|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00942 |
PRK00942 |
acetylglutamate kinase; Provisional |
1-293 |
7.15e-165 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 458.80 E-value: 7.15e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 1 MITQSDRAKVLIEALPYIQRFNGATIVVKYGGHAMVDEKLKRDFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPV 80
Cdd:PRK00942 1 MIDALEKAEVLSEALPYIQRFMGKTIVIKYGGNAMTDEELKEAFARDIVLLKQVGINPVVVHGGGPQIDELLKKLGIESE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 81 FVDGMRVTDPQTMDVVEMVLVGKVNKEIVTLINTNGGRAVGLSGKDGQLVTAQRMkylksrgedqpPELIDMGLVGEITA 160
Cdd:PRK00942 81 FVNGLRVTDAETMEVVEMVLAGKVNKELVSLINKHGGKAVGLSGKDGGLITAKKL-----------EEDEDLGFVGEVTP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 161 VDPTILLKLMEDAFIPVIAPVGGGAEGETFNINADLVAGAVASALRARKLILLTDTPGVLDQSGGLLSTLKEGEARELMG 240
Cdd:PRK00942 150 VNPALLEALLEAGYIPVISPIGVGEDGETYNINADTAAGAIAAALGAEKLILLTDVPGVLDDKGQLISELTASEAEELIE 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 654867927 241 RGVIKGGMIPKVNCCLDALKGGVRKTHIIDGRQEHAILLEIFTKEGVGTEIVP 293
Cdd:PRK00942 230 DGVITGGMIPKVEAALDAARGGVRSVHIIDGRVPHALLLELFTDEGIGTMIVP 282
|
|
| ArgB |
COG0548 |
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
1-292 |
2.08e-163 |
|
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: 455.26 E-value: 2.08e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 1 MITQSDRAKVLIEALPYIQRFNGATIVVKYGGHAMVDEKLKRDFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPV 80
Cdd:COG0548 1 MESAIEKAEWLREALPYIQAFRGKTFVIKYGGEAMEDEELKAALAQDIALLKSLGIRPVLVHGGGPQINELLKRLGIESE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 81 FVDGMRVTDPQTMDVVEMVLVGKVNKEIVTLINTNGGRAVGLSGKDGQLVTAQRMKylksrgedqPPELIDMGLVGEITA 160
Cdd:COG0548 81 FVNGLRVTDEETLEVVEMVLAGKVNKEIVALLSQGGGNAVGLSGKDGNLITARPLG---------VGDGVDLGHVGEVRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 161 VDPTILLKLMEDAFIPVIAPVGGGAEGETFNINADLVAGAVASALRARKLILLTDTPGVLDQSGGLLSTLKEGEARELMG 240
Cdd:COG0548 152 VDPELIRALLDAGYIPVISPIGYSPTGEVYNINADTVAGAIAAALKAEKLILLTDVPGVLDDPGSLISELTAAEAEELIA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 654867927 241 RGVIKGGMIPKVNCCLDALKGGVRKTHIIDGRQEHAILLEIFTKEGVGTEIV 292
Cdd:COG0548 232 DGVISGGMIPKLEAALDAVRGGVKRVHIIDGRVPHALLLELFTDDGIGTMIV 283
|
|
| AAK_NAGK-C |
cd04250 |
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
10-291 |
5.86e-157 |
|
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: 438.48 E-value: 5.86e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 10 VLIEALPYIQRFNGATIVVKYGGHAMVDEKLKRDFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPVFVDGMRVTD 89
Cdd:cd04250 1 VLIEALPYIQKFRGKTVVIKYGGNAMKDEELKESFARDIVLLKYVGINPVVVHGGGPEINEMLKKLGIESEFVNGLRVTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 90 PQTMDVVEMVLVGKVNKEIVTLINTNGGRAVGLSGKDGQLVTAQRMKYLKsrgedqPPELIDMGLVGEITAVDPTILLKL 169
Cdd:cd04250 81 EETMEIVEMVLVGKVNKEIVSLINRAGGKAVGLSGKDGNLIKAKKKDATV------IEEIIDLGFVGEVTEVNPELLETL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 170 MEDAFIPVIAPVGGGAEGETFNINADLVAGAVASALRARKLILLTDTPGVLD---QSGGLLSTLKEGEARELMGRGVIKG 246
Cdd:cd04250 155 LEAGYIPVIAPVGVGEDGETYNINADTAAGAIAAALKAEKLILLTDVAGVLDdpnDPGSLISEISLKEAEELIADGIISG 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 654867927 247 GMIPKVNCCLDALKGGVRKTHIIDGRQEHAILLEIFTKEGVGTEI 291
Cdd:cd04250 235 GMIPKVEACIEALEGGVKAAHIIDGRVPHSLLLEIFTDEGIGTMI 279
|
|
| AAK_NAGK-like |
cd04238 |
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
26-291 |
1.41e-137 |
|
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: 388.79 E-value: 1.41e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 26 IVVKYGGHAMVDEKLKRDFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPVFVDGMRVTDPQTMDVVEMVLVGKVN 105
Cdd:cd04238 1 VVIKYGGSAMKDEELKEAFADDIVLLKQVGINPVIVHGGGPEINELLKRLGIESEFVNGLRVTDKETMEIVEMVLAGKVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 106 KEIVTLINTNGGRAVGLSGKDGQLVTAQRMkylksrgedqPPELIDMGLVGEITAVDPTILLKLMEDAFIPVIAPVGGGA 185
Cdd:cd04238 81 KELVSLLNRAGGKAVGLSGKDGGLIKAEKK----------EEKDIDLGFVGEVTEVNPELLETLLEAGYIPVIAPIAVDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 186 EGETFNINADLVAGAVASALRARKLILLTDTPGVLDQSGGLLSTLKEGEARELMGRGVIKGGMIPKVNCCLDALKGGVRK 265
Cdd:cd04238 151 DGETYNVNADTAAGAIAAALKAEKLILLTDVPGVLDDPGSLISELTPKEAEELIEDGVISGGMIPKVEAALEALEGGVRK 230
|
250 260
....*....|....*....|....*.
