLLFVDIAVPRDIEPEVGELegVYLYTVDDLKEV 136
PRK13940 PRK13940
glutamyl-tRNA reductase; Provisional
 1-400 9.33e-35

glutamyl-tRNA reductase; Provisional


Pssm-ID: 172450 [Multi-domain]  Cd Length: 414  Bit Score: 133.60  E-value: 9.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690   1 MHYLDISFTYKNTDISVREKLAFdSDEKKEQILKLINSNKNIKESMVLNTCNRVEIIASVEDVKVatahIIRCMSIFSGV 80
Cdd:PRK13940   1 MALISLAIDYKKSPIEVRSEFAL-SGLDVSMLYRSILAIDNVVHAVILSTCNRTEVYLEISDLRV----VDDILVWWQGY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  81 FEDELYERADIY---ENSGAAHHLFAVASSLDSLVVGETQIVGQLKNAFKFAYDNNSCSEDISKIIHYACKCAAKVRNET 157
Cdd:PRK13940  76 VRNPNYKIKDYFklrQGTEVIMHLMKLACGLESMVLGEPQILGQVKDSYTLSKKNHAIGKELDRVFQKVFATAKRVRSET 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 158 QISKNPISVSSVAVAKAKEIFGTLEGKTAIVVGAGEMGELAAKHLIS-SGAEVIIINRSSERVEQLVDSLgDNASWDSIL 236
Cdd:PRK13940 156 RIGHCPVSVAFSAITLAKRQLDNISSKNVLIIGAGQTGELLFRHVTAlAPKQIMLANRTIEKAQKITSAF-RNASAHYLS 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 237 KLKEYVNNYDLIFSSTAAPHAIITGEIIEPREfhRYFFDIAVPRDID--LLNTELISVYTVDSLEEIVRKNLALREEQAQ 314
Cdd:PRK13940 235 ELPQLIKKADIIIAAVNVLEYIVTCKYVGDKP--RVFIDISIPQALDpkLGELEQNVYYCVDDINAVIEDNKDKRKYESS 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 315 KAYSIVGQDTSEFLKTLKEDMSVPLIKSIRKQAEICAKNELEKAIKKGYLKHSDYDEAQKLIHQVFKAFLHQPTMKLKGL 394
Cdd:PRK13940 313 KAQKIIVKSLEEYLEKEKAIISNSAIKELFQKADGLVDLSLEKSLAKIRNGKDAEEIIKRFAYEIKKKVLHYPVVGMKEA 392


                 ....*.
gi 363652690 395 AYEERA 400
Cdd:PRK13940 393 SKQGRS 398
GlutR_dimer pfam00745
Glutamyl-tRNAGlu reductase, dimerization domain;
315-398 1.08e-14

Glutamyl-tRNAGlu reductase, dimerization domain;


Pssm-ID: 459922 [Multi-domain]  Cd Length: 95  Bit Score: 69.14  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  315 KAYSIVGQDTSEFLKTLKEDMSVPLIKSIRKQAEICAKNELEKAIKKGYLKHSDYDEAQKLIHQVFKAFLHQPTMKLKGL 394
Cdd:pfam00745   1 KAEAIIEEEVEEFMAWLKSLEVVPTIRALREKAEEIREEELERALKKLGLDGEDREELEKLTRSLVNKLLHDPTVRLKEA 80


                  ....
gi 363652690  395 AYEE 398
Cdd:pfam00745  81 EEGD 84
hemA PRK00676
glutamyl-tRNA reductase; Validated
 15-316 1.47e-11

