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Conserved domains on  [gi|641744506|gb|AIA69977|]
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N-acetylglutamate synthase [Pectobacterium atrosepticum]

Protein Classification

N-acetylglutamate synthase( domain architecture ID 11480526)

N-acetylglutamate synthase catalyzes the production of N-acetylglutamate (NAG) from glutamate and acetyl-CoA in the first committed step of l-arginine biosynthesis in plants and micro-organisms

EC:  2.3.1.1
Gene Ontology:  GO:0006526|GO:0103045|GO:0004042|GO:0005737
PubMed:  19095660|12633501

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 1-441 0e+00

N-acetylglutamate synthase; Validated


:

Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 886.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506   1 MKERSTELVQGFRHSVPYINAHRGKTFVIMLGGEAIEHANFSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPH 80
Cdd:PRK05279   2 MKERSTEFVDWFRHSAPYINAHRGKTFVIMLGGEAIAHGNFSNIVHDIALLHSLGIRLVLVHGARPQIEEQLAARGIEPR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  81 YHKNTRITDSATLELVKQAAGMLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEEAV 160
Cdd:PRK05279  82 YHKGLRVTDAAALECVKQAAGELRLDIEARLSMGLPNTPMAGAHIRVVSGNFVTARPLGVDDGVDYQHTGEVRRIDAEAI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 161 HRQLNSGAIVLLGPVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGVTNEEGRIISELFPDDAQQRIDVLEQaG 240
Cdd:PRK05279 162 RRQLDSGAIVLLSPLGYSPTGESFNLTMEEVATQVAIALKADKLIFFTESQGVLDEDGELIRELSPNEAQALLEALED-G 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 241 DYHSGTVRFLRGAVKACRSGVRRSHLISYQDDGALLQELFSRDGIGTQIVMESAEQVRRATINDIGGILELIRPLEEQGI 320
Cdd:PRK05279 241 DYNSGTARFLRAAVKACRGGVRRSHLISYAEDGALLQELFTRDGIGTMIVMESLEQLRRATIDDVGGILELIRPLEEQGI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 321 LVRRSREQLEMEIDKFTVVVRDNLTIACAALYPFPEESIGEMACVAVHPDYRSSSRGDMLLMRVAAQARQQGLQKLFVLT 400
Cdd:PRK05279 321 LVRRSREQLEREIDKFTVIERDGLIIGCAALYPFPEEKMGEMACLAVHPDYRGSGRGERLLKRIEQRARQLGLKRLFVLT 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 641744506 401 THSIHWFQERGFLPAEVEMLPKKKQALYNYQRRSKILVLDL 441
Cdd:PRK05279 401 TRTAHWFLERGFVPVDVDDLPEAKRQLYNYQRRSKVLVKDL 441
 
Name Accession Description Interval E-value
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 1-441 0e+00

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 886.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506   1 MKERSTELVQGFRHSVPYINAHRGKTFVIMLGGEAIEHANFSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPH 80
Cdd:PRK05279   2 MKERSTEFVDWFRHSAPYINAHRGKTFVIMLGGEAIAHGNFSNIVHDIALLHSLGIRLVLVHGARPQIEEQLAARGIEPR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  81 YHKNTRITDSATLELVKQAAGMLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEEAV 160
Cdd:PRK05279  82 YHKGLRVTDAAALECVKQAAGELRLDIEARLSMGLPNTPMAGAHIRVVSGNFVTARPLGVDDGVDYQHTGEVRRIDAEAI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 161 HRQLNSGAIVLLGPVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGVTNEEGRIISELFPDDAQQRIDVLEQaG 240
Cdd:PRK05279 162 RRQLDSGAIVLLSPLGYSPTGESFNLTMEEVATQVAIALKADKLIFFTESQGVLDEDGELIRELSPNEAQALLEALED-G 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 241 DYHSGTVRFLRGAVKACRSGVRRSHLISYQDDGALLQELFSRDGIGTQIVMESAEQVRRATINDIGGILELIRPLEEQGI 320
Cdd:PRK05279 241 DYNSGTARFLRAAVKACRGGVRRSHLISYAEDGALLQELFTRDGIGTMIVMESLEQLRRATIDDVGGILELIRPLEEQGI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 321 LVRRSREQLEMEIDKFTVVVRDNLTIACAALYPFPEESIGEMACVAVHPDYRSSSRGDMLLMRVAAQARQQGLQKLFVLT 400
Cdd:PRK05279 321 LVRRSREQLEREIDKFTVIERDGLIIGCAALYPFPEEKMGEMACLAVHPDYRGSGRGERLLKRIEQRARQLGLKRLFVLT 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 641744506 401 THSIHWFQERGFLPAEVEMLPKKKQALYNYQRRSKILVLDL 441
Cdd:PRK05279 401 TRTAHWFLERGFVPVDVDDLPEAKRQLYNYQRRSKVLVKDL 441
N-Ac-Glu-synth TIGR01890
amino-acid N-acetyltransferase; This model represents a clade of amino-acid ...
 8-441 0e+00

amino-acid N-acetyltransferase; This model represents a clade of amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the "acetylated" ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273856 [Multi-domain]  Cd Length: 429  Bit Score: 624.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506    8 LVQGFRHSVPYINAHRGKTFVIMLGGEAIEHANFSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHKNTRI 87
Cdd:TIGR01890   1 FVAWFREAAPYINAHRGKTFVVGLGGELVEGGNLGNIVADIALLHSLGVRLVLVHGARPQIERILAARGRTPHYHRGLRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506   88 TDSATLELVKQAAGMLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEEAVHRQLNSG 167
Cdd:TIGR01890  81 TDEASLEQAQQAAGTLRLAIEARLSMSLSNTPMAGSRLPVVSGNFVTARPIGVIEGVDYEHTGVIRKIDTEGIRRQLDAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  168 AIVLLGPVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGVTNEEGRIISELFPDDAQQRIDVLEQagdyhSGTV 247
Cdd:TIGR01890 161 SIVLLSPLGHSPTGETFNLDMEDVATSVAISLKADKLIYFTLSPGISDPDGTLAAELSPQEVESLAERLGS-----ETTR 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  248 RFLRGAVKACRSGVRRSHLISYQDDGALLQELFSRDGIGTQIVMESAEQVRRATINDIGGILELIRPLEEQGILVRRSRE 327
Cdd:TIGR01890 236 RLLSAAVKACRGGVHRSHIVSYAEDGSLLQELFTRDGIGTSISKEAFESIRQATIDDIGGIAALIRPLEEQGILVRRSRE 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  328 QLEMEIDKFTVVVRDNLTIACAALYPFPEESIGEMACVAVHPDYRSSSRGDMLLMRVAAQARQQGLQKLFVLTTHSIHWF 407
Cdd:TIGR01890 316 YLEREISEFSIIEHDGNIIGCAALYPYAEEDCGEMACLAVSPEYQDGGRGERLLAHIEDRARQMGISRLFVLTTRTGHWF 395