gi 654867927 266 THIIDGRQEHAILLEIFTKEGVGTEI 291
Cdd:cd04238 231 VHIIDGRVPHSLLLELFTDEGIGTMI 256
|
|
| PLN02512 |
PLN02512 |
acetylglutamate kinase |
2-291 |
1.92e-127 |
|
acetylglutamate kinase
Pssm-ID: 178128 Cd Length: 309 Bit Score: 365.16 E-value: 1.92e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 2 ITQSDRAKVLIEALPYIQRFNGATIVVKYGGHAMVDEKLKRDFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPVF 81
Cdd:PLN02512 26 STNLSRVDILSEALPFIQRFRGKTVVVKYGGAAMKDPELKAGVIRDLVLLSCVGLRPVLVHGGGPEINSWLKKVGIEPQF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 82 VDGMRVTDPQTMDVVEMVLVGKVNKEIVTLINTNGGRAVGLSGKDGQLVTAQRMkylksrgedqpPELIDMGLVGEITAV 161
Cdd:PLN02512 106 KNGLRVTDAETMEVVEMVLVGKVNKSLVSLINKAGGTAVGLSGKDGRLLRARPS-----------PNSADLGFVGEVTRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 162 DPTILLKLMEDAFIPVIAPVGGGAEGETFNINADLVAGAVASALRARKLILLTDTPGVL---DQSGGLLSTLKEGEAREL 238
Cdd:PLN02512 175 DPTVLRPLVDDGHIPVIATVAADEDGQAYNINADTAAGEIAAALGAEKLILLTDVAGVLedkDDPGSLVKELDIKGVRKL 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 654867927 239 MGRGVIKGGMIPKVNCCLDALKGGVRKTHIIDGRQEHAILLEIFTKEGVGTEI 291
Cdd:PLN02512 255 IADGKIAGGMIPKVECCVRSLAQGVKTAHIIDGRVPHSLLLEILTDEGAGTMI 307
|
|
| argB |
CHL00202 |
acetylglutamate kinase; Provisional |
1-292 |
6.93e-119 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 133644 [Multi-domain] Cd Length: 284 Bit Score: 342.54 E-value: 6.93e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 1 MITQSDRAKVLIEALPYIQRFNGATIVVKYGGHAMVDEKLKRDFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPV 80
Cdd:CHL00202 1 MLNNDERVQVLSEALPYIQKFRGRIMVIKYGGAAMKNLILKADIIKDILFLSCIGLKIVVVHGGGPEINFWLKQLNISPK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 81 FVDGMRVTDPQTMDVVEMVLVGKVNKEIVTLINTNGGRAVGLSGKDGQLVTAqrmkylksrgedQPPELIDMGLVGEITA 160
Cdd:CHL00202 81 FWNGIRVTDKVTMEIVEMVLAGKVNKDLVGSINANGGKAVGLCGKDANLIVA------------RASDKKDLGLVGEIQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 161 VDPTILLKLMEDAFIPVIAPVGGGAEGETFNINADLVAGAVASALRARKLILLTDTPGVL---DQSGGLLSTLKEGEARE 237
Cdd:CHL00202 149 VDPQLIDMLLEKNYIPVIASVAADHDGQTYNINADVVAGEIAAKLNAEKLILLTDTPGILadiNDPNSLISTLNIKEARN 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 654867927 238 LMGRGVIKGGMIPKVNCCLDALKGGVRKTHIIDGRQEHAILLEIFTKEGVGTEIV 292
Cdd:CHL00202 229 LASTGIISGGMIPKVNCCIRALAQGVEAAHIIDGKEKHALLLEILTEKGIGSMLV 283
|
|
| argB |
TIGR00761 |
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ... |
25-268 |
5.22e-88 |
|
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: 262.22 E-value: 5.22e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 25 TIVVKYGGHAMVDekLKRDFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPVFVDGMRVTDPQTMDVVEMVLVGKV 104
Cdd:TIGR00761 1 TIVIKIGGAAISD--LLEAFASDIAFLRAVGIKPVIVHGGGPEINELLEALGIPPEFKNGLRVTDKETLEVVEMVLIGQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 105 NKEIVTLINTNGGRAVGLSGKDGQLVTAQRMKYLksrgedqppeliDMGLVGEITAVDPTILLKLMEDAFIPVIAPVGGG 184
Cdd:TIGR00761 79 NKELVALLNKHGINAIGLTGGDGQLFTARYLDKE------------DLGYVGEIKKVNKALIEALLKAGYIPVISSLALT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 185 AEGETFNINADLVAGAVASALRARKLILLTDTPGVLDQSGG-LLSTLKEGEARELMGRGVIKGGMIPKVNCCLDALKGGV 263
Cdd:TIGR00761 147 AEGQALNVNADTAAGALAAALGAEKLVLLTDVPGILNGDGQsLISEIPLDEIEQLIKQGIIKGGMIPKVNAALEALRGGV 226
|
....*
gi 654867927 264 RKTHI 268
Cdd:TIGR00761 227 RSVHI 231
|
|
| PRK05279 |