glutamyl-tRNA reductase; Validated


Pssm-ID: 234810 [Multi-domain]  Cd Length: 338  Bit Score: 65.27  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  15 ISVREKlAFDSDEKKEQILKLINSNKNIKE--------SMVLNTCNRVEIIA---SVEDVKVATAHIIRCMSIfsgvfed 83
Cdd:PRK00676   8 ISYREA-ALKEREQVIQILQQFEGSLFFRQrffgeegdFVLLLTCHRAELYYysvSPAELQSSLLSEITSLGV------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  84 elyeRADIYENSGAAHHLFAVASSLDSLVVGETQIVGQLKNAFKFAYDNNSCSEDISKIIHYACKCAAKVRNETQISKNP 163
Cdd:PRK00676  80 ----RPYFYRGLDCFTHLFCVTSGMDSLILGETEIQGQVKRAYLKAARERKLPFALHFLFQKALKEGKVFRSKGGAPYAE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 164 ISVSSVaVAKAKEIFGTLEGKTAIVVGAGEMGELAAKHLISSGAEVIIINrSSERVeqlvdslgdNASWDSILKLK-EYV 242
Cdd:PRK00676 156 VTIESV-VQQELRRRQKSKKASLLFIGYSEINRKVAYYLQRQGYSRITFC-SRQQL---------TLPYRTVVREElSFQ 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 243 NNYDLIF-----SSTAAPHAIITGEIIEPRefhRYFFDIAVPRDIDLLNTELISVYT-VDSLEEIVRKNLALREEQAQKA 316
Cdd:PRK00676 225 DPYDVIFfgsseSAYAFPHLSWESLADIPD---RIVFDFNVPRTFPWSETPFPHRYLdMDFISEWVQKHLQCRKEVNNKH 301
aroE PRK00258
shikimate 5-dehydrogenase; Reviewed
 181-276 1.98e-09

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 234703 [Multi-domain]  Cd Length: 278  Bit Score: 58.28  E-value: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 181 LEGKTAIVVGAGemGelAAK----HLISSG-AEVIIINRSSERVEQLVDSLGDNASWDSILKLKEYVNNYDLIFSSTAA- 254
Cdd:PRK00258 121 LKGKRILILGAG--G--AARavilPLLDLGvAEITIVNRTVERAEELAKLFGALGKAELDLELQEELADFDLIINATSAg 196

                         90       100
                 ....*....|....*....|....*..
gi 363652690 255 -----PHAIITGEIIEPrefHRYFFDI 276
Cdd:PRK00258 197 msgelPLPPLPLSLLRP---GTIVYDM 220
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 181-319 4.08e-09

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: 54.97  E-value: 4.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 181 LEGKTAIVVGAGEMGELAAKHLISSGA-EVIIINRSSERVEQLVDSLGDNASWDSILKLKEYVNNYDLIFSSTAAPHAII 259
Cdd:cd01065   17 LKGKKVLILGAGGAARAVAYALAELGAaKIVIVNRTLEKAKALAERFGELGIAIAYLDLEELLAEADLIINTTPVGMKPG 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 363652690 260 TGEIIEPREFH--RYFFDIAV-PRDIDLLN-TELISVYTVDSLEEIVrknlalreEQAQKAYSI 319
Cdd:cd01065   97 DELPLPPSLLKpgGVVYDVVYnPLETPLLKeARALGAKTIDGLEMLV--------YQAAEAFEL 152
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 180-230 2.50e-07

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 51.34  E-value: 2.50e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 363652690 180 TLEGKTAIVVGAGE-MGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDNA 230
Cdd:COG4221    2 SDKGKVALITGASSgIGAATARALAAAGARVVLAARRAERLEALAAELGGRA 53
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 170-255 2.27e-06

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: 47.77  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 170 AVAKAKEIFGT-LEGKTAIVVGA-GEMGELAAKHLISSGAEVIIINRSSERVEQLVDSLG-------DNASWDSILKLKE 240
Cdd:cd01078   14 AAGKALELMGKdLKGKTAVVLGGtGPVGQRAAVLLAREGARVVLVGRDLERAQKAADSLRarfgegvGAVETSDDAARAA 93

                         90
                 ....*....|....*
gi 363652690 241 YVNNYDLIFSSTAAP 255
Cdd:cd01078   94 AIKGADVVFAAGAAG 108
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 181-226 2.86e-06