                         410       420       430
                  ....*....|....*....|....*....|....
gi 641744506  408 QERGFLPAEVEMLPKKKQALYNYQRRSKILVLDL 441
Cdd:TIGR01890 396 RERGFQTASVDELPEARRKLYNYQRNSKILMKRL 429
AAK_NAGS-ABP cd04237
AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 7-289 2.11e-163

AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the arginine-biosynthesis pathway (ABP) found in gamma- and beta-proteobacteria and higher plant chloroplasts. Domain architecture of these NAGS consisted of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal NAG synthase, acetyltransferase (ArgA) domain. Both bacterial and plant sequences in this CD have a conserved N-terminal extension; a similar sequence in the NAG kinases of the cyclic arginine-biosynthesis pathway has been implicated in feedback inhibition sensing. Plant sequences also have an N-terminal chloroplast transit peptide and an insert (approx. 70 residues) in the C-terminal region of ArgB. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239770 [Multi-domain]  Cd Length: 280  Bit Score: 461.25  E-value: 2.11e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506   7 ELVQGFRHSVPYINAHRGKTFVIMLGGEAIEHANFSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHKNTR 86
Cdd:cd04237    1 QFVDWFREAAPYINAHRGKTFVIAFGGEAVAHPNFDNIVHDIALLHSLGIRLVLVHGARPQIDQRLAERGLEPRYHRGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  87 ITDSATLELVKQAAGMLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEEAVHRQLNS 166
Cdd:cd04237   81 ITDAAALECVKEAAGAVRLEIEALLSMGLPNSPMAGARIRVVSGNFVTARPLGVVDGVDFGHTGEVRRIDADAIRRQLDQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 167 GAIVLLGPVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGVTNEEGRIISELFPDDAQQRidvLEQAGDYHSGT 246
Cdd:cd04237  161 GSIVLLSPLGYSPTGEVFNLSMEDVATAVAIALKADKLIFLTDGPGLLDDDGELIRELTAQEAEAL---LETGALLTNDT 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 641744506 247 VRFLRGAVKACRSGVRRSHLISYQDDGALLQELFSRDGIGTQI 289
Cdd:cd04237  238 ARLLQAAIEACRGGVPRVHLISYAEDGALLLELFTRDGVGTLI 280
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 3-290 2.38e-132

N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440314 [Multi-domain]  Cd Length: 283  Bit Score: 382.46  E-value: 2.38e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506   3 ERSTELVQGFRHSVPYINAHRGKTFVIMLGGEAIEHANF-SSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHY 81
Cdd:COG0548    2 ESAIEKAEWLREALPYIQAFRGKTFVIKYGGEAMEDEELkAALAQDIALLKSLGIRPVLVHGGGPQINELLKRLGIESEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  82 HKNTRITDSATLELVKQA-AGMLQLDITARLSMSLNNtplqGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEEAV 160
Cdd:COG0548   82 VNGLRVTDEETLEVVEMVlAGKVNKEIVALLSQGGGN----AVGLSGKDGNLITARPLGVGDGVDLGHVGEVRRVDPELI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 161 HRQLNSGAIVLLGPVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGVTNEEGRIISELFPDDAQQRIDvleqAG 240
Cdd:COG0548  158 RALLDAGYIPVISPIGYSPTGEVYNINADTVAGAIAAALKAEKLILLTDVPGVLDDPGSLISELTAAEAEELIA----DG 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 641744506 241 DYHSGTVRFLRGAVKACRSGVRRSHLISYQDDGALLQELFSRDGIGTQIV 290
Cdd:COG0548  234 VISGGMIPKLEAALDAVRGGVKRVHIIDGRVPHALLLELFTDDGIGTMIV 283
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 25-268 1.29e-32

Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.


Pssm-ID: 395565 [Multi-domain]  Cd Length: 232  Bit Score: 123.25  E-value: 1.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506   25 KTFVIMLGGEAIEHAN-FSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHkntRITDSATLELVK-QAAGM 102
Cdd:pfam00696   1 KRVVIKLGGSSLTDKErLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFA---RLTDAETLEVATmDALGS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  103 LQLDITARL-SMSLNNTPLQGAHINVVSGNFIiaqplgvddgvdychSGRIRRIDEEAVHRQLNSGAIVLLGP-VAVSVT 180
Cdd:pfam00696  78 LGERLNAALlAAGLPAVGLPAAQLLATEAGFI---------------DDVVTRIDTEALEELLEAGVVPVITGfIGIDPE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  181 GESFNLTSEEVATQLAIKLKAEKMIGFCSSQGV------TNEEGRIISELFPDDAQQridvLEQAGDYHSGTVRFLRGAV 254
Cdd:pfam00696 143 GELGRGSSDTLAALLAEALGADKLIILTDVDGVytadprKVPDAKLIPEISYDELLE----LLASGLATGGMKVKLPAAL 218

                         250
                  ....*....|....
gi 641744506  255 KACRSGVRRSHLIS 268
Cdd:pfam00696 219 EAARRGGIPVVIVN 232
 
Name Accession Description Interval E-value
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 1-441 0e+00