PRK05279 |
N-acetylglutamate synthase; Validated |
13-292 |
5.29e-49 |
|
N-acetylglutamate synthase; Validated
Pssm-ID: 235386 [Multi-domain] Cd Length: 441 Bit Score: 168.41 E-value: 5.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 13 EALPYIQRFNGATIVVKYGGHAMVDEKLkRDFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPVFVDGMRVTDPQT 92
Cdd:PRK05279 15 HSAPYINAHRGKTFVIMLGGEAIAHGNF-SNIVHDIALLHSLGIRLVLVHGARPQIEEQLAARGIEPRYHKGLRVTDAAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 93 MDVVEMVlVGKVNKEI-----VTLINT--NGG--RAVGlsgkdGQLVTAQRMkylksrGEDqppELIDMGLVGEITAVDP 163
Cdd:PRK05279 94 LECVKQA-AGELRLDIearlsMGLPNTpmAGAhiRVVS-----GNFVTARPL------GVD---DGVDYQHTGEVRRIDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 164 TILLKLMEDAFIPVIAPVGGGAEGETFNINADLVAGAVASALRARKLILLTDTPGVLDQSGGLLSTLKEGEAREL---MG 240
Cdd:PRK05279 159 EAIRRQLDSGAIVLLSPLGYSPTGESFNLTMEEVATQVAIALKADKLIFFTESQGVLDEDGELIRELSPNEAQALleaLE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 654867927 241 RGVIKGGMIPKVNCCLDALKGGVRKTHIIDGRQEHAILLEIFTKEGVGTEIV 292
Cdd:PRK05279 239 DGDYNSGTARFLRAAVKACRGGVRRSHLISYAEDGALLQELFTRDGIGTMIV 290
|
|
| AAK_NAGS-ABP |
cd04237 |
AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ... |
13-291 |
1.06e-47 |
|
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: 160.80 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 13 EALPYIQRFNGATIVVKYGGHAMVDEKLKRdFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPVFVDGMRVTDPQT 92
Cdd:cd04237 8 EAAPYINAHRGKTFVIAFGGEAVAHPNFDN-IVHDIALLHSLGIRLVLVHGARPQIDQRLAERGLEPRYHRGLRITDAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 93 MDVVeMVLVGKVNKEIVTLI-----NTNGGRAvGLSGKDGQLVTAQRMKYLksrgedqppELIDMGLVGEITAVDPTILL 167
Cdd:cd04237 87 LECV-KEAAGAVRLEIEALLsmglpNSPMAGA-RIRVVSGNFVTARPLGVV---------DGVDFGHTGEVRRIDADAIR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 168 KLMEDAFIPVIAPVGGGAEGETFNINADLVAGAVASALRARKLILLTDTPGVLDQSGGLLSTLKEGEARELM-GRGVIKG 246
Cdd:cd04237 156 RQLDQGSIVLLSPLGYSPTGEVFNLSMEDVATAVAIALKADKLIFLTDGPGLLDDDGELIRELTAQEAEALLeTGALLTN 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 654867927 247 GMIPKVNCCLDALKGGVRKTHIIDGRQEHAILLEIFTKEGVGTEI 291
Cdd:cd04237 236 DTARLLQAAIEACRGGVPRVHLISYAEDGALLLELFTRDGVGTLI 280
|
|
| PRK14058 |
PRK14058 |
[LysW]-aminoadipate/[LysW]-glutamate kinase; |
25-293 |
1.69e-47 |
|
[LysW]-aminoadipate/[LysW]-glutamate kinase;
Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 159.68 E-value: 1.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 25 TIVVKYGGHAMVDEKlkrDFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPVFV---DGM--RVTDPQTMDVVEMV 99
Cdd:PRK14058 1 MIVVKIGGSVGIDPE---DALIDVASLWADGERVVLVHGGSDEVNELLERLGIEPRFVtspSGVtsRYTDRETLEVFIMA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 100 LvGKVNKEIVTLINTNGGRAVGLSGKDGQLVTAQRMKYLKSRgEDQPPELIDMGLVGEITAVDPTILLKLMEDAFIPVIA 179
Cdd:PRK14058 78 M-ALINKQLVERLQSLGVNAVGLSGLDGGLLEGKRKKAVRVV-EEGKKKIIRGDYTGKIEEVNTDLLKLLLKAGYLPVVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 180 PVGGGAEGETFNINADLVAGAVASALRARKLILLTDTPGVL---DQSGGLLSTLKEGEARELMgrGVIKGGMIPKVNCCL 256
Cdd:PRK14058 156 PPALSEEGEPLNVDGDRAAAAIAGALKAEALVLLSDVPGLLrdpPDEGSLIERITPEEAEELS--KAAGGGMKKKVLMAA 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 654867927 257 DALKGGVRKTHIIDGRQEHAILLEIftkEGVGTEIVP 293
Cdd:PRK14058 234 EAVEGGVGRVIIADANVDDPISAAL---AGEGTVIVN 267
