|
Name |
Accession |
Description |
Interval |
E-value |
| metL |
PRK09466 |
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional |
1-810 |
0e+00 |
|
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional
Pssm-ID: 236530 [Multi-domain] Cd Length: 810 Bit Score: 1576.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 1 MSVIAQAGAKGRQLHKFGGSSLADAKCYLRVAGIMTEYSQAGDMMVVSAAGSTTNQLISWLKLSQTDRLSAHQVQQSLRR 80
Cdd:PRK09466 1 MSVIAQAGAMGRQLHKFGGSSLADAKCYRRVAGILAEYSQPDDLVVVSAAGKTTNQLISWLKLSQTDRLSAHQVQQTLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 81 YQMELISGLLSPDAADTLIAIFIQDLERLAGLLDGGITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSFLRAE 160
Cdd:PRK09466 81 YQQDLIEGLLPAEQARSLLSRLISDLERLAALLDGGINDAQYAEVVGHGEVWSARLMAALLNQQGLPAAWLDARSFLRAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 161 RSAQPQVDEGLSYPLLQQLIAQHPNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADP 240
Cdd:PRK09466 161 RAAQPQVDEGLSYPLLQQLLAQHPGKRLVVTGFISRNEAGETVLLGRNGSDYSATLIGALAGVERVTIWSDVAGVYSADP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 241 RKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIERVLASGTGARIVTSHDDVCLI 320
Cdd:PRK09466 241 RKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYQPEQGSTRIERVLASGTGARIVTSLDDVCLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 321 EFQVPGGQDFKLAHKELDAILKRAQLRPLAVGVHADRKLLQFCYTSEVADSALKLLDEAGLPGELRLRQKLALVAMVGAG 400
Cdd:PRK09466 321 ELQVPASHDFKLAQKELDQLLKRAQLRPLAVGVHPDRQLLQLAYTSEVADSALKLLDDAALPGELKLREGLALVALVGAG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 401 VTRNPLHCHRFWQQLKGQPVEFTWQSEEGISLVAVLRAGPTESLIQGLHQSLFRAEKRIGLVLFGKGNIGSRWLELFARE 480
Cdd:PRK09466 401 VTRNPLHCHRFYQQLKDQPVEFIWQSEDGLSLVAVLRQGPTESLIQGLHQSLFRAEKRIGLVLFGKGNIGSRWLELFARE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 481 QTTLSARTGFEFILAGVVDSRRSLLNYEGLDASRALAFFNDEAVEQDEESLFLWMRAHPYDDLVVLDVTASAQLADQYLD 560
Cdd:PRK09466 481 QSTLSARTGFEFVLVGVVDSRRSLLNYDGLDASRALAFFDDEAVEWDEESLFLWLRAHPYDELVVLDVTASEQLALQYPD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 561 FASHGFHVISANKLAGASSSSKYRQIHDAFEKTGRHWLYNATVGAGLPVNHTVRDLIDSGDTILALSGIFSGTLSWLFLQ 640
Cdd:PRK09466 561 FASHGFHVISANKLAGSSPSNFYRQIKDAFAKTGRHWLYNATVGAGLPINHTVRDLRNSGDSILAISGIFSGTLSWLFLQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 641 FDGTVPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAREAGYNIEPDQVRVESLVPAHCEEGSVDHFFENGEALNE 720
Cdd:PRK09466 641 FDGSVPFSELVDQAWQQGLTEPDPRDDLSGRDVMRKLVILAREAGYEIEPDDVRVESLVPAHLEDGSLDQFFENGDELDE 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 721 QMLQRLEAAREMGLVLRYVARFDANGKARVGVEAVREEHPLAALLPCDNVFAIESRWYRDNPLVIRGPGAGRDVTAGAIQ 800
Cdd:PRK09466 721 QMLQRLEAAAEQGKVLRYVARFDANGKARVGVEAVRPDHPLANLLPCDNVFAIESRWYRDNPLVIRGPGAGREVTAGAIQ 800
|
810
....*....|
gi 490994282 801 SDINRLAQLL 810
Cdd:PRK09466 801 SDLNRLAQLL 810
|
|
| thrA |
PRK09436 |
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional |
15-807 |
0e+00 |
|
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
Pssm-ID: 181856 [Multi-domain] Cd Length: 819 Bit Score: 582.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 15 HKFGGSSLADAKCYLRVAGIMTEYSQAGDMMVV-SAAGSTTNQLISWLKLSQTDRLSAHQVQQSLRRYqMELISGL---L 90
Cdd:PRK09436 4 LKFGGTSVANAERFLRVADIIESNARQEQVAVVlSAPAKVTNHLVAMIEKAAKGDDAYPEILDAERIF-HELLDGLaaaL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 91 SPDAADTLIAIFIQDLERLAGLLDG-----GITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSFLRAERS-AQ 164
Cdd:PRK09436 83 PGFDLAQLKAKVDQEFAQLKDILHGisllgECPDSVNAAIISRGERLSIAIMAAVLEARGHDVTVIDPRELLLADGHyLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 165 PQVDEGLSYPLLQQLIAQHPNkRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVK 244
Cdd:PRK09436 163 STVDIAESTRRIAASFIPADH-VILMPGFTAGNEKGELVTLGRNGSDYSAAILAACLDADCCEIWTDVDGVYTADPRVVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 245 DACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIERvlASGTGARIV---TSHDDVCLIE 321
Cdd:PRK09436 242 DARLLKSLSYQEAMELSYFGAKVLHPRTIAPIAQFQIPCLIKNTFNPQAPGTLIGA--ESDEDSLPVkgiSNLNNMAMFN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 322 FQVPGGQD--------FklahkeldAILKRAQlrplaVGV---------HAdrklLQFCYTSEVADSALKLLDEA----- 379