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 886.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506   1 MKERSTELVQGFRHSVPYINAHRGKTFVIMLGGEAIEHANFSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPH 80
Cdd:PRK05279   2 MKERSTEFVDWFRHSAPYINAHRGKTFVIMLGGEAIAHGNFSNIVHDIALLHSLGIRLVLVHGARPQIEEQLAARGIEPR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  81 YHKNTRITDSATLELVKQAAGMLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEEAV 160
Cdd:PRK05279  82 YHKGLRVTDAAALECVKQAAGELRLDIEARLSMGLPNTPMAGAHIRVVSGNFVTARPLGVDDGVDYQHTGEVRRIDAEAI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 161 HRQLNSGAIVLLGPVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGVTNEEGRIISELFPDDAQQRIDVLEQaG 240
Cdd:PRK05279 162 RRQLDSGAIVLLSPLGYSPTGESFNLTMEEVATQVAIALKADKLIFFTESQGVLDEDGELIRELSPNEAQALLEALED-G 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 241 DYHSGTVRFLRGAVKACRSGVRRSHLISYQDDGALLQELFSRDGIGTQIVMESAEQVRRATINDIGGILELIRPLEEQGI 320
Cdd:PRK05279 241 DYNSGTARFLRAAVKACRGGVRRSHLISYAEDGALLQELFTRDGIGTMIVMESLEQLRRATIDDVGGILELIRPLEEQGI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 321 LVRRSREQLEMEIDKFTVVVRDNLTIACAALYPFPEESIGEMACVAVHPDYRSSSRGDMLLMRVAAQARQQGLQKLFVLT 400
Cdd:PRK05279 321 LVRRSREQLEREIDKFTVIERDGLIIGCAALYPFPEEKMGEMACLAVHPDYRGSGRGERLLKRIEQRARQLGLKRLFVLT 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 641744506 401 THSIHWFQERGFLPAEVEMLPKKKQALYNYQRRSKILVLDL 441
Cdd:PRK05279 401 TRTAHWFLERGFVPVDVDDLPEAKRQLYNYQRRSKVLVKDL 441
N-Ac-Glu-synth TIGR01890
amino-acid N-acetyltransferase; This model represents a clade of amino-acid ...
 8-441 0e+00

amino-acid N-acetyltransferase; This model represents a clade of amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the "acetylated" ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273856 [Multi-domain]  Cd Length: 429  Bit Score: 624.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506    8 LVQGFRHSVPYINAHRGKTFVIMLGGEAIEHANFSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHKNTRI 87
Cdd:TIGR01890   1 FVAWFREAAPYINAHRGKTFVVGLGGELVEGGNLGNIVADIALLHSLGVRLVLVHGARPQIERILAARGRTPHYHRGLRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506   88 TDSATLELVKQAAGMLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEEAVHRQLNSG 167
Cdd:TIGR01890  81 TDEASLEQAQQAAGTLRLAIEARLSMSLSNTPMAGSRLPVVSGNFVTARPIGVIEGVDYEHTGVIRKIDTEGIRRQLDAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  168 AIVLLGPVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGVTNEEGRIISELFPDDAQQRIDVLEQagdyhSGTV 247
Cdd:TIGR01890 161 SIVLLSPLGHSPTGETFNLDMEDVATSVAISLKADKLIYFTLSPGISDPDGTLAAELSPQEVESLAERLGS-----ETTR 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  248 RFLRGAVKACRSGVRRSHLISYQDDGALLQELFSRDGIGTQIVMESAEQVRRATINDIGGILELIRPLEEQGILVRRSRE 327
Cdd:TIGR01890 236 RLLSAAVKACRGGVHRSHIVSYAEDGSLLQELFTRDGIGTSISKEAFESIRQATIDDIGGIAALIRPLEEQGILVRRSRE 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  328 QLEMEIDKFTVVVRDNLTIACAALYPFPEESIGEMACVAVHPDYRSSSRGDMLLMRVAAQARQQGLQKLFVLTTHSIHWF 407
Cdd:TIGR01890 316 YLEREISEFSIIEHDGNIIGCAALYPYAEEDCGEMACLAVSPEYQDGGRGERLLAHIEDRARQMGISRLFVLTTRTGHWF 395

                         410       420       430
                  ....*....|....*....|....*....|....
gi 641744506  408 QERGFLPAEVEMLPKKKQALYNYQRRSKILVLDL 441
Cdd:TIGR01890 396 RERGFQTASVDELPEARRKLYNYQRNSKILMKRL 429
AAK_NAGS-ABP cd04237
AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 7-289 2.11e-163

AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the arginine-biosynthesis pathway (ABP) found in gamma- and beta-proteobacteria and higher plant chloroplasts. Domain architecture of these NAGS consisted of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal NAG synthase, acetyltransferase (ArgA) domain. Both bacterial and plant sequences in this CD have a conserved N-terminal extension; a similar sequence in the NAG kinases of the cyclic arginine-biosynthesis pathway has been implicated in feedback inhibition sensing. Plant sequences also have an N-terminal chloroplast transit peptide and an insert (approx. 70 residues) in the C-terminal region of ArgB. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239770 [Multi-domain]  Cd Length: 280  Bit Score: 461.25  E-value: 2.11e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506   7 ELVQGFRHSVPYINAHRGKTFVIMLGGEAIEHANFSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHKNTR 86
Cdd:cd04237    1 QFVDWFREAAPYINAHRGKTFVIAFGGEAVAHPNFDNIVHDIALLHSLGIRLVLVHGARPQIDQRLAERGLEPRYHRGLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  87 ITDSATLELVKQAAGMLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEEAVHRQLNS 166
Cdd:cd04237   81 ITDAAALECVKEAAGAVRLEIEALLSMGLPNSPMAGARIRVVSGNFVTARPLGVVDGVDFGHTGEVRRIDADAIRRQLDQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 167 GAIVLLGPVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGVTNEEGRIISELFPDDAQQRidvLEQAGDYHSGT 246
Cdd:cd04237  161 GSIVLLSPLGYSPTGEVFNLSMEDVATAVAIALKADKLIFLTDGPGLLDDDGELIRELTAQEAEAL---LETGALLTNDT 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 641744506 247 VRFLRGAVKACRSGVRRSHLISYQDDGALLQELFSRDGIGTQI 289
Cdd:cd04237  238 ARLLQAAIEACRGGVPRVHLISYAEDGALLLELFTRDGVGTLI 280
ArgB COG0548
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ...
 3-290 2.38e-132