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 48.24  E-value: 2.86e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 363652690 181 LEGKTAIVVGAGE-MGELAAKHLISSGAEVIIINRSSERVEQLVDSL 226
Cdd:COG1028    4 LKGKVALVTGGSSgIGRAIARALAAEGARVVITDRDAEALEAAAAEL 50
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 188-266 4.39e-06

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: 46.31  E-value: 4.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  188 VVGAGEMGELAAKHLISSGAEVIIINRSSERVEQLVDslgDNASW-DSIlklKEYVNNYDLIFSS-TAAPH--AIITGEI 263
Cdd:pfam03446   4 FIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVA---AGAIAaASP---AEFVAGLDVVITMvPAGAAvdAVIFGEG 77


                  ...
gi 363652690  264 IEP 266
Cdd:pfam03446  78 LLP 80
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 181-252 7.46e-06

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


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 44.39  E-value: 7.46e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 363652690  181 LEGKTAIVVGAGEMGELAAKHLISSGAEVIII-NRSSERVEQLVDSLGDnaswdsilKLKEYVNNYDLIFSST 252
Cdd:pfam13241   5 LRGKRVLVVGGGEVAARKARKLLEAGAKVTVVsPEITPFLEGLLDLIRR--------EFEGDLDGADLVIAAT 69
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 187-252 1.84e-05

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: 46.21  E-value: 1.84e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 363652690 187 IVVGAGEMGELAAKHLISSGAEVIIINRSSERVEQLVDSL-----GDnASWDSILKlKEYVNNYDLIFSST 252
Cdd:COG0569   99 IIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDvlvivGD-ATDEEVLE-EAGIEDADAVIAAT 167
FabG-like PRK07231
SDR family oxidoreductase;
181-228 3.75e-05

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 44.82  E-value: 3.75e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 363652690 181 LEGKTAIVVGAGE-MGELAAKHLISSGAEVIIINRSSERVEQLVDSLGD 228
Cdd:PRK07231   3 LEGKVAIVTGASSgIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILA 51
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 181-229 5.15e-05

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 44.89  E-value: 5.15e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 363652690 181 LEGKTAIVVGA-GEMGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDN 229
Cdd:PRK08277   8 LKGKVAVITGGgGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAA 57
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 163-260 6.16e-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: 44.91  E-value: 6.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 163 PISVSSVAVAKAKEifgtLEGKTAIVVGAGEMGELAAKHLISSGAE-VIIINRSSERVE--------QLVDSLGDNASWd 233
Cdd:cd08236  144 PAAVALHAVRLAGI----TLGDTVVVIGAGTIGLLAIQWLKILGAKrVIAVDIDDEKLAvarelgadDTINPKEEDVEK- 218

                         90       100
                 ....*....|....*....|....*....
gi 363652690 234 silkLKEYVNN--YDLIFSSTAAPHAIIT 260
Cdd:cd08236  219 ----VRELTEGrgADLVIEAAGSPATIEQ 243
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 181-230 6.46e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 44.23  E-value: 6.46e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 363652690 181 LEGKTAIVVGAGEM-GELAAKHLISSGAEVIIINRSSERVEQLVDSLGDNA 230
Cdd:PRK08265   4 LAGKVAIVTGGATLiGAAVARALVAAGARVAIVDIDADNGAAVAASLGERA 54
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 173-242 9.29e-05

Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomains but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants.