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
25-270 |
9.27e-46 |
|
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: 154.06 E-value: 9.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 25 TIVVKYGGHAMVDEKLKRDFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPVFVdgmRVTDPQTMDVVEMVLVGKV 104
Cdd:pfam00696 2 RVVIKLGGSSLTDKERLKRLADEIAALLEEGRKLVVVHGGGAFADGLLALLGLSPRFA---RLTDAETLEVATMDALGSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 105 NKEIVTLINTNGGRAVGLSGKDGQLVTAQRMKylksrgedqppelidmglvGEITAVDPTILLKLMEDAFIPVIAP-VGG 183
Cdd:pfam00696 79 GERLNAALLAAGLPAVGLPAAQLLATEAGFID-------------------DVVTRIDTEALEELLEAGVVPVITGfIGI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 184 GAEGETFNINADLVAGAVASALRARKLILLTDTPGVLD------QSGGLLSTLKEGEARELMGRGVIKGGMIPKVNCCLD 257
Cdd:pfam00696 140 DPEGELGRGSSDTLAALLAEALGADKLIILTDVDGVYTadprkvPDAKLIPEISYDELLELLASGLATGGMKVKLPAALE 219
|
250
....*....|...
gi 654867927 258 ALKGGVRKTHIID 270
Cdd:pfam00696 220 AARRGGIPVVIVN 232
|
|
| AAK_NAGK-NC |
cd04249 |
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ... |
59-291 |
2.10e-44 |
|
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis using the acetylated, noncyclic route of ornithine biosynthesis. There are two variants of this pathway. In one, typified by the pathway in Escherichia coli, glutamate is acetylated by acetyl-CoA and acetylornithine is deacylated hydrolytically. In this pathway, feedback inhibition by arginine occurs at the initial acetylation of glutamate and not at the phosphorylation of NAG by NAGK. Homodimeric NAGK-NC are members of the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239782 [Multi-domain] Cd Length: 252 Bit Score: 151.41 E-value: 2.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 59 VVVHGGGPQIGELLKRLSIEPVFVDGMRVTDPQTMDVVEMVLVGKVNKEIVTLINTNGGRAVGLSGKDGQLVTAQRMKyl 138
Cdd:cd04249 35 VIVHGGGCVVDELLKKLNFPSEKKNGLRVTPKEQIPYITGALAGTANKQLMAQAIKAGLKPVGLSLADGGMTAVTQLD-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 139 ksrgedqpPELidmGLVGEITAVDPTILLKLMEDAFIPVIAPVGGGAEGETFNINADLVAGAVASALRArKLILLTDTPG 218
Cdd:cd04249 113 --------PEL---GAVGKATANDPSLLNDLLKAGFLPIISSIGADDQGQLMNVNADQAATAIAQLLNA-DLVLLSDVSG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654867927 219 VLDQSGGLLSTLKEGEARELMGRGVIKGGMIPKVNCCLDALKGGVRKTHIIDGRQEHAiLLEIFTKEGVGTEI 291
Cdd:cd04249 181 VLDADKQLISELNAKQAAELIEQGVITDGMIVKVNAALDAAQSLRRGIDIASWQYPEQ-LTALLAGEPVGTKI 252
|
|
| AAK_NAGK-UC |
cd04251 |
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
26-278 |
1.35e-41 |
|
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: 144.05 E-value: 1.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 26 IVVKYGGHAMVDEklkrDFALDIILlkYVGLNPVVVHGGGPQIGELLKRLSIEPVFV---DGM--RVTDPQTMDVVEMVL 100
Cdd:cd04251 1 IVVKIGGSVVSDL----DKVIDDIA--NFGERLIVVHGGGNYVNEYLKRLGVEPKFVtspSGIrsRYTDKETLEVFVMVM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 101 vGKVNKEIVTLINTNGGRAVGLSGKDGQLVTAQRMKYLKSRgEDQPPELIDMGLVGEITAVDPTILLKLMEDAFIPVIAP 180
Cdd:cd04251 75 -GLINKKIVARLHSLGVKAVGLTGLDGRLLEAKRKEIVRVN-ERGRKMIIRGGYTGKVEKVNSDLIEALLDAGYLPVVSP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 181 VGGGAEGETFNINADLVAGAVASALRARKLILLTDTPGVLdQSGGLLSTLKEGEARELMGRgvIKGGMIPKVNCCLDALK 260
Cdd:cd04251 153 VAYSEEGEPLNVDGDRAAAAIAAALKAERLILLTDVEGLY-LDGRVIERITVSDAESLLEK--AGGGMKRKLLAAAEAVE 229
|
250
....*....|....*...