Cdd:PRK09436 320 VSGPGMKGmvgmasrvF--------AALSRAG-----ISVvlitqssseYS----ISFCVPQSDAAKAKRALEEEfalel 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 380 --GLPGELRLRQKLALVAMVGAGVTRNPLHCHRFWQQL-----------KGQpveftwqSEEGISLVAvlragPTESLIQ 446
Cdd:PRK09436 383 keGLLEPLEVEENLAIISVVGDGMRTHPGIAAKFFSALgraninivaiaQGS-------SERSISVVI-----DNDDATK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 447 GL---HQSLFRAEKRIGLVLFGKGNIGSRWLELFAREQTTLSARtGFEFILAGVVDSRRSLLNYEGLDASRALAFFNDEA 523
Cdd:PRK09436 451 ALracHQSFFLSDQVLDVFVIGVGGVGGALLEQIKRQQPWLKKK-NIDLRVCGIANSRKMLLDEHGIDLDNWREELAEAG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 524 VEQDEESLFLWMRAHPYDDLVVLDVTASAQLADQYLDFASHGFHVISANKLAGASSSSKYRQIHDAFEKTGRHWLYNATV 603
Cdd:PRK09436 530 EPFDLDRLIRLVKEYHLLNPVIVDCTSSQAVADQYADFLAAGFHVVTPNKKANTSSYAYYHQLREAARKSRRKFLYETNV 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 604 GAGLPVNHTVRDLIDSGDTILALSGIFSGTLSWLFLQFDGTVPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILARE 683
Cdd:PRK09436 610 GAGLPVIETLQNLLNAGDELLKFEGILSGSLSFIFGKLDEGMSFSEATRLAKEKGYTEPDPRDDLSGMDVARKLLILARE 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 684 AGYNIEPDQVRVESLVPAHC-EEGSVDHFFENGEALNEQMLQRLEAAREMGLVLRYVARFDaNGKARVGVEAVREEHPLA 762
Cdd:PRK09436 690 AGYELELEDIEVESVLPEEFdASGSVDEFMARLPELDAEFAARVAKARAEGKVLRYVGQIE-DGKCRVGIAEVDANHPLY 768
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 490994282 763 ALLPCDNVFAIESRWYRDNPLVIRGPGAGRDVTAGAIQSDINRLA 807
Cdd:PRK09436 769 KVKGGENALAFYTRYYQPIPLVLRGYGAGNEVTAAGVFADLLRTL 813
|
|
| AAK_AK-HSDH |
cd04257 |
AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal ... |
13-299 |
5.78e-121 |
|
AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK - homoserine dehydrogenase (HSDH). These aspartokinases are found in bacteria (E. coli AKI-HSDHI, ThrA and E. coli AKII-HSDHII, MetL) and higher plants (Z. mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains, located C-terminal to the AK catalytic domain, were shown to be involved in allosteric activation.
Pssm-ID: 239790 [Multi-domain] Cd Length: 294 Bit Score: 366.14 E-value: 5.78e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 13 QLHKFGGSSLADAKCYLRVAGIMTEYS-QAGDMMVVSAAGSTTNQLISWLKLSQTDRLSAHQVQQSLRRYQMELISGLLS 91
Cdd:cd04257 2 KVLKFGGTSLANAERIRRVADIILNAAkQEQVAVVVSAPGKVTDLLLELAELASSGDDAYEDILQELESKHLDLITELLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 92 PDAADTLIAIFIQDLERLAGLLDGGI-----TDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSFLRAERSAQP- 165
Cdd:cd04257 82 GDAAAELLSALGNDLEELKDLLEGIYllgelPDSIRAKVLSFGERLSARLLSALLNQQGLDAAWIDARELIVTDGGYLNa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 166 QVDEGLSYPLLQQLIAQHpNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVKD 245
Cdd:cd04257 162 VVDIELSKERIKAWFSSN-GKVIVVTGFIASNPQGETTTLGRNGSDYSAAILAALLDADQVEIWTDVDGVYSADPRKVKD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490994282 246 ACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIE 299
Cdd:cd04257 241 ARLLPSLSYQEAMELSYFGAKVLHPKTIQPVAKKNIPILIKNTFNPEAPGTLIS 294
|
|
| AAK_AK-HSDH-like |
cd04243 |
AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the ... |
13-298 |
1.22e-115 |
|
AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the N-terminal catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK- homoserine dehydrogenase (HSDH). These aspartokinases are found in such bacteria as E. coli (AKI-HSDHI, ThrA and AKII-HSDHII, MetL) and in higher plants (Z. mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains, located C-terminal to the AK catalytic domain, were shown to be involved in allosteric activation. Also included in this CD is the catalytic domain of the aspartokinase (AK) of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme (LysC) found in some bacteria such as E. coli. In E. coli, LysC is reported to be a homodimer of 50 kD subunits. Also included in this CD is the catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK - DAP decarboxylase (DapDC) found in some bacteria. DapDC, which is the lysA gene product, catalyzes the decarboxylation of DAP to lysine.