Pssm-ID: 240625 [Multi-domain]  Cd Length: 313  Bit Score: 44.05  E-value: 9.29e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 363652690 173 KAKEIFGTLEGKTAIVVGAGEMG-ELA--AKHLissGAEVIIINRSSERVEQLVDSLGDNASWDSILKLKEYV 242
Cdd:cd05300  124 QRRGPVRELAGKTVLIVGLGDIGrEIArrAKAF---GMRVIGVRRSGRPAPPVVDEVYTPDELDELLPEADYV 193
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 181-232 1.01e-04

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 43.53  E-value: 1.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 363652690 181 LEGKTAIVVGAGE-MGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDNASW 232
Cdd:cd05345    3 LEGKVAIVTGAGSgFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIA 55
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
188-231 1.11e-04

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 43.24  E-value: 1.11e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 363652690 188 VVGAGEMGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDNAS 231
Cdd:COG2085    3 IIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAELGPGAR 46
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
180-226 1.39e-04

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 43.32  E-value: 1.39e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 363652690 180 TLEGKTAIVVGA-GEMGELAAKHLISSGAEVIIINRSSERVEQLVDSL 226
Cdd:COG0300    2 SLTGKTVLITGAsSGIGRALARALAARGARVVLVARDAERLEALAAEL 49
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
 163-259 1.59e-04

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 43.47  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 163 PISVSSVAVAKAKEIFGTLE--GKTAIVVGAGEMGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDNA---SWDSiLK 237
Cdd:PLN02178 157 PLLCAGITVYSPMKYYGMTKesGKRLGVNGLGGLGHIAVKIGKAFGLRVTVISRSSEKEREAIDRLGADSflvTTDS-QK 235

                         90       100
                 ....*....|....*....|..
gi 363652690 238 LKEYVNNYDLIFSSTAAPHAII 259
Cdd:PLN02178 236 MKEAVGTMDFIIDTVSAEHALL 257
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 181-276 1.90e-04

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 42.83  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 181 LEGKTAIVVGA-GEMGELAAKHLISSGAEVIIINRSSERVEQLVDSL-----------GDNASWDSILKLKEYVN----N 244
Cdd:cd08935    3 LKNKVAVITGGtGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEItalggraialaADVLDRASLERAREEIVaqfgT 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 363652690 245 YDLIFSSTAA--PHAIITGEIIEPrEFHRYFFDI 276
Cdd:cd08935   83 VDILINGAGGnhPDATTDPEHYEP-ETEQNFFDL 115
aroE TIGR00507
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ...
 183-277 2.21e-04

shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally equivalent domains from larger, multifunctional proteins of fungi and plants. Below the trusted cutoff of 180, but above the noise cutoff of 20, are the putative shikimate dehydrogenases of Thermotoga maritima and Mycobacterium tuberculosis, and uncharacterized paralogs of shikimate dehydrogenase from E. coli and H. influenzae. The related enzyme quinate 5-dehydrogenase scores below the noise cutoff. A neighbor-joining tree, constructed with quinate 5-dehydrogenases as the outgroup, shows the Clamydial homolog as clustering among the shikimate dehydrogenases, although the sequence is unusual in the degree of sequence divergence and the presence of an additional N-terminal domain. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 161904 [Multi-domain]  Cd Length: 270  Bit Score: 42.79  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  183 GKTAIVVGAGEMGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDNASWDSILKLKEYVNNYDLIFSSTAAPHAIITGE 262
Cdd:TIGR00507 117 NQNVLIIGAGGAAKAVALELLKADCNVIIANRTVSKAEELAERFQRYGEIQAFSMDELPLHRVDLIINATSAGMSGNIDE 196

                          90
                  ....*....|....*...
gi 363652690  263 IIEPREFHR---YFFDIA 277
Cdd:TIGR00507 197 PPVPAEYLKegkLVYDLV 214
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 181-226 2.50e-04

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 42.53  E-value: 2.50e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 363652690 181 LEGKTAIVVGAGE-MGELAAKHLISSGAEVIIINRSSERVEQLVDSL 226
Cdd:cd08934    1 LQGKVALVTGASSgIGEATARALAAEGAAVAIAARRVDRLEALADEL 47
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 163-259 3.41e-04

Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain dehydrogenase/zinc-dependent alcohol dehydrogenase-like family, catalyzes the NADP(+)-dependent oxidation of glucose to gluconate, the first step in the Entner-Doudoroff pathway, an alternative to or substitute for glycolysis or the pentose phosphate pathway. 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-Rossman 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: 176192 [Multi-domain]  Cd Length: 355  Bit Score: 42.59  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 163 PISVSSVAVAKAKEI---FGTLEGKTAIVVGAGEMGELAAKHLISSGAEVIIINR---SSERVEqLVDSLGDN--ASWDS 234
Cdd:cd08230  150 PLSVVEKAIEQAEAVqkrLPTWNPRRALVLGAGPIGLLAALLLRLRGFEVYVLNRrdpPDPKAD-IVEELGATyvNSSKT 228

                         90       100
                 ....*....|....*....|....*
gi 363652690 235 ILKLKEYVNNYDLIFSSTAAPHAII 259
Cdd:cd08230  229 PVAEVKLVGEFDLIIEATGVPPLAF 253
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 163-258 3.73e-04

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. 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: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 42.18  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 163 PISVSSVAVAKAkeifGTLEGKTAIVVGAGEMGELAAKHLISSGAEVIIINRSSER----VEQLVDSLGDNASWDSILKL 238
Cdd:cd08261  144 PLAIGAHAVRRA----GVTAGDTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERlefaRELGADDTINVGDEDVAARL 219

                         90       100
                 ....*....|....*....|..
gi 363652690 239 KEYVNN--YDLIFSSTAAPHAI 258
Cdd:cd08261  220 RELTDGegADVVIDATGNPASM 241
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 179-232 3.75e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 42.26  E-value: 3.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 363652690 179 GTLEGKTAIVVGAGE-MGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDNASW 232
Cdd:PRK05872   5 TSLAGKVVVVTGAARgIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRV 59
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 172-227 3.78e-04

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


Pssm-ID: 133444  Cd Length: 200  Bit Score: 41.42  E-value: 3.78e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 363652690 172 AKAKEIFGT--LEGKTAIVVGAGEMGELAAKHLISSGAEVIIINRSSERVEQLVDSLG 227
Cdd:cd01075   15 AAAEHLLGTdsLEGKTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAELFG 72
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 163-258 5.24e-04

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 41.98  E-value: 5.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 163 PISVSSVAVAKAkeifGTLEGKTAIVVGAGEMGELAAKHLISSGAEVIIINRSSERVEQLVDSLGD----NASWDSILKL 238
Cdd:PRK09880 154 PLAVAIHAAHQA----GDLQGKRVFVSGVGPIGCLIVAAVKTLGAAEIVCADVSPRSLSLAREMGAdklvNPQNDDLDHY 229

                         90       100
                 ....*....|....*....|
gi 363652690 239 KEYVNNYDLIFSSTAAPHAI 258
Cdd:PRK09880 230 KAEKGYFDVSFEVSGHPSSI 249
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 179-230 8.86e-04

Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases.


Pssm-ID: 240631 [Multi-domain]  Cd Length: 310  Bit Score: 41.06  E-value: 8.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 363652690 179 GTLEGKTAIVVGAGEMGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDNA 230
Cdd:cd12154  156 PDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKNV 207
NAD_bind_amino_acid_DH cd05191
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ...
 165-215 1.17e-03

NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and are found in glutamate, leucine, and phenylalanine DHs (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: 133449 [Multi-domain]  Cd Length: 86  Bit Score: 37.74  E-value: 1.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 363652690 165 SVSSVAVAKA-KEIFGTLEGKTAIVVGAGEMGELAAKHL-ISSGAEVIIINRS 215
Cdd:cd05191    4 AGAVALLKAAgKVTNKSLKGKTVVVLGAGEVGKGIAKLLaDEGGKKVVLCDRD 56
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 179-230 1.20e-03

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 40.44  E-value: 1.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 363652690 179 GTLEGKTAIVVGAGE-MGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDNA 230
Cdd:cd05341    1 NRLKGKVAIVTGGARgLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAA 53
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 183-230 1.47e-03