gi 654867927 261 GGVRKTHIIDGRQEHAIL 278
Cdd:cd04251 230 GGVREVVIGDARADSPIS 247
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
27-291 |
6.76e-39 |
|
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: 136.80 E-value: 6.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 27 VVKYGGHAMVDEKLKRDFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPVFVDGMRVTDPQTMDVVEMVLvGKVNK 106
Cdd:cd02115 1 VIKFGGSSVSSEERLRNLARILVKLASEGGRVVVVHGAGPQITDELLAHGELLGYARGLRITDRETDALAAMGE-GMSNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 107 EIVTLINTNGGRAVGLSGKDGQLVTAqrmkylksrgedqppeliDMGLVGEITAVDPTILLKLMEDAFIPVIAPVGGGAE 186
Cdd:cd02115 80 LIAAALEQHGIKAVPLDLTQAGFASP------------------NQGHVGKITKVSTDRLKSLLENGILPILSGFGGTDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 187 GET---FNINADLVAGAVASALRARKLILLTDTPGVLD------QSGGLLSTLKEGEARELMGrgviKGGMIPKVNCCLD 257
Cdd:cd02115 142 KETgtlGRGGSDSTAALLAAALKADRLVILTDVDGVYTadprkvPDAKLLSELTYEEAAELAY----AGAMVLKPKAADP 217
|
250 260 270
....*....|....*....|....*....|....
gi 654867927 258 ALKGGVRkTHIIDGrqEHAILLEIFTKEGVGTEI 291
Cdd:cd02115 218 AARAGIP-VRIANT--ENPGALALFTPDGGGTLI 248
|
|
| N-Ac-Glu-synth |
TIGR01890 |
amino-acid N-acetyltransferase; This model represents a clade of amino-acid ... |
13-292 |
3.07e-38 |
|
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: 139.55 E-value: 3.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 13 EALPYIQRFNGATIVVKYGGHAMVDEKLKRdFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPVFVDGMRVTDPQT 92
Cdd:TIGR01890 7 EAAPYINAHRGKTFVVGLGGELVEGGNLGN-IVADIALLHSLGVRLVLVHGARPQIERILAARGRTPHYHRGLRVTDEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 93 MDVVeMVLVGKVNKEI-VTL---INTNGGRAVGLSGKDGQLVTAQRMKYLksrgedqppELIDMGLVGEITAVDPTILLK 168
Cdd:TIGR01890 86 LEQA-QQAAGTLRLAIeARLsmsLSNTPMAGSRLPVVSGNFVTARPIGVI---------EGVDYEHTGVIRKIDTEGIRR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 169 LMEDAFIPVIAPVGGGAEGETFNINADLVAGAVASALRARKLILLTDTPGVLDQSGGLLSTLKEGEARELMGRgVIKGGM 248
Cdd:TIGR01890 156 QLDAGSIVLLSPLGHSPTGETFNLDMEDVATSVAISLKADKLIYFTLSPGISDPDGTLAAELSPQEVESLAER-LGSETT 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 654867927 249 IPKVNCCLDALKGGVRKTHIIDGRQEHAILLEIFTKEGVGTEIV 292
Cdd:TIGR01890 235 RRLLSAAVKACRGGVHRSHIVSYAEDGSLLQELFTRDGIGTSIS 278
|
|
| AAK_NAGK-fArgBP |
cd04252 |
AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic ... |
27-291 |
2.10e-37 |
|
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: 132.89 E-value: 2.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 27 VVKYGGhAMVDEKLKrDFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPVFVDGMRVTDPQTMDVVEMVLVgKVNK 106
Cdd:cd04252 2 VIKVGG-AIIEDDLD-ELAASLSFLQHVGLYPIVVHGAGPQLNEELEAAGVEPEYVDGLRVTDPETLAVARKVFL-EENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 107 EIVTLINTNGGRAVGLSGKDGQLVTAQRMKYlksrgedqppelidmGLVGEITAVDPTILLKLMEDAFIPVIAPVGGGAE 186
Cdd:cd04252 79 KLVEALERNGARARPITSGVFEAEYLDKDKY---------------GLVGKITGVNKAPIEAAIRAGYLPILTSLAETPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 187 GETFNINADLVAGAVASALRARKLILLTDTPGVLDQSGGLLSTLK-EGEARELMGRGVIKGGM---IPKVNCCLDALKgg 262
Cdd:cd04252 144 GQLLNVNADVAAGELARVLEPLKIVFLNETGGLLDGTGKKISAINlDEEYDDLMKQPWVKYGTklkIKEIKELLDTLP-- 221
|
250 260 270
....*....|....*....|....*....|.
gi 654867927 263 vRKTH--IIDGRQehaILLEIFTKEGVGTEI 291
Cdd:cd04252 222 -RSSSvsITSPDD---LQKELFTHSGAGTLI 248
|
|
| ARG2 |
COG5630 |
N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism]; |
17-291 |
1.01e-34 |
|
N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];
Pssm-ID: 444357 [Multi-domain] Cd Length: 437 Bit Score: 130.21 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 17 YIQRFNGAT----IVVKYGGhAMVDEKLKrDFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPVFVDGMRVTDPQT 92
Cdd:COG5630 26 YLKRFSQVDaerfAVVKVGG-AVLRDDLD-ALASSLSFLQQVGLTPIVVHGAGPQLDAALAAAGIETQRVDGLRVTSPEA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 93 MDVVEMVLVgKVNKEIVTLINTNGGRAVGL-SGkdgqLVTAqrmKYLKSRgedqppeliDMGLVGEITAVDPTILLKLME 171
Cdd:COG5630 104 LEIVRRVFQ-QENLKLVEALEAMGTRARPIpSG----VFEA---EYLDRD---------TLGLVGEVTGVHLAPIEASLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 172 DAFIPVIAPVGGGAEGETFNINADLVAGAVASALRARKLILLTDTPGVLDQSGGLLSTLKEGEARE-LMGRGVIKGGMIP 250
Cdd:COG5630 167 AGSIPIIASLGETPSGQILNINADVAARELVHALQPYKIVFLTGTGGLLDEDGKIISSINLATDFDhLMAQPWVNGGMRL 246
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 654867927 251 KVNCCLDALKGGVRKTHIIDGRQEHaILLEIFTKEGVGTEI 291
Cdd:COG5630 247 KLEEIKDLLDDLPLTSSVSITRPSE-LAKELFTHKGSGTLV 286
|
|
| PRK04531 |
PRK04531 |
acetylglutamate kinase; Provisional |
13-289 |
9.71e-25 |
|
acetylglutamate kinase; Provisional
Pssm-ID: 235306 [Multi-domain] Cd Length: 398 Bit Score: 102.43 E-value: 9.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 13 EALPYIQRFNGAT----IVVKYGGhAMVDEKLKrDFALDIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPVFVDGMRVT 88
Cdd:PRK04531 22 EISQYLKRFSQLDaerfAVIKVGG-AVLRDDLE-ALASSLSFLQEVGLTPIVVHGAGPQLDAELDAAGIEKETVNGLRVT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 89 DPQTMdvveMVLVGKVNKEIVTLINtnggrAVGLSGKDGQlvtaqrmkylksrgedqppelidmglvgeitavdptillk 168
Cdd:PRK04531 100 SPEAL----AIVRKVFQRSNLDLVE-----AVESSLRAGS---------------------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 169 lmedafIPVIAPVGGGAEGETFNINADLVAGAVASALRARKLILLTDTPGVLDQSGGLLSTLK-EGEARELMGRGVIKGG 247
Cdd:PRK04531 131 ------IPVIASLGETPSGQILNINADVAANELVSALQPYKIIFLTGTGGLLDADGKLISSINlSTEYDHLMQQPWINGG 204
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 654867927 248 MIPKVNCCLDALKGGVRKTHIIDGRQEHaILLEIFTKEGVGT 289
Cdd:PRK04531 205 MKLKLEQIKELLDRLPLESSVSITSPSD-LAKELFTHKGSGT 245
|
|
| PLN02825 |
PLN02825 |
amino-acid N-acetyltransferase |
13-291 |
2.71e-19 |
|
amino-acid N-acetyltransferase
Pssm-ID: 215441 [Multi-domain] Cd Length: 515 Bit Score: 87.52 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 13 EALPYIQRFNGATIVVKYGGHAMVDEKLkrDFAL-DIILLKYVGLNPVVVHGGGPQIGELLKRLSIEPVFVDGMRVTDPQ 91
Cdd:PLN02825 7 EAWPYIQGHRGSTFVVVISGEVVAGPHL--DNILqDISLLHGLGIKFVLVPGTHVQIDKLLAERGREPKYVGAYRITDSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 92 TMDVvEMVLVGKVNKEI---------VTLINTNGGRA----VGLSGKDGQLVTAQRmkylksRGedqPPELIDMGLVGEI 158
Cdd:PLN02825 85 ALQA-SMEAAGKIRVMIeaklspgpsIPNLRRHGDNSrwheVGVSVASGNFLAAKR------RG---VVNGVDFGATGEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 159 TAVDPTILLKLMEDAFIPVIAPVGGGAEGETFNINADLVAGAVASALRARKLILLTDTPgVLDQSGGLLSTLKEGEAREL 238
Cdd:PLN02825 155 KKIDVSRIKERLDSNCIVLLSNLGYSSSGEVLNCNTYEVATACALAIGADKLICIVDGP-ILDENGRLIRFMTLEEADML 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 239 M---------------------------------------GRGVIKGG------------------------------MI 249
Cdd:PLN02825 234 IrkrakqseiaanyvkavggedysyslgldsvnttpfnnnGRGFWGSGsatdsfqngvgfdngnglsgeqgfaiggeeRL 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 654867927 250 PKVNCCLDAL-------KGGVRKTHIIDGRQEHAILLEIFTKEGVGTEI 291
Cdd:PLN02825 314 SRLNGYLSELaaaafvcRGGVQRVHLLDGTIEGVLLLELFTRDGMGTMI 362
|
|
| AAK_NAGS-Urea |
cd04236 |
AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ... |
156-229 |
1.03e-06 |
|
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: 49.07 E-value: 1.03e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654867927 156 GEITAVDPTILLKLMEDAFIPVIAPVGGGAEGETFNINADLVAGAVASALRARKLILLTDTPGVLDQSGGLLST 229
Cdd:cd04236 136 GPSVSVDTELLQWCLGSGHIPLVCPIGETSSGRSVSLDSSEVTTAIAKALQPIKVIFLNRSGGLRDQKHKVLPQ 209
|
|
| AAK_FomA-like |
cd04241 |
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ... |
25-291 |
1.89e-06 |
|
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar proteins found in a wide range of organisms. Together, the fomA and fomB genes in the fosfomycin biosynthetic gene cluster of Streptomyces wedmorensis confer high-level fosfomycin resistance. FomA and FomB proteins converted fosfomycin to fosfomycin monophosphate and fosfomycin diphosphate in the presence of ATP and a magnesium ion, indicating that FomA and FomB catalyzed phosphorylations of fosfomycin and fosfomycin monophosphate, respectively. FomA and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239774 [Multi-domain] Cd Length: 252 Bit Score: 48.03 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 25 TIVVKYGGHAMVDEKLKRDFALDII------LLKYVGLNPVVVHGGG----PQIGELLKRLSIEPVFVDGMRVTdpqTMD 94
Cdd:cd04241 1 MIILKLGGSVITDKDRPETIREENLeriareLAEAIDEKLVLVHGGGsfghPKAKEYGLPDGDGSFSAEGVAET---HEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 95 VVEmvlvgkVNKEIVTLINTNGGRAVGLSGKdgQLVTAQRmkylksrgedqppelidmglvGEITAVDPTILLKLMEDAF 174
Cdd:cd04241 78 MLE------LNSIVVDALLEAGVPAVSVPPS--SFFVTEN---------------------GRIVSFDLEVIKELLDRGF 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 175 IPVIApvgGGA---EGETFNI-NADLVAGAVASALRARKLILLTDTPGVLDQS---GGLLSTLKEGEARELMGRGVIK-- 245
Cdd:cd04241 129 VPVLH---GDVvldEGGGITIlSGDDIVVELAKALKPERVIFLTDVDGVYDKPppdAKLIPEIDVGSLEDILAALGSAgt 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 654867927 246 ---GGMIPKVNCCLDALKGGVrKTHIIDGRqEHAILLEIFTKEGVGTEI 291
Cdd:cd04241 206 dvtGGMAGKIEELLELARRGI-EVYIFNGD-KPENLYRALLGNFIGTRI 252
|
|
| AAK_P5CS_ProBA |
cd04256 |
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ... |
195-289 |
3.29e-04 |
|
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR, ProA), the first and second enzyme catalyzing proline (and, in mammals, ornithine) biosynthesis. G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, and is subject to feedback allosteric inhibition by proline or ornithine. In plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia.
Pssm-ID: 239789 [Multi-domain] Cd Length: 284 Bit Score: 41.65 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 195 DLVAGAVASALRARKLILLTDTPGVLDQSGG-----LLSTLKEGEAREL-------MGRGvikgGMIPKVNCCLDALKGG 262
Cdd:cd04256 181 DSLAARLAVELKADLLILLSDVDGLYDGPPGsddakLIHTFYPGDQQSItfgtksrVGTG----GMEAKVKAALWALQGG 256
|
90 100
....*....|....*....|....*..
gi 654867927 263 VrKTHIIDGRQEHAIlLEIFTKEGVGT 289
Cdd:cd04256 257 T-SVVITNGMAGDVI-TKILEGKKVGT 281
|
|
| AAK_G5K_ProB |
cd04242 |
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
195-289 |
4.01e-04 |
|
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (and, in mammals, ornithine) biosynthesis. G5K is subject to feedback allosteric inhibition by proline or ornithine. In microorganisms and plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia. Microbial G5K generally consists of two domains: a catalytic G5K domain and one PUA (pseudo uridine synthases and archaeosine-specific transglycosylases) domain, and some lack the PUA domain. G5K requires free Mg for activity, it is tetrameric, and it aggregates to higher forms in a proline-dependent way. G5K lacking the PUA domain remains tetrameric, active, and proline-inhibitable, but the Mg requirement and the proline-triggered aggregation are greatly diminished and abolished, respectively, and more proline is needed for inhibition. Although plant and animal G5Ks are part of a bifunctional polypeptide, delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR; ProA); bacterial and yeast G5Ks are monofunctional single-polypeptide enzymes. In this CD, all three domain architectures are present: G5K, G5K+PUA, and G5K+G5PR.
Pssm-ID: 239775 [Multi-domain] Cd Length: 251 Bit Score: 40.89 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 195 DLVAGAVASALRARKLILLTDTPGVLDQSGG------LLSTLKEGEArELM------GRGVIKGGMIPKVNCCLDALKGG 262
Cdd:cd04242 145 DRLSALVAGLVNADLLILLSDVDGLYDKNPRenpdakLIPEVEEITD-EIEamaggsGSSVGTGGMRTKLKAARIATEAG 223
|
90 100
....*....|....*....|....*..
gi 654867927 263 VrKTHIIDGRQEHaILLEIFTKEGVGT 289
Cdd:cd04242 224 I-PVVIANGRKPD-VLLDILAGEAVGT 248
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|
| ArcC |
COG0549 |
Carbamate kinase [Amino acid transport and metabolism]; |
175-293 |
7.02e-04 |
|
Carbamate kinase [Amino acid transport and metabolism];
Pssm-ID: 440315 Cd Length: 313 Bit Score: 40.44 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 175 IPVIAPVGGGAEGetfnINA----DLVAGAVASALRARKLILLTDTPGVL------DQSGglLSTLKEGEARELMGRGVI 244
Cdd:COG0549 195 IPVVRDEDGGLKG----VEAvidkDLASALLAEELDADLLLILTDVDKVYinfgkpDQRA--LDEVTVAEAKKYIEEGHF 268
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 654867927 245 -KGGMIPKVNCCLDALKGGVRKTHIidGRQEHAilLEIFtKEGVGTEIVP 293
Cdd:COG0549 269 aAGSMGPKVEAAIRFVEATGKRAII--TSLEKA--EEAL-AGKAGTRIVP 313
|
|
| AAK_UC |
cd04240 |
AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few ... |
191-291 |
2.75e-03 |
|
AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few bacteria. Sequences in this CD are members of the Amino Acid Kinase (AAK) superfamily.
Pssm-ID: 239773 [Multi-domain] Cd Length: 203 Bit Score: 38.11 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 191 NINADLVAGAVASALRARKLILLTDTPGVLDQSGGLlstLKEGEARELMGRGVIKGGMIP-----KVNCcldalkggvrk 265
Cdd:cd04240 113 EVTSDSIAAWLAKKLGAKRLVIVTDVDGIYEKDGKL---VNEIAAAELLGETSVDPAFPRlltkyGIRC----------- 178
|
90 100
....*....|....*....|....*.
gi 654867927 266 tHIIDGRQEHAILLEIFTKEGVGTEI 291
Cdd:cd04240 179 -YVVNGDDPERVLAALRGREGVGTRI 203
|
|
| ProB |
COG0263 |
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ... |
201-293 |
5.33e-03 |
|
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440033 [Multi-domain] Cd Length: 371 Bit Score: 38.09 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654867927 201 VASALRARKLILLTDTPGV------LDQSGGLLSTLKEGEAR-ELM----GRGVIKGGMIPKVNCCLDALKGGVRkTHII 269
Cdd:COG0263 159 VANLVEADLLVLLTDVDGLydadprKDPDAKLIPEVEEITPEiEAMaggaGSGLGTGGMATKLEAARIATRAGIP-TVIA 237
|
90 100
....*....|....*....|....
gi 654867927 270 DGRQEHaILLEIFTKEGVGTEIVP 293
Cdd:COG0263 238 SGREPN-VLLRILAGERVGTLFLP 260
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