Pssm-ID: 239776 [Multi-domain] Cd Length: 293 Bit Score: 352.24 E-value: 1.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 13 QLHKFGGSSLADAKCYLRVAGIMTEYSQAGDMMVVSAAGSTTNQLISWLKLSQTDRLSAHQVQQSLRRYQMELISGLLSP 92
Cdd:cd04243 2 KVLKFGGTSVASAERIRRVADIIKSRASSPVLVVVSALGGVTNRLVALAELAASGDDAQAIVLQEIRERHLDLIKELLSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 93 DAADTLIAIFIQDLERLAGLLDG-----GITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSFLRAERSA-QPQ 166
Cdd:cd04243 82 ESAAELLAALDSLLERLKDLLEGirllgELSDKTRAEVLSFGELLSSRLMSAYLQEQGLPAAWLDARELLLTDDGFlNAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 167 VDEGLSYPLLQQLIAQHpNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVKDA 246
Cdd:cd04243 162 VDLKLSKERLAQLLAEH-GKVVVTQGFIASNEDGETTTLGRGGSDYSAALLAALLDAEEVEIWTDVDGVYTADPRKVPDA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490994282 247 CLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRI 298
Cdd:cd04243 241 RLLKELSYDEAMELAYFGAKVLHPRTIQPAIRKNIPIFIKNTFNPEAPGTLI 292
|
|
| MetL1 |
COG0527 |
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ... |
11-456 |
4.96e-110 |
|
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440293 [Multi-domain] Cd Length: 407 Bit Score: 342.06 E-value: 4.96e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 11 GRQLHKFGGSSLADAKCYLRVAGIMTEYSQAGD--MMVVSAAGSTTNQLISwlklsqtdrlsahqvqqslrryqmelisg 88
Cdd:COG0527 2 ALIVQKFGGTSVADAERIKRVADIVKKAKEAGNrvVVVVSAMGGVTDLLIA----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 89 llspdaadtliaifiqdlerLAGLLDGGITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSF-LRAERS-AQPQ 166
Cdd:COG0527 53 --------------------LAEELLGEPSPRELDMLLSTGEQLSAALLAMALQELGVPAVSLDGRQAgIITDDNhGKAR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 167 VDEGLSYPLLQQLIAQhpNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVKDA 246
Cdd:COG0527 113 IDLIETPERIRELLEE--GKVVVVAGFQGVTEDGEITTLGRGGSDTTAVALAAALKADECEIWTDVDGVYTADPRIVPDA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 247 CLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIERVLA-SGTGARIVTSHDDVCLIEFQVP 325
Cdd:COG0527 191 RKLPEISYEEMLELAYLGAKVLHPRAVEPAMKYNIPLRVRSTFNPDAPGTLITAEDEmEGPVVKGIASDKDIALITVSGV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 326 GGQDFKLAHKELDAILKRAQLRPLAVGVHADRKLLQFCYTSEVADSALKLLDEA---GLPGELRLRQKLALVAMVGAGVT 402
Cdd:COG0527 271 PMVDEPGFAARIFSALAEAGINVDMISQSSSETSISFTVPKSDLEKALEALEEElklEGLEEVEVEEDLAKVSIVGAGMR 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 490994282 403 RNPLHCHRFWQQL--KGQPVEFTWQSEEGISLVAVLRAGPTESLIQGLHQSLFRAE 456
Cdd:COG0527 351 SHPGVAARMFSALaeAGINIRMISQGSSEISISVVVDEEDAEKAVRALHEAFFLDK 406
|
|
| ThrA |
COG0460 |
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ... |
478-810 |
2.45e-88 |
|
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440228 [Multi-domain] Cd Length: 302 Bit Score: 281.16 E-value: 2.45e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 478 AREQTTLSARTGFEFILAGVVDSRRSllNYEGLDASRALAFFNDEAVeqdeeslflwMRAHPYDdlVVLDVTASAQLA-D 556
Cdd:COG0460 1 LENAEELARRLGLDLRVVGVAVRDGM--KPRGIDLPRWLLTTDLEEL----------IKDPEID--VVVELTGGSEPArE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 557 QYLDFASHGFHVISANKLAGASsssKYRQIHDAFEKTGRHWLYNATVGAGLPVNHTVRDLIdSGDTILALSGