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Conserved domains on  [gi|446095353|ref|WP_000173208|]
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MULTISPECIES: glutamyl-tRNA reductase [Salmonella]

Protein Classification

glutamyl-tRNA reductase( domain architecture ID 11477807)

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

EC:  1.2.1.70
Gene Ontology:  GO:0008883|GO:0050661
SCOP:  4000132

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
1-418 0e+00

glutamyl-tRNA reductase; Reviewed


:

Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 602.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353   1 MTLLALGINHKTAPVSLRERVTFSPDTLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNLN 80
Cdd:PRK00045   1 MSLLAVGLNHKTAPVELREKLAFSEDELEEALESLLASPSVLEAVILSTCNRTEIYAVVDQFHAGREAIIRWLAEYHGLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  81 EDDLRNSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTETDIGA 160
Cdd:PRK00045  81 LEELRPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYALAQEAGTVGTILNRLFQKAFSVAKRVRTETGIGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 161 SAVSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGAEVISLSDIDARL 240
Cdd:PRK00045 161 GAVSVASAAVELAKQIFGDLSGKKVLVIGAGEMGELVAKHLAEKGVRKITVANRTLERAEELAEEFGGEAIPLDELPEAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 241 QDADIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLAQRQAAAVE 320
Cdd:PRK00045 241 AEADIVISSTGAPHPIIGKGMVERALKARRHRPLLLVDLAVPRDIEPEVGELPGVYLYDVDDLQEIVEENLAQRQEAAEK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 321 AETIVEQEASEFMAWLRAQGASETIREYRSQSEQIRDELTTKALSALQQGGDAQAILQDLAWKLTNRLIHAPTKSLQQAA 400
Cdd:PRK00045 321 AEAIVEEEVAEFMEWLRSLEVVPTIRALREQAEEIREEELERALKKLGPGEDEEEVLEKLARSLVNKLLHAPTVRLKEAA 400
                        410
                 ....*....|....*...
gi 446095353 401 RDGDDERLNILRDSLGLE 418
Cdd:PRK00045 401 EEGDDEYLEALRELFGLD 418
 
Name Accession Description Interval E-value
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
1-418 0e+00

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 602.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353   1 MTLLALGINHKTAPVSLRERVTFSPDTLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNLN 80
Cdd:PRK00045   1 MSLLAVGLNHKTAPVELREKLAFSEDELEEALESLLASPSVLEAVILSTCNRTEIYAVVDQFHAGREAIIRWLAEYHGLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  81 EDDLRNSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTETDIGA 160
Cdd:PRK00045  81 LEELRPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYALAQEAGTVGTILNRLFQKAFSVAKRVRTETGIGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 161 SAVSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGAEVISLSDIDARL 240
Cdd:PRK00045 161 GAVSVASAAVELAKQIFGDLSGKKVLVIGAGEMGELVAKHLAEKGVRKITVANRTLERAEELAEEFGGEAIPLDELPEAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 241 QDADIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLAQRQAAAVE 320
Cdd:PRK00045 241 AEADIVISSTGAPHPIIGKGMVERALKARRHRPLLLVDLAVPRDIEPEVGELPGVYLYDVDDLQEIVEENLAQRQEAAEK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 321 AETIVEQEASEFMAWLRAQGASETIREYRSQSEQIRDELTTKALSALQQGGDAQAILQDLAWKLTNRLIHAPTKSLQQAA 400
Cdd:PRK00045 321 AEAIVEEEVAEFMEWLRSLEVVPTIRALREQAEEIREEELERALKKLGPGEDEEEVLEKLARSLVNKLLHAPTVRLKEAA 400
                        410
                 ....*....|....*...
gi 446095353 401 RDGDDERLNILRDSLGLE 418
Cdd:PRK00045 401 EEGDDEYLEALRELFGLD 418
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
1-418 0e+00

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: 582.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353   1 MTLLALGINHKTAPVSLRERVTFSPDTLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNLN 80
Cdd:COG0373    1 MSLLVVGLNHKTAPVEIREKLAFSEEELEEALEELKAQPGVDEAVILSTCNRTEIYAVADDPHAGLEALIEFLAEYHGLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  81 EDDLRNSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTETDIGA 160
Cdd:COG0373   81 VEELEPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYELAREAGTTGPVLNRLFQKAFSVAKRVRTETGIGE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 161 SAVSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGAEVISLSDIDARL 240
Cdd:COG0373  161 GAVSVSSAAVELAKKIFGDLSGKTVLVIGAGEMGELAARHLAAKGVKRITVANRTLERAEELAEEFGGEAVPLEELPEAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 241 QDADIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLAQRQAAAVE 320
Cdd:COG0373  241 AEADIVISSTGAPHPVITKEMVERALKKRRHRPLFLIDLAVPRDIEPEVGELPGVYLYDIDDLQEVVDENLEERQAAAPK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 321 AETIVEQEASEFMAWLRAQGASETIREYRSQSEQIRDELTTKALSALQ-QGGDAQAILQDLAWKLTNRLIHAPTKSLQQA 399
Cdd:COG0373  321 AEAIIEEEVEEFLEWLKSREVVPTIRALREKAEAIREEELERALKKLPdLGEDEREVLEKLTRSLVNKLLHAPTVRLKEA 400
                        410       420
                 ....*....|....*....|
gi 446095353 400 ARDGDDER-LNILRDSLGLE 418
Cdd:COG0373  401 AAEGEDDEyLEALRRLFDLE 420
hemA TIGR01035
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ...
3-418 0e+00

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: 534.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353    3 LLALGINHKTAPVSLRERVTFSPDTLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNLNED 82
Cdd:TIGR01035   1 ILVLGVSHKSAPVEVREKLSIDEIKLKKALDTLKAEPSIEEAMVLSTCNRVEIYAVVDNLHEGKSALLQILAENKNMSNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353   83 DLRNSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTETDIGASA 162
Cdd:TIGR01035  81 DLEKYLYILTGESAVEHLFRVASGLDSMVVGETQILGQVKNAYKVAQEEKTVGKVLERLFQKAFSVGKRVRTETDISAGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  163 VSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGAEVISLSDIDARLQD 242
Cdd:TIGR01035 161 VSISSAAVELAERIFGSLKGKKALLIGAGEMGELVAKHLLRKGVGKILIANRTYERAEDLAKELGGEAVKFEDLEEYLAE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  243 ADIIISSTASPLPIIGKGMVERALKsRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLAQRQAAAVEAE 322
Cdd:TIGR01035 241 ADIVISSTGAPHPIVSKEDVERALR-ERTRPLFIIDIAVPRDVDPAVARLEGVFLYDVDDLQPVVEENLAERREEAEKAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  323 TIVEQEASEFMAWLRAQGASETIREYRSQSEQIRDELTTKALSALQQG-GDAQAILQDLAWKLTNRLIHAPTKSLQQAAR 401
Cdd:TIGR01035 320 EIVEEETAEFKQWLRSLEVEPTIKALRSLAEIVREKELEKALKKLPGLsKDVEEVLEDLARKLINKLLHAPTVRLKQLAD 399
                         410
                  ....*....|....*...
gi 446095353  402 DGD-DERLNILRDSLGLE 418
Cdd:TIGR01035 400 KEEsEVCLEALKNLFGLE 417
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
3-318 1.02e-122

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: 358.12  E-value: 1.02e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353   3 LLALGINHKTAPVSLRERVTFSPDTLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLcdYHNLNED 82
Cdd:cd05213    1 ILVIGLSHKTAPVELREKLAFSEEELKEALRRLLEKPGISEAVLLSTCNRVELYLVGDNFHKLADELEELL--AELLNEP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  83 DLRNSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTETDIGASA 162
Cdd:cd05213   79 ELREYLYVGRGQDAVRHLFRVASGLDSMVVGETQILGQVKNAYKLAKEAGTSGKLLNRLFQKAIKVGKRVRTETGISRGA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 163 VSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGAEVISLSDIDARLQD 242
Cdd:cd05213  159 VSISSAAVELAEKIFGNLKGKKVLVIGAGEMGELAAKHLAAKGVAEITIANRTYERAEELAKELGGNAVPLDELLELLNE 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446095353 243 ADIIISSTASPLPIIgkgMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLAQRQAAA 318
Cdd:cd05213  239 ADVVISATGAPHYAK---IVERAMKKRSGKPRLIVDLAVPRDIEPEVGELEGVRLYTIDDLEEVVEENLERREKEA 311
GlutR_N pfam05201
Glutamyl-tRNAGlu reductase, N-terminal domain;
9-156 1.36e-66

Glutamyl-tRNAGlu reductase, N-terminal domain;


Pssm-ID: 461585  Cd Length: 144  Bit Score: 208.51  E-value: 1.36e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353    9 NHKTAPVSLRERVTFSPDTLDQALDSLLAQPmvqGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNlNEDDLRNSL 88
Cdd:pfam05201   1 NHKTAPVEIREKLAFSEEELEEALQELRGID---EAVILSTCNRTEIYAVADDFHAALEAVIEFLAEHSG-DLEELRPYL 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446095353   89 YWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTET 156
Cdd:pfam05201  77 YVYEGEEAVRHLFRVASGLDSMVLGEDQILGQVKDAYELAREAGTTGPVLNRLFQKAITVAKRVRTET 144
 
Name Accession Description Interval E-value
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
1-418 0e+00

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 602.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353   1 MTLLALGINHKTAPVSLRERVTFSPDTLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNLN 80
Cdd:PRK00045   1 MSLLAVGLNHKTAPVELREKLAFSEDELEEALESLLASPSVLEAVILSTCNRTEIYAVVDQFHAGREAIIRWLAEYHGLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  81 EDDLRNSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTETDIGA 160
Cdd:PRK00045  81 LEELRPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYALAQEAGTVGTILNRLFQKAFSVAKRVRTETGIGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 161 SAVSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGAEVISLSDIDARL 240
Cdd:PRK00045 161 GAVSVASAAVELAKQIFGDLSGKKVLVIGAGEMGELVAKHLAEKGVRKITVANRTLERAEELAEEFGGEAIPLDELPEAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 241 QDADIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLAQRQAAAVE 320
Cdd:PRK00045 241 AEADIVISSTGAPHPIIGKGMVERALKARRHRPLLLVDLAVPRDIEPEVGELPGVYLYDVDDLQEIVEENLAQRQEAAEK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 321 AETIVEQEASEFMAWLRAQGASETIREYRSQSEQIRDELTTKALSALQQGGDAQAILQDLAWKLTNRLIHAPTKSLQQAA 400
Cdd:PRK00045 321 AEAIVEEEVAEFMEWLRSLEVVPTIRALREQAEEIREEELERALKKLGPGEDEEEVLEKLARSLVNKLLHAPTVRLKEAA 400
                        410
                 ....*....|....*...
gi 446095353 401 RDGDDERLNILRDSLGLE 418
Cdd:PRK00045 401 EEGDDEYLEALRELFGLD 418
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
1-418 0e+00

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: 582.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353   1 MTLLALGINHKTAPVSLRERVTFSPDTLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNLN 80
Cdd:COG0373    1 MSLLVVGLNHKTAPVEIREKLAFSEEELEEALEELKAQPGVDEAVILSTCNRTEIYAVADDPHAGLEALIEFLAEYHGLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  81 EDDLRNSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTETDIGA 160
Cdd:COG0373   81 VEELEPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYELAREAGTTGPVLNRLFQKAFSVAKRVRTETGIGE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 161 SAVSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGAEVISLSDIDARL 240
Cdd:COG0373  161 GAVSVSSAAVELAKKIFGDLSGKTVLVIGAGEMGELAARHLAAKGVKRITVANRTLERAEELAEEFGGEAVPLEELPEAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 241 QDADIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLAQRQAAAVE 320
Cdd:COG0373  241 AEADIVISSTGAPHPVITKEMVERALKKRRHRPLFLIDLAVPRDIEPEVGELPGVYLYDIDDLQEVVDENLEERQAAAPK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 321 AETIVEQEASEFMAWLRAQGASETIREYRSQSEQIRDELTTKALSALQ-QGGDAQAILQDLAWKLTNRLIHAPTKSLQQA 399
Cdd:COG0373  321 AEAIIEEEVEEFLEWLKSREVVPTIRALREKAEAIREEELERALKKLPdLGEDEREVLEKLTRSLVNKLLHAPTVRLKEA 400
                        410       420
                 ....*....|....*....|
gi 446095353 400 ARDGDDER-LNILRDSLGLE 418
Cdd:COG0373  401 AAEGEDDEyLEALRRLFDLE 420
hemA TIGR01035
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ...
3-418 0e+00

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: 534.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353    3 LLALGINHKTAPVSLRERVTFSPDTLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNLNED 82
Cdd:TIGR01035   1 ILVLGVSHKSAPVEVREKLSIDEIKLKKALDTLKAEPSIEEAMVLSTCNRVEIYAVVDNLHEGKSALLQILAENKNMSNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353   83 DLRNSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTETDIGASA 162
Cdd:TIGR01035  81 DLEKYLYILTGESAVEHLFRVASGLDSMVVGETQILGQVKNAYKVAQEEKTVGKVLERLFQKAFSVGKRVRTETDISAGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  163 VSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGAEVISLSDIDARLQD 242
Cdd:TIGR01035 161 VSISSAAVELAERIFGSLKGKKALLIGAGEMGELVAKHLLRKGVGKILIANRTYERAEDLAKELGGEAVKFEDLEEYLAE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  243 ADIIISSTASPLPIIGKGMVERALKsRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLAQRQAAAVEAE 322
Cdd:TIGR01035 241 ADIVISSTGAPHPIVSKEDVERALR-ERTRPLFIIDIAVPRDVDPAVARLEGVFLYDVDDLQPVVEENLAERREEAEKAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  323 TIVEQEASEFMAWLRAQGASETIREYRSQSEQIRDELTTKALSALQQG-GDAQAILQDLAWKLTNRLIHAPTKSLQQAAR 401
Cdd:TIGR01035 320 EIVEEETAEFKQWLRSLEVEPTIKALRSLAEIVREKELEKALKKLPGLsKDVEEVLEDLARKLINKLLHAPTVRLKQLAD 399
                         410
                  ....*....|....*...
gi 446095353  402 DGD-DERLNILRDSLGLE 418
Cdd:TIGR01035 400 KEEsEVCLEALKNLFGLE 417
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
3-318 1.02e-122

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: 358.12  E-value: 1.02e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353   3 LLALGINHKTAPVSLRERVTFSPDTLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLcdYHNLNED 82
Cdd:cd05213    1 ILVIGLSHKTAPVELREKLAFSEEELKEALRRLLEKPGISEAVLLSTCNRVELYLVGDNFHKLADELEELL--AELLNEP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  83 DLRNSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTETDIGASA 162
Cdd:cd05213   79 ELREYLYVGRGQDAVRHLFRVASGLDSMVVGETQILGQVKNAYKLAKEAGTSGKLLNRLFQKAIKVGKRVRTETGISRGA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 163 VSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGAEVISLSDIDARLQD 242
Cdd:cd05213  159 VSISSAAVELAEKIFGNLKGKKVLVIGAGEMGELAAKHLAAKGVAEITIANRTYERAEELAKELGGNAVPLDELLELLNE 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446095353 243 ADIIISSTASPLPIIgkgMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLAQRQAAA 318
Cdd:cd05213  239 ADVVISATGAPHYAK---IVERAMKKRSGKPRLIVDLAVPRDIEPEVGELEGVRLYTIDDLEEVVEENLERREKEA 311
PLN00203 PLN00203
glutamyl-tRNA reductase
2-407 4.37e-79

glutamyl-tRNA reductase


Pssm-ID: 215101 [Multi-domain]  Cd Length: 519  Bit Score: 253.52  E-value: 4.37e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353   2 TLLALGINHKTAPVSLRERVTFSPDTLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNLNE 81
Cdd:PLN00203  84 SIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCSLNHIEEAAVLSTCNRMEIYVVALSWHRGVKEVTEWMSKTSGIPV 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  82 DDLRNSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTETDI--G 159
Cdd:PLN00203 164 SELRQHLFLLYDKDATQHLFEVSGGLDSLVLGEGQILAQVKQVVKVGQGVDGFGRNLSGLFKHAITAGKRVRTETNIasG 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 160 ASAVSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEV-GAEVI--SLSDI 236
Cdd:PLN00203 244 AVSVSSAAVELALMKLPESSHASARVLVIGAGKMGKLLVKHLVSKGCTKMVVVNRSEERVAALREEFpDVEIIykPLDEM 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 237 DARLQDADIIISSTASPLPIIGKGMVER--ALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLAQR 314
Cdd:PLN00203 324 LACAAEADVVFTSTSSETPLFLKEHVEAlpPASDTVGGKRLFVDISVPRNVGACVSELESARVYNVDDLKEVVAANKEDR 403
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 315 QAAAVEAETIVEQEASEFMAWLRAQGASETIREYRSQSEQIRDELTTKALSALQQGGDAQ--AILQDLAWKLTNRLIHAP 392
Cdd:PLN00203 404 LRKAMEAQTIIREESKNFEAWRDSLETVPTIKKLRSYAERIRAAELEKCLSKMGDDLTKKqrKAVEDLSRGIVNKLLHGP 483
                        410
                 ....*....|....*
gi 446095353 393 TKSLQqaaRDGDDER 407
Cdd:PLN00203 484 MQHLR---CDGSDSR 495
GlutR_N pfam05201
Glutamyl-tRNAGlu reductase, N-terminal domain;
9-156 1.36e-66

Glutamyl-tRNAGlu reductase, N-terminal domain;


Pssm-ID: 461585  Cd Length: 144  Bit Score: 208.51  E-value: 1.36e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353    9 NHKTAPVSLRERVTFSPDTLDQALDSLLAQPmvqGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNlNEDDLRNSL 88
Cdd:pfam05201   1 NHKTAPVEIREKLAFSEEELEEALQELRGID---EAVILSTCNRTEIYAVADDFHAALEAVIEFLAEHSG-DLEELRPYL 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446095353   89 YWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTET 156
Cdd:pfam05201  77 YVYEGEEAVRHLFRVASGLDSMVLGEDQILGQVKDAYELAREAGTTGPVLNRLFQKAITVAKRVRTET 144
PRK13940 PRK13940
glutamyl-tRNA reductase; Provisional
1-417 2.57e-66

glutamyl-tRNA reductase; Provisional


Pssm-ID: 172450 [Multi-domain]  Cd Length: 414  Bit Score: 217.19  E-value: 2.57e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353   1 MTLLALGINHKTAPVSLRERVTFSPDTLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNLN 80
Cdd:PRK13940   1 MALISLAIDYKKSPIEVRSEFALSGLDVSMLYRSILAIDNVVHAVILSTCNRTEVYLEISDLRVVDDILVWWQGYVRNPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  81 EDdLRNSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTETDIGA 160
Cdd:PRK13940  81 YK-IKDYFKLRQGTEVIMHLMKLACGLESMVLGEPQILGQVKDSYTLSKKNHAIGKELDRVFQKVFATAKRVRSETRIGH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 161 SAVSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEV-GAEVISLSDIDAR 239
Cdd:PRK13940 160 CPVSVAFSAITLAKRQLDNISSKNVLIIGAGQTGELLFRHVTALAPKQIMLANRTIEKAQKITSAFrNASAHYLSELPQL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 240 LQDADIIISSTASPLPIIgkgmverALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLAQRQAAAV 319
Cdd:PRK13940 240 IKKADIIIAAVNVLEYIV-------TCKYVGDKPRVFIDISIPQALDPKLGELEQNVYYCVDDINAVIEDNKDKRKYESS 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 320 EAETIVEQEASEFMAWLRAQGASETIREYRSQSEQIRDELTTKALSALQQGGDAQAILQDLAWKLTNRLIHAPTKSLQQA 399
Cdd:PRK13940 313 KAQKIIVKSLEEYLEKEKAIISNSAIKELFQKADGLVDLSLEKSLAKIRNGKDAEEIIKRFAYEIKKKVLHYPVVGMKEA 392
                        410
                 ....*....|....*...
gi 446095353 400 ARDGDDERLNILRDSLGL 417
Cdd:PRK13940 393 SKQGRSDCLVCMKRMFGL 410
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
172-306 2.59e-61

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: 194.71  E-value: 2.59e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  172 LARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGA-EVISLSDIDARLQDADIIISST 250
Cdd:pfam01488   2 LAKKIFGDLKDKKVLLIGAGEMGELVAKHLLAKGAKEVTIANRTIERAQELAEKFGGvEALPLDDLKEYLAEADIVISAT 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446095353  251 ASPLPIIGKGMVERALKsRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSI 306
Cdd:pfam01488  82 SSPTPIITKEMVERALK-PRKKPLLFVDIAVPRDIEPEVGELEGVYLYTVDDLKEV 136
GlutR_dimer pfam00745
Glutamyl-tRNAGlu reductase, dimerization domain;
320-413 4.65e-25

Glutamyl-tRNAGlu reductase, dimerization domain;


Pssm-ID: 459922 [Multi-domain]  Cd Length: 95  Bit Score: 98.03  E-value: 4.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  320 EAETIVEQEASEFMAWLRAQGASETIREYRSQSEQIRDELTTKALSALQQGGDAQAILQDLAWKLTNRLIHAPTKSLQQA 399
Cdd:pfam00745   1 KAEAIIEEEVEEFMAWLKSLEVVPTIRALREKAEEIREEELERALKKLGLDGEDREELEKLTRSLVNKLLHDPTVRLKEA 80
                          90
                  ....*....|....
gi 446095353  400 ARDGDDERLNILRD 413
Cdd:pfam00745  81 EEGDGDEYLEALRR 94
hemA PRK00676
glutamyl-tRNA reductase; Validated
1-155 8.48e-21

glutamyl-tRNA reductase; Validated


Pssm-ID: 234810 [Multi-domain]  Cd Length: 338  Bit Score: 92.62  E-value: 8.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353   1 MTLLALGINHKTAPVSLRERVTfspDTLDQA-LDSLLAQPMVQGG---VVLSTCNRTELYLSVEEQDNLQEALIRWLcdy 76
Cdd:PRK00676   1 MVLGVVGISYREAALKEREQVI---QILQQFeGSLFFRQRFFGEEgdfVLLLTCHRAELYYYSVSPAELQSSLLSEI--- 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446095353  77 hnlneDDLRNSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLNASALERMFQKSFSVAKRVRTE 155
Cdd:PRK00676  75 -----TSLGVRPYFYRGLDCFTHLFCVTSGMDSLILGETEIQGQVKRAYLKAARERKLPFALHFLFQKALKEGKVFRSK 148
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
184-262 9.69e-13

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


Pssm-ID: 439939 [Multi-domain]  Cd Length: 270  Bit Score: 67.86  E-value: 9.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 184 TVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGAEVISLSDIDARLQDADIIISST--------ASPLP 255
Cdd:COG0169  123 RVLVLGAGGAARAVAAALAEAGAAEITIVNRTPERAEALAARLGVRAVPLDDLAAALAGADLVINATplgmaggdALPLP 202