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 39.93  E-value: 1.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 363652690 183 GKTAIVVGAGE-MGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDNA 230
Cdd:cd08939    1 GKHVLITGGSSgIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEA 49
trkA PRK09496
Trk system potassium transporter TrkA;
187-226 1.50e-03

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 40.49  E-value: 1.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 363652690 187 IVVGAGEMGELAAKHLISSGAEVIIINRSSERVEQLVDSL 226
Cdd:PRK09496   4 IIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRL 43
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 181-237 1.83e-03

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 39.76  E-value: 1.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 363652690 181 LEGKTAIVVGAGE-MGELAAKHLISSGAEVIIINRSSERVEQLVDS-------LGDNASWDSILK 237
Cdd:cd05351    5 FAGKRALVTGAGKgIGRATVKALAKAGARVVAVSRTQADLDSLVREcpgiepvCVDLSDWDATEE 69
PRK06124 PRK06124
SDR family oxidoreductase;
181-226 1.89e-03

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 39.70  E-value: 1.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 363652690 181 LEGKTAIVVGAGE-MGELAAKHLISSGAEVIIINRSSERVEQLVDSL 226
Cdd:PRK06124   9 LAGQVALVTGSARgLGFEIARALAGAGAHVLVNGRNAATLEAAVAAL 55
murD PRK14106
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
 181-255 2.18e-03

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


Pssm-ID: 184511 [Multi-domain]  Cd Length: 450  Bit Score: 40.34  E-value: 2.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363652690 181 LEGKTAIVVGAGEMGELAAKHLISSGAEVIIINRSSErvEQLVDSLGDNASWDSILKLKEY----VNNYDLIFSSTAAP 255
Cdd:PRK14106   3 LKGKKVLVVGAGVSGLALAKFLKKLGAKVILTDEKEE--DQLKEALEELGELGIELVLGEYpeefLEGVDLVVVSPGVP 79
PLN02520 PLN02520
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
 181-230 2.36e-03

bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase


Pssm-ID: 178135 [Multi-domain]  Cd Length: 529  Bit Score: 40.13  E-value: 2.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 363652690 181 LEGKTAIVVGAGEMGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDNA 230
Cdd:PLN02520 377 LAGKLFVVIGAGGAGKALAYGAKEKGARVVIANRTYERAKELADAVGGQA 426
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 181-229 3.02e-03

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 39.05  E-value: 3.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 363652690 181 LEGKTAIVVGA-GEMGELAAKHLISSGAEVIII-NRSSERVEQLVDSLGDN 229
Cdd:PRK05565   3 LMGKVAIVTGAsGGIGRAIAELLAKEGAKVVIAyDINEEAAQELLEEIKEE 53
PRK09242 PRK09242
SDR family oxidoreductase;
180-226 3.21e-03

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 38.96  E-value: 3.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 363652690 180 TLEGKTAIVVGAGE-MGELAAKHLISSGAEVIIINRSSERVEQLVDSL 226
Cdd:PRK09242   6 RLDGQTALITGASKgIGLAIAREFLGLGADVLIVARDADALAQARDEL 53
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 181-231 3.26e-03

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 38.88  E-value: 3.26e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 363652690 181 LEGKTAIVVGAGE-MGELAAKHLISSGAEVIIINRSSERVE---QLVDSLGDNAS 231
Cdd:cd05347    3 LKGKVALVTGASRgIGFGIASGLAEAGANIVINSRNEEKAEeaqQLIEKEGVEAT 57
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
180-229 3.38e-03