N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440314 [Multi-domain]  Cd Length: 283  Bit Score: 382.46  E-value: 2.38e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506   3 ERSTELVQGFRHSVPYINAHRGKTFVIMLGGEAIEHANF-SSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHY 81
Cdd:COG0548    2 ESAIEKAEWLREALPYIQAFRGKTFVIKYGGEAMEDEELkAALAQDIALLKSLGIRPVLVHGGGPQINELLKRLGIESEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  82 HKNTRITDSATLELVKQA-AGMLQLDITARLSMSLNNtplqGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEEAV 160
Cdd:COG0548   82 VNGLRVTDEETLEVVEMVlAGKVNKEIVALLSQGGGN----AVGLSGKDGNLITARPLGVGDGVDLGHVGEVRRVDPELI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 161 HRQLNSGAIVLLGPVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGVTNEEGRIISELFPDDAQQRIDvleqAG 240
Cdd:COG0548  158 RALLDAGYIPVISPIGYSPTGEVYNINADTVAGAIAAALKAEKLILLTDVPGVLDDPGSLISELTAAEAEELIA----DG 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 641744506 241 DYHSGTVRFLRGAVKACRSGVRRSHLISYQDDGALLQELFSRDGIGTQIV 290
Cdd:COG0548  234 VISGGMIPKLEAALDAVRGGVKRVHIIDGRVPHALLLELFTDDGIGTMIV 283
PLN02825 PLN02825
amino-acid N-acetyltransferase
 9-435 1.90e-110

amino-acid N-acetyltransferase


Pssm-ID: 215441 [Multi-domain]  Cd Length: 515  Bit Score: 335.20  E-value: 1.90e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506   9 VQGFRHSVPYINAHRGKTFVIMLGGEAIEHANFSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHKNTRIT 88
Cdd:PLN02825   2 VRWFREAWPYIQGHRGSTFVVVISGEVVAGPHLDNILQDISLLHGLGIKFVLVPGTHVQIDKLLAERGREPKYVGAYRIT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  89 DSATLELVKQAAGMLQLDITARLS---MSLN------NTPLQGAHINVVSGNFIIAQPLGVDDGVDYCHSGRIRRIDEEA 159
Cdd:PLN02825  82 DSAALQASMEAAGKIRVMIEAKLSpgpSIPNlrrhgdNSRWHEVGVSVASGNFLAAKRRGVVNGVDFGATGEVKKIDVSR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 160 VHRQLNSGAIVLLGPVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQgVTNEEGRIISELFPDDA----QQRIDV 235
Cdd:PLN02825 162 IKERLDSNCIVLLSNLGYSSSGEVLNCNTYEVATACALAIGADKLICIVDGP-ILDENGRLIRFMTLEEAdmliRKRAKQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 236 LEQAGDY---------------------------------HSGTVRFLRG------------------------------ 252
Cdd:PLN02825 241 SEIAANYvkavggedysyslgldsvnttpfnnngrgfwgsGSATDSFQNGvgfdngnglsgeqgfaiggeerlsrlngyl 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 253 -----AVKACRSGVRRSHLISYQDDGALLQELFSRDGIGTQIVMESAEQVRRATINDIGGILELIRPLEEQGILVRRSRE 327
Cdd:PLN02825 321 selaaAAFVCRGGVQRVHLLDGTIEGVLLLELFTRDGMGTMIASDMYEGTRMARVEDLAGIRQIIRPLEESGILVRRTDE 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 328 QLEMEIDKFTVVVRDNLTIACAALYPFPEESIGEMACVAVHPDYRSSSRGDMLLMRVAAQARQQGLQKLFVLTTHSIHWF 407
Cdd:PLN02825 401 ELLRALDSFVVVEREGSIIACAALFPFFEEKCGEVAAIAVSPECRGQGQGDKLLDYIEKKAASLGLEKLFLLTTRTADWF 480

                        490       500
                 ....*....|....*....|....*...
gi 641744506 408 QERGFLPAEVEMLPKKKQALYNYQRRSK 435
Cdd:PLN02825 481 VRRGFSECSIESLPEARRKRINLSRGSK 508
PRK00942 PRK00942
acetylglutamate kinase; Provisional
 17-290 2.09e-42

acetylglutamate kinase; Provisional


Pssm-ID: 234869 [Multi-domain]  Cd Length: 283  Bit Score: 151.03  E-value: 2.09e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  17 PYINAHRGKTFVIMLGGEAIEHANFS-SIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHKNTRITDSATLEL 95
Cdd:PRK00942  16 PYIQRFMGKTIVIKYGGNAMTDEELKeAFARDIVLLKQVGINPVVVHGGGPQIDELLKKLGIESEFVNGLRVTDAETMEV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  96 VKQA-AGMLQLDITARLsmslnntplQGAHINVV-----SGNFIIAQPLGVDdgVDYCHSGRIRRIDEEAVHRQLNSGAI 169
Cdd:PRK00942  96 VEMVlAGKVNKELVSLI---------NKHGGKAVglsgkDGGLITAKKLEED--EDLGFVGEVTPVNPALLEALLEAGYI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 170 VLLGPVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGVTNEEGRIISELFPDDAQQRIDvleqAGDYHSGTVRF 249
Cdd:PRK00942 165 PVISPIGVGEDGETYNINADTAAGAIAAALGAEKLILLTDVPGVLDDKGQLISELTASEAEELIE----DGVITGGMIPK 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 641744506 250 LRGAVKACRSGVRRSHLISYQDDGALLQELFSRDGIGTQIV 290
Cdd:PRK00942 241 VEAALDAARGGVRSVHIIDGRVPHALLLELFTDEGIGTMIV 281
AAK_NAGK-C cd04250
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ...
 15-289 9.61e-40

AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of this pathway. In one, typified by the pathway in Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation. NAGK-C are members of the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239783 [Multi-domain]  Cd Length: 279  Bit Score: 143.80  E-value: 9.61e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  15 SVPYINAHRGKTFVIMLGGEAIEHAN-FSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHKNTRITDSATL 93
Cdd:cd04250    5 ALPYIQKFRGKTVVIKYGGNAMKDEElKESFARDIVLLKYVGINPVVVHGGGPEINEMLKKLGIESEFVNGLRVTDEETM 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  94 ELVKQaagMLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPL---GVDDGVDYCHSGRIRRIDEEAVHRQLNSGAIV 170
Cdd:cd04250   85 EIVEM---VLVGKVNKEIVSLINRAGGKAVGLSGKDGNLIKAKKKdatVIEEIIDLGFVGEVTEVNPELLETLLEAGYIP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 171 LLGPVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGV---TNEEGRIISELFPDDAQQRIDvleqAGDYHSGTV 247
Cdd:cd04250  162 VIAPVGVGEDGETYNINADTAAGAIAAALKAEKLILLTDVAGVlddPNDPGSLISEISLKEAEELIA----DGIISGGMI 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 641744506 248 RFLRGAVKACRSGVRRSHLIsyqdDG----ALLQELFSRDGIGTQI 289
Cdd:cd04250  238 PKVEACIEALEGGVKAAHII----DGrvphSLLLEIFTDEGIGTMI 279
AAK_NAGK-like cd04238
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ...
 27-289 1.09e-38

AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the Escherichia coli and Pseudomonas aeruginosa type NAGKs which catalyze the phosphorylation of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in bacteria and photosynthetic organisms using either the acetylated, noncyclic (NC), or non-acetylated, cyclic (C) route of ornithine biosynthesis. Also included in this CD is a distinct group of uncharacterized (UC) bacterial and archeal NAGKs. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239771 [Multi-domain]  Cd Length: 256  Bit Score: 140.34  E-value: 1.09e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  27 FVIMLGGEAIEHAN-FSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHKNTRITDSATLELVKQA-AGmlq 104
Cdd:cd04238    1 VVIKYGGSAMKDEElKEAFADDIVLLKQVGINPVIVHGGGPEINELLKRLGIESEFVNGLRVTDKETMEIVEMVlAG--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 105 lDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLGVDDgVDYCHSGRIRRIDEEAVHRQLNSGAIVLLGPVAVSVTGESF 184
Cdd:cd04238   78 -KVNKELVSLLNRAGGKAVGLSGKDGGLIKAEKKEEKD-IDLGFVGEVTEVNPELLETLLEAGYIPVIAPIAVDEDGETY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 185 NLTSEEVATQLAIKLKAEKMIgFCSS-QGVTNEEGRIISELFPDDAQQRIDvleqAGDYHSGTVRFLRGAVKACRSGVRR 263
Cdd:cd04238  156 NVNADTAAGAIAAALKAEKLI-LLTDvPGVLDDPGSLISELTPKEAEELIE----DGVISGGMIPKVEAALEALEGGVRK 230

                        250       260
                 ....*....|....*....|....*.
gi 641744506 264 SHLISYQDDGALLQELFSRDGIGTQI 289
Cdd:cd04238  231 VHIIDGRVPHSLLLELFTDEGIGTMI 256
argB CHL00202
acetylglutamate kinase; Provisional
 6-291 1.09e-34

acetylglutamate kinase; Provisional


Pssm-ID: 133644 [Multi-domain]  Cd Length: 284  Bit Score: 130.30  E-value: 1.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506   6 TELVQGFRHSVPYINAHRGKTFVIMLGGEAIEHANFSS-IVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHKN 84
Cdd:CHL00202   5 DERVQVLSEALPYIQKFRGRIMVIKYGGAAMKNLILKAdIIKDILFLSCIGLKIVVVHGGGPEINFWLKQLNISPKFWNG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  85 TRITDSATLELVKQA-AGMLQLDITArlsmSLNNTPLQGAHINVVSGNFIIAQPlgvDDGVDYCHSGRIRRIDEEAVHRQ 163
Cdd:CHL00202  85 IRVTDKVTMEIVEMVlAGKVNKDLVG----SINANGGKAVGLCGKDANLIVARA---SDKKDLGLVGEIQQVDPQLIDML 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 164 LNSGAIVLLGPVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGV---TNEEGRIISELFPDDAQQridvLEQAG 240
Cdd:CHL00202 158 LEKNYIPVIASVAADHDGQTYNINADVVAGEIAAKLNAEKLILLTDTPGIladINDPNSLISTLNIKEARN----LASTG 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 641744506 241 DYHSGTVRFLRGAVKACRSGVRRSHLISYQDDGALLQELFSRDGIGTQIVM 291
Cdd:CHL00202 234 IISGGMIPKVNCCIRALAQGVEAAHIIDGKEKHALLLEILTEKGIGSMLVV 284
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 295-441 5.02e-33

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 121.25  E-value: 5.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 295 EQVRRATINDIGGILELIRPLEeqgilvrrsreqLEMEIDKFTVVVRDNLTIACAALYPFPEEsIGEMACVAVHPDYRSS 374
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYA------------LEEEIGEFWVAEEDGEIVGCAALHPLDED-LAELRSLAVHPDYRGR 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744506 375 SRGDMLLMRVAAQARQQGLQKLFVLTTH-SIHWFQERGFLPAEVEMLPKKKQalynYQRRSKILVLDL 441
Cdd:COG1246   68 GIGRRLLEALLAEARELGLKRLFLLTTSaAIHFYEKLGFEEIDKEDLPYAKV----WQRDSVVMEKDL 131
AA_kinase pfam00696
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ...
 25-268 1.29e-32

Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2.


Pssm-ID: 395565 [Multi-domain]  Cd Length: 232  Bit Score: 123.25  E-value: 1.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506   25 KTFVIMLGGEAIEHAN-FSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHkntRITDSATLELVK-QAAGM 102
Cdd:pfam00696   1 KRVVIKLGGSSLTDKErLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFA---RLTDAETLEVATmDALGS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  103 LQLDITARL-SMSLNNTPLQGAHINVVSGNFIiaqplgvddgvdychSGRIRRIDEEAVHRQLNSGAIVLLGP-VAVSVT 180
Cdd:pfam00696  78 LGERLNAALlAAGLPAVGLPAAQLLATEAGFI---------------DDVVTRIDTEALEELLEAGVVPVITGfIGIDPE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  181 GESFNLTSEEVATQLAIKLKAEKMIGFCSSQGV------TNEEGRIISELFPDDAQQridvLEQAGDYHSGTVRFLRGAV 254
Cdd:pfam00696 143 GELGRGSSDTLAALLAEALGADKLIILTDVDGVytadprKVPDAKLIPEISYDELLE----LLASGLATGGMKVKLPAAL 218

                         250
                  ....*....|....
gi 641744506  255 KACRSGVRRSHLIS 268
Cdd:pfam00696 219 EAARRGGIPVVIVN 232
PLN02512 PLN02512
acetylglutamate kinase
 15-289 5.04e-29

acetylglutamate kinase


Pssm-ID: 178128  Cd Length: 309  Bit Score: 115.55  E-value: 5.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  15 SVPYINAHRGKTFVIMLGGEAIEHANF-SSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHKNTRITDSATL 93
Cdd:PLN02512  38 ALPFIQRFRGKTVVVKYGGAAMKDPELkAGVIRDLVLLSCVGLRPVLVHGGGPEINSWLKKVGIEPQFKNGLRVTDAETM 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  94 ELVKQaagMLQLDITARLSMSLNNTPLQGAHINVVSGNFIIAQPLgvDDGVDYCHSGRIRRIDEEAVHRQLNSGAIVLLG 173
Cdd:PLN02512 118 EVVEM---VLVGKVNKSLVSLINKAGGTAVGLSGKDGRLLRARPS--PNSADLGFVGEVTRVDPTVLRPLVDDGHIPVIA 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 174 PVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGV---TNEEGRIISELFPDDAQQRIDVLEQAGdyhsGTVRFL 250
Cdd:PLN02512 193 TVAADEDGQAYNINADTAAGEIAAALGAEKLILLTDVAGVledKDDPGSLVKELDIKGVRKLIADGKIAG----GMIPKV 268

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 641744506 251 RGAVKACRSGVRRSHLISYQDDGALLQELFSRDGIGTQI 289
Cdd:PLN02512 269 ECCVRSLAQGVKTAHIIDGRVPHSLLLEILTDEGAGTMI 307
AAK cd02115
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ...
 28-289 6.97e-27

Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition.


Pssm-ID: 239033 [Multi-domain]  Cd Length: 248  Bit Score: 108.30  E-value: 6.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  28 VIMLGGEAIEH-ANFSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHKNTRITDSATLELVKQAAGMLQLD 106
Cdd:cd02115    1 VIKFGGSSVSSeERLRNLARILVKLASEGGRVVVVHGAGPQITDELLAHGELLGYARGLRITDRETDALAAMGEGMSNLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 107 ITARLSMS-LNNTPLQGAHINVVSGNfiiaqplgvddgvdYCHSGRIRRIDEEAVHRQLNSGAIVLLGPVAVSV---TGE 182
Cdd:cd02115   81 IAAALEQHgIKAVPLDLTQAGFASPN--------------QGHVGKITKVSTDRLKSLLENGILPILSGFGGTDekeTGT 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 183 SFNLTSEEVATQLAIKLKAEKMI------GFCSSQGVTNEEGRIISELFPDDAQQridvLEQAGdyhsGTVRFLRgAVKA 256
Cdd:cd02115  147 LGRGGSDSTAALLAAALKADRLViltdvdGVYTADPRKVPDAKLLSELTYEEAAE----LAYAG----AMVLKPK-AADP 217

                        250       260       270
                 ....*....|....*....|....*....|...
gi 641744506 257 CRSGVRRSHLISYQDDGALlqELFSRDGIGTQI 289
Cdd:cd02115  218 AARAGIPVRIANTENPGAL--ALFTPDGGGTLI 248
argB TIGR00761
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ...
 26-265 2.14e-26

acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many prokaryotes and the N-acetylglutamate kinase domains of multifunctional proteins from yeasts. This enzyme is the second step in the "acetylated" ornithine biosynthesis pathway. A related group of enzymes representing the first step of the pathway contain a homologous domain and are excluded from this model. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 273256 [Multi-domain]  Cd Length: 231  Bit Score: 106.21  E-value: 2.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506   26 TFVIMLGGEAIEHaNFSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHKNTRITDSATLELVKQA-AGMLQ 104
Cdd:TIGR00761   1 TIVIKIGGAAISD-LLEAFASDIAFLRAVGIKPVIVHGGGPEINELLEALGIPPEFKNGLRVTDKETLEVVEMVlIGQVN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  105 LDITArlsmSLNNTPLQGAHINVVSGNFIIAQPLGVDdgvDYCHSGRIRRIDEEAVHRQLNSGAIVLLGPVAVSVTGESF 184
Cdd:TIGR00761  80 KELVA----LLNKHGINAIGLTGGDGQLFTARYLDKE---DLGYVGEIKKVNKALIEALLKAGYIPVISSLALTAEGQAL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  185 NLTSEEVATQLAIKLKAEKMIGFCSSQGV-TNEEGRIISELFPDDAQQridvLEQAGDYHSGTVRFLRGAVKACRSGVRR 263
Cdd:TIGR00761 153 NVNADTAAGALAAALGAEKLVLLTDVPGIlNGDGQSLISEIPLDEIEQ----LIKQGIIKGGMIPKVNAALEALRGGVRS 228


                  ..
gi 641744506  264 SH 265
Cdd:TIGR00761 229 VH 230
AAK_NAGK-fArgBP cd04252
AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic ...
 28-289 1.39e-18

AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway (fArgBP). The nuclear-encoded, mitochondrial polyprotein precursor with an N-terminal NAGK (ArgB) domain (this CD), a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-Acetylglutamate Phosphate Reductase, NAGPR). The precursor is cleaved in the mitochondria into two distinct enzymes (NAGK-DUF619 and NAGPR). Native molecular weights of these proteins indicate that the kinase is an octamer whereas the reductase is a dimer. This CD also includes some gamma-proteobacteria (Xanthomonas and Xylella) NAG kinases with an N-terminal NAGK (ArgB) domain (this CD) and a C-terminal DUF619 domain. The DUF619 domain is described as a putative distant homolog of the acetyltransferase, ArgA, predicted to function in NAG synthase association in fungi. Eukaryotic sequences have an N-terminal mitochondrial transit peptide. Members of this NAG kinase domain CD belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239785 [Multi-domain]  Cd Length: 248  Bit Score: 84.74  E-value: 1.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  28 VIMLGGEAIEHaNFSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHKNTRITDSATLELVKQaagmLQLDI 107
Cdd:cd04252    2 VIKVGGAIIED-DLDELAASLSFLQHVGLYPIVVHGAGPQLNEELEAAGVEPEYVDGLRVTDPETLAVARK----VFLEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 108 TARLSMSLNNTplqGAHINVVSGNFIIAQPLgvdDGVDYCHSGRIRRIDEEAVHRQLNSGAIVLLGPVAVSVTGESFNLT 187
Cdd:cd04252   77 NLKLVEALERN---GARARPITSGVFEAEYL---DKDKYGLVGKITGVNKAPIEAAIRAGYLPILTSLAETPSGQLLNVN 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 188 SEEVATQLAIKLKAEKMIGFCSSQGVTNEEGRIISELFPDdaqQRIDVLEQAGDYHSGTVRFLRgAVKACRSGVRRSHLI 267
Cdd:cd04252  151 ADVAAGELARVLEPLKIVFLNETGGLLDGTGKKISAINLD---EEYDDLMKQPWVKYGTKLKIK-EIKELLDTLPRSSSV 226

                        250       260
                 ....*....|....*....|..
gi 641744506 268 SYQDDGALLQELFSRDGIGTQI 289
Cdd:cd04252  227 SITSPDDLQKELFTHSGAGTLI 248
PRK07757 PRK07757
N-acetyltransferase;
296-423 6.03e-16

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 74.85  E-value: 6.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 296 QVRRATINDIGGILELIRPLEEQGILVRRSREQLEMEIDKFTVVVRDNLTIACAALYpFPEESIGEMACVAVHPDYRSSS 375
Cdd:PRK07757   3 EIRKARLSDVKAIHALINVYAKKGLMLPRSLDELYENIRDFYVAEEEGEIVGCCALH-ILWEDLAEIRSLAVSEDYRGQG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 641744506 376 RGDMLLMRVAAQARQQGLQKLFVLtTHSIHWFQERGFLPAEVEMLPKK 423
Cdd:PRK07757  82 IGRMLVEACLEEARELGVKRVFAL-TYQPEFFEKLGFREVDKEALPQK 128
AAK_NAGK-UC cd04251
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ...
 28-289 2.50e-14

AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar to Escherichia coli and Pseudomonas aeruginosa NAGKs which catalyze the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis. These uncharacterized domain sequences are found in some bacteria (Deinococci and Chloroflexi) and archea and belong to the Amino Acid Kinase Superfamily (AAK).


Pssm-ID: 239784 [Multi-domain]  Cd Length: 257  Bit Score: 72.40  E-value: 2.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  28 VIMLGGE-AIEHANFSSIVNDIGLlhslgiKLVVVYGARPQIDANLTTHHYEPHYHKN-----TRITDSATLELVKQAAG 101
Cdd:cd04251    2 VVKIGGSvVSDLDKVIDDIANFGE------RLIVVHGGGNYVNEYLKRLGVEPKFVTSpsgirSRYTDKETLEVFVMVMG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 102 MLQLDITARLSM---------SLNNTPLQGAHINVVSGNfIIAQPLGVDDGvdycHSGRIRRIDEEAVHRQLNSGAIVLL 172
Cdd:cd04251   76 LINKKIVARLHSlgvkavgltGLDGRLLEAKRKEIVRVN-ERGRKMIIRGG----YTGKVEKVNSDLIEALLDAGYLPVV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 173 GPVAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGVTnEEGRIISELFPDDAQQridVLEQAGDyhsGTVRFLRG 252
Cdd:cd04251  151 SPVAYSEEGEPLNVDGDRAAAAIAAALKAERLILLTDVEGLY-LDGRVIERITVSDAES---LLEKAGG---GMKRKLLA 223

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 641744506 253 AVKACRSGVRRSHLISYQDDGALLQELfsrDGIGTQI 289
Cdd:cd04251  224 AAEAVEGGVREVVIGDARADSPISSAL---NGGGTVI 257
PRK14058 PRK14058
[LysW]-aminoadipate/[LysW]-glutamate kinase;
28-263 1.01e-13

[LysW]-aminoadipate/[LysW]-glutamate kinase;


Pssm-ID: 237599 [Multi-domain]  Cd Length: 268  Bit Score: 71.08  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  28 VIMLGGEAIEhaNFSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHY--HKN---TRITDSATLELVKQAAGM 102
Cdd:PRK14058   3 VVKIGGSVGI--DPEDALIDVASLWADGERVVLVHGGSDEVNELLERLGIEPRFvtSPSgvtSRYTDRETLEVFIMAMAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 103 LQLDITARL-SMSLNNTPLQGAHINVVSG---NFIIAqplgVDDG----VDYCHSGRIRRIDEEAVHRQLNSGAIVLLGP 174
Cdd:PRK14058  81 INKQLVERLqSLGVNAVGLSGLDGGLLEGkrkKAVRV----VEEGkkkiIRGDYTGKIEEVNTDLLKLLLKAGYLPVVAP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 175 VAVSVTGESFNLTSEEVATQLAIKLKAEKMIGFCSSQGV---TNEEGRIISELFPDDAQqriDVLEQAGDyhsGTVRFLR 251
Cdd:PRK14058 157 PALSEEGEPLNVDGDRAAAAIAGALKAEALVLLSDVPGLlrdPPDEGSLIERITPEEAE---ELSKAAGG---GMKKKVL 230

                        250
                 ....*....|..
gi 641744506 252 GAVKACRSGVRR 263
Cdd:PRK14058 231 MAAEAVEGGVGR 242
PRK12308 PRK12308
argininosuccinate lyase;
293-423 3.15e-13

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 71.74  E-value: 3.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 293 SAEQVRRATINDIGGILELIRPLEEQGILVRRSREQLEMEIDKFTVVVRDNLTIACAALYPFpEESIGEMACVAVHPDYR 372
Cdd:PRK12308 462 SGVKVRPARLTDIDAIEGMVAYWAGLGENLPRSRNELVRDIGSFAVAEHHGEVTGCASLYIY-DSGLAEIRSLGVEAGWQ 540

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 641744506 373 SSSRGDMLLMRVAAQARQQGLQKLFVLtTHSIHWFQERGFLPAEVEMLPKK 423
Cdd:PRK12308 541 VQGQGSALVQYLVEKARQMAIKKVFVL-TRVPEFFMKQGFSPTSKSLLPEK 590
PRK07922 PRK07922
amino-acid N-acetyltransferase;
290-420 2.08e-11

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 62.25  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 290 VMESAEQVRRATINDIGGILELIRPLEEQGILVRRSREQLEMEIDKFTVVVRDNLT-IACAALYPFPEEsIGEMACVAVH 368
Cdd:PRK07922   1 TAAGAITVRRARTSDVPAIKRLVDPYAQGRILLEKNLVTLYEAVQEFWVAEHLDGEvVGCGALHVMWED-LAEIRTVAVD 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641744506 369 PDYRSSSRGDMLLMRVAAQARQQGLQKLFVLtTHSIHWFQERGF-------LPAEV--EML 420
Cdd:PRK07922  80 PAARGRGVGHAIVERLLDVARELGLSRVFVL-TFEVEFFARHGFveidgtpVTPEVyaELL 139
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 28-301 3.97e-09

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 58.14  E-value: 3.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  28 VIMLGGEAIEHaNFSSIVNDIGLLHSLGIKLVVVYGARPQIDANLTTHHYEPHYHKNTRITDSATLElvkqaagmlqldI 107
Cdd:PRK04531  40 VIKVGGAVLRD-DLEALASSLSFLQEVGLTPIVVHGAGPQLDAELDAAGIEKETVNGLRVTSPEALA------------I 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 108 TARLSMSLNntplqgahinvvsgnfiiaQPLgvddgvdychsgrirridEEAVHRQLNSGAIVLLGPVAVSVTGESFNLT 187
Cdd:PRK04531 107 VRKVFQRSN-------------------LDL------------------VEAVESSLRAGSIPVIASLGETPSGQILNIN 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 188 SEEVATQLAIKLKAEKMIGFCSSQGVTNEEGRIISELfpdDAQQRIDVLEQAGDYHSGTVRFLRgAVKACRSGVRRSHLI 267
Cdd:PRK04531 150 ADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSI---NLSTEYDHLMQQPWINGGMKLKLE-QIKELLDRLPLESSV 225

                        250       260       270
                 ....*....|....*....|....*....|....
gi 641744506 268 SYQDDGALLQELFSRDGIGTQIvmESAEQVRRAT 301
Cdd:PRK04531 226 SITSPSDLAKELFTHKGSGTLV--RRGERILRAT 257
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 302-412 1.53e-08

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 52.52  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  302 INDIGGILELIRPLEEQGILVRRSREQLEMEIDKFTVVVRDNLTIACAALYPFPEES-IGEMACVAVHPDYRSSSRGDML 380
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPpVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 641744506  381 LMRVAAQARQQGLQKLFVLT----THSIHWFQERGF 412
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVaadnLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
297-416 1.01e-07

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 50.85  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 297 VRRATINDIGGILELIR---PLEEQGILVRRSREQLEMEIdkFTVVVRDNLTIACAALYPFP---EESIGEMACVAVHPD 370
Cdd:COG3153    1 IRPATPEDAEAIAALLRaafGPGREAELVDRLREDPAAGL--SLVAEDDGEIVGHVALSPVDidgEGPALLLGPLAVDPE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 641744506 371 YRSSSRGDMLLMRVAAQARQQGLQKLFVLTTHSIHWFQER-GFLPAE 416
Cdd:COG3153   79 YRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERfGFRPAG 125
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 332-412 1.31e-07

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 48.99  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  332 EIDKFTVVVRDNLTIACAALYPFPEESIGEMACVAVHPDYRSSSRGDMLLMRVAAQARQQGLQKLFVLTTHS-IHWFQER 410
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRaAAFYEKL 80


                  ..
gi 641744506  411 GF 412
Cdd:pfam13508  81 GF 82
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
296-412 5.07e-07

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 49.22  E-value: 5.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 296 QVRRATINDIGGILELIRPLEEQGI----LVRRSREQLEMEIDKFT-------VVVRDNLTIACAALYPFPEES----IG 360
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNEAIAEGTatfeTEPPSEEEREAWFAAILapgrpvlVAEEDGEVVGFASLGPFRPRPayrgTA 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 641744506 361 EMAcVAVHPDYRSSSRGDMLLMRVAAQARQQGLQKLFVLT----THSIHWFQERGF 412
Cdd:COG1247   83 EES-IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVladnEASIALYEKLGF 137
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 297-412 5.71e-06

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 45.81  E-value: 5.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 297 VRRATINDIGGILeLIRPLEEQgilvRRSREQLEMEiDKFTVVVRDNLTIACAALYPFPEEsIGEMACVAVHPDYRSSSR 376
Cdd:COG0454    3 IRKATPEDINFIL-LIEALDAE----LKAMEGSLAG-AEFIAVDDKGEPIGFAGLRRLDDK-VLELKRLYVLPEYRGKGI 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 641744506 377 GDMLLMRVAAQARQQGLQKLFVLT----THSIHWFQERGF 412
Cdd:COG0454   76 GKALLEALLEWARERGCTALELDTldgnPAAIRFYERLGF 115
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 347-412 8.41e-06

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 43.88  E-value: 8.41e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 347 ACAALYPFPEESIGEMACVAVHPDYRSSSRGDMLLMRVAAQARQQGLQKLFVLTTHS----IHWFQERGF 412
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDneaaIALYEKLGF 70
AAK_NAGS-Urea cd04236
AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ...
 38-287 1.30e-05

AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the urea cycle found in animals. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate; NAG is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Ureogenic NAGS activity is dependent on the concentration of glutamate (substrate) and arginine (activator). Domain architecture of ureogenic NAGS consists of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal DUF619 domain. Members of this CD belong to the protein superfamily, the Amino Acid Kinase Family (AAKF).


Pssm-ID: 239769 [Multi-domain]  Cd Length: 271  Bit Score: 46.76  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506  38 HANFSSIVNDIGLLHSLGIKLVVVYGArPQIDAnltthhyephyhkntriTDSATLELVKQAAGMlqlditARLSMSLNN 117
Cdd:cd04236   50 LEMVQSLSFGLAFLQRMDMKLLVVMGL-SAPDG-----------------TNMSDLELQAARSRL------VKDCKTLVE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 118 TpLQGAHINVV----SGNFIIAQplGVDDGVDYchsGRIRRIDEEAVHRQLNSGAIVLLGPVAVSVTGESFNLTSEEVAT 193
Cdd:cd04236  106 A-LQANSAAAHplfsGESVLQAE--EPEPGASK---GPSVSVDTELLQWCLGSGHIPLVCPIGETSSGRSVSLDSSEVTT 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744506 194 QLAIKLKAEKMIGFCSSQGVTNEEGRIISE-LFPDDAQQRIDVlEQAGDYHSGTVRFLRGAVKACRSGvrRSHLISYQDd 272
Cdd:cd04236  180 AIAKALQPIKVIFLNRSGGLRDQKHKVLPQvHLPADLPSLSDA-EWLSETEQNRIQDIATLLNALPSM--SSAVITSAE- 255

                        250
                 ....*....|....*
gi 641744506 273 gALLQELFSRDGIGT 287
Cdd:cd04236  256 -TLLTELFSHKGSGT 269
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 336-398 6.88e-05

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 40.72  E-value: 6.88e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641744506 336 FTVVVRDNLTIACAALYPFP-EESIGEMACVAVHPDYRSSSRGDMLLMRVAAQARQQGLQKLFV 398
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
 
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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