                 ....*....
gi 446095353 256 --IIGKGMV 262
Cdd:COG0169  203 asLLAPGAV 211
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
184-250 1.39e-10

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: 59.21  E-value: 1.39e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446095353 184 TVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVG--AEVISLSDIDARLQDADIIISST 250
Cdd:cd01065   21 KVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGelGIAIAYLDLEELLAEADLIINTT 89
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
173-291 2.37e-09

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 58.70  E-value: 2.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 173 ARQIFESLSTVTVLLVGAGETIELV-ARHLREhKVQKMIIANRTRERAQALADEV----GAEVISLSDIDARLQDADIII 247
Cdd:COG5322  142 AERMGIDLKKATVAVVGATGSIGSVcARLLAR-EVKRLTLVARNLERLEELAEEIlrnpGGKVTITTDIDEALREADIVV 220
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446095353 248 SSTASPLPIIGKGMveraLKsrrnQPMLLVDIAVPRDVEPEVGK 291
Cdd:COG5322  221 TVTSAVGAIIDPED----LK----PGAVVCDVARPRDVSRRVAE 256
aroE PRK00258
shikimate 5-dehydrogenase; Reviewed
172-252 2.15e-08

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 234703 [Multi-domain]  Cd Length: 278  Bit Score: 55.19  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 172 LARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGAEVISLSDIDAR--LQDADIIISS 249
Cdd:PRK00258 113 LEERLGVDLKGKRILILGAGGAARAVILPLLDLGVAEITIVNRTVERAEELAKLFGALGKAELDLELQeeLADFDLIINA 192

                 ...
gi 446095353 250 TAS 252
Cdd:PRK00258 193 TSA 195
OCDMu COG2423
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid ...
184-262 9.49e-08

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


Pssm-ID: 441972 [Multi-domain]  Cd Length: 322  Bit Score: 53.22  E-value: 9.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 184 TVLLVGAGETIELVARHLRE-HKVQKMIIANRTRERAQALADEV---GAEVISLSDIDARLQDADIIISSTASPLPIIGK 259
Cdd:COG2423  129 TLGIIGAGVQARTQLRALAAvRPIERVRVWGRDPEKAEAFAARLaaeGLPVEAADDLEEAVADADIIVTATPSREPVLRG 208

                 ...
gi 446095353 260 GMV 262
Cdd:COG2423  209 EWL 211
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
188-282 8.35e-06

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 44.14  E-value: 8.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  188 VGAGETIELVARHLREHKVQKMIIAN-RTRERAQALADEVGAEVISLSDIDArLQDADIIIssTASPLPiigkgMVERAL 266
Cdd:pfam03807   3 IGAGNMGEALARGLVAAGPHEVVVANsRNPEKAEELAEEYGVGATAVDNEEA-AEEADVVF--LAVKPE-----DAPDVL 74
                          90
                  ....*....|....*...
gi 446095353  267 KSRRN--QPMLLVDIAVP 282
Cdd:pfam03807  75 SELSDllKGKIVISIAAG 92
PLN02520 PLN02520
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
180-252 4.01e-05

bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase


Pssm-ID: 178135 [Multi-domain]  Cd Length: 529  Bit Score: 45.91  E-value: 4.01e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446095353 180 LSTVTVLLVGAGETIELVARHLREhKVQKMIIANRTRERAQALADEVGAEVISLSDIDARLQDADIIISSTAS 252
Cdd:PLN02520 377 LAGKLFVVIGAGGAGKALAYGAKE-KGARVVIANRTYERAKELADAVGGQALTLADLENFHPEEGMILANTTS 448
PRK08291 PRK08291
cyclodeaminase;
172-257 5.39e-05

cyclodeaminase;