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 38.99  E-value: 3.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 363652690 180 TLEGKTAIVVGA-GEMGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDN 229
Cdd:PRK05653   2 SLQGKTALVTGAsRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAA 52
cysG_Nterm TIGR01470
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ...
 177-255 3.51e-03

siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal region-related sequences. All sequences in the seed alignment for this model are N-terminal regions of known or predicted siroheme synthases. The C-terminal region of each is uroporphyrin-III C-methyltransferase (EC 2.1.1.107), which catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). The region represented by this model completes the process of oxidation and iron insertion to yield siroheme. Siroheme is a cofactor for nitrite and sulfite reductases, so siroheme synthase is CysG of cysteine biosynthesis in some organisms. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 130536 [Multi-domain]  Cd Length: 205  Bit Score: 38.54  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690  177 IFGTLEGKTAIVVGAGEMGELAAKHLISSGAEVIIINRSSERVEQLVdsLGDN-ASWDSILKLKEYVNNYDLIFSSTAAP 255
Cdd:TIGR01470   3 VFANLEGRAVLVVGGGDVALRKARLLLKAGAQLRVIAEELESELTLL--AEQGgITWLARCFDADILEGAFLVIAATDDE 80
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
181-230 4.47e-03

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 38.47  E-value: 4.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 363652690 181 LEGKTAIVVG-AGEMGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDNA 230
Cdd:PRK07067   4 LQGKVALLTGaASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAA 54
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 175-228 4.68e-03

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 38.58  E-value: 4.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 363652690 175 KEIFgTLEGKTAIVVGAGE-MGELAAKHLISSGAEVIIINRSSERVEQLVDSLGD 228
Cdd:PRK08085   2 NDLF-SLAGKNILITGSAQgIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQ 55
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 181-230 4.82e-03

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 38.53  E-value: 4.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 363652690 181 LEGKTAIVVGAGE-MGELAAKHLISSGAEVII-INRSSERVEQLVDSLGDNA 230
Cdd:PRK08642   3 ISEQTVLVTGGSRgLGAAIARAFAREGARVVVnYHQSEDAAEALADELGDRA 54
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
181-227 4.86e-03

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 39.06  E-value: 4.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 363652690 181 LEGKTAIVVG-AGEMGELAAKHLISSGAEVIIINRSSERVEQLVDSLG 227
Cdd:PRK08324 420 LAGKVALVTGaAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELG 467
PRK07041 PRK07041
SDR family oxidoreductase;
187-231 7.34e-03

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 37.71  E-value: 7.34e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 363652690 187 IVVGAGEMGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDNAS 231
Cdd:PRK07041   2 VVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGAP 46
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 188-224 7.66e-03

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 38.17  E-value: 7.66e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 363652690 188 VVGAGEMGELAAKHLISSGAEVIIINRSSERVEQLVD 224
Cdd:COG2084    6 FIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVA 42
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 168-258 7.97e-03

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


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 38.20  E-value: 7.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363652690 168 SVAVaKAKEIFGTLEGKTAIVVGAGEMGELAAKHLISSGA-EVIIINRSSERVEqLVDSLG-----DNASWDSILKLKEY 241
Cdd:COG1063  148 AVAL-HAVERAGVKPGDTVLVIGAGPIGLLAALAARLAGAaRVIVVDRNPERLE-LARELGadavvNPREEDLVEAVREL 225

                         90
                 ....*....|....*....
gi 363652690 242 VNN--YDLIFSSTAAPHAI 258
Cdd:COG1063  226 TGGrgADVVIEAVGAPAAL 244
PRK06500 PRK06500
SDR family oxidoreductase;
181-230 8.29e-03

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 37.63  E-value: 8.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 363652690 181 LEGKTAIVVG--AGeMGELAAKHLISSGAEVIIINRSSERVEQLVDSLGDNA 230
Cdd:PRK06500   4 LQGKTALITGgtSG-IGLETARQFLAEGARVAITGRDPASLEAARAELGESA 54
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
186-222 8.91e-03

Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];


Pssm-ID: 440839 [Multi-domain]  Cd Length: 279  Bit Score: 37.79  E-value: 8.91e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 363652690 186 AIVVGAGEMGELAAKHLISSGAEVIIINRSSERVEQL 222
Cdd:COG1226  127 VIIAGFGRVGQIVARLLRAEGIPFVVIDLDPERVEEL 163
 
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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