Pssm-ID: 236221 [Multi-domain]  Cd Length: 330  Bit Score: 44.95  E-value: 5.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 172 LARqifESLSTVTVLlvGAGETIELVARHLR-EHKVQKMIIANRTRERAQALADEV----GAEVISLSDIDARLQDADII 246
Cdd:PRK08291 127 LAR---EDASRAAVI--GAGEQARLQLEALTlVRPIREVRVWARDAAKAEAYAADLraelGIPVTVARDVHEAVAGADII 201
                         90
                 ....*....|.
gi 446095353 247 ISSTASPLPII 257
Cdd:PRK08291 202 VTTTPSEEPIL 212
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
185-284 1.05e-04

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 41.42  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353  185 VLLVGAG----ETIELVARHlreHKVQKMIIANRTRERAQALADEVG-----AEVISLSDIDARL----QDADIIISstA 251
Cdd:pfam03435   1 VLIIGAGsvgqGVAPLLARH---FDVDRITVADRTLEKAQALAAKLGgvrfiAVAVDADNYEAVLaallKEGDLVVN--L 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 446095353  252 SPlPIIGKGMVERALKSRrnqpMLLVDIAVPRD 284
Cdd:pfam03435  76 SP-PTLSLDVLKACIETG----VHYVDTSYLRE 103
PRK08618 PRK08618
ornithine cyclodeaminase family protein;
184-256 2.09e-03

ornithine cyclodeaminase family protein;


Pssm-ID: 236313 [Multi-domain]  Cd Length: 325  Bit Score: 40.04  E-value: 2.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446095353 184 TVLLVGAGETIE-LVARHLREHKVQKMIIANRTRERAQALADEV----GAEVISLSDIDARLQDADIIISSTASPLPI 256
Cdd:PRK08618 129 TLCLIGTGGQAKgQLEAVLAVRDIERVRVYSRTFEKAYAFAQEIqskfNTEIYVVNSADEAIEEADIIVTVTNAKTPV 206
PRK07340 PRK07340
delta(1)-pyrroline-2-carboxylate reductase family protein;
172-256 4.56e-03

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


Pssm-ID: 235996  Cd Length: 304  Bit Score: 38.79  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 172 LARQIFESLSTVTVLLVGAGETielvARHLRE-----HKVQKMIIANRTRERAQALADEVGAEVISLS--DIDARLQDAD 244
Cdd:PRK07340 115 LAARTLAPAPPGDLLLIGTGVQ----ARAHLEafaagLPVRRVWVRGRTAASAAAFCAHARALGPTAEplDGEAIPEAVD 190
                         90
                 ....*....|..
gi 446095353 245 IIISSTASPLPI 256
Cdd:PRK07340 191 LVVTATTSRTPV 202
PRK14027 PRK14027
quinate/shikimate dehydrogenase (NAD+);
184-255 4.57e-03

quinate/shikimate dehydrogenase (NAD+);


Pssm-ID: 172521 [Multi-domain]  Cd Length: 283  Bit Score: 38.87  E-value: 4.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446095353 184 TVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGAEV--ISLSDIDAR-----LQDADIIISSTASPLP 255
Cdd:PRK14027 129 SVVQVGAGGVGNAVAYALVTHGVQKLQVADLDTSRAQALADVINNAVgrEAVVGVDARgiedvIAAADGVVNATPMGMP 207
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
173-280 8.70e-03

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


Pssm-ID: 240643 [Multi-domain]  Cd Length: 300  Bit Score: 37.95  E-value: 8.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446095353 173 ARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTREraqaladevGAEVISLSDIDARLQDADIIISSTas 252
Cdd:cd12166  123 EPRRTPSLADRRVLIVGYGSIGRAIERRLAPFEVRVTRVARTARP---------GEQVHGIDELPALLPEADVVVLIV-- 191
                         90       100
                 ....*....|....*....|....*...
gi 446095353 253 PLPIIGKGMVERALKSRRNQPMLLVDIA 280
Cdd:cd12166  192 PLTDETRGLVDAEFLARMPDGALLVNVA 219
 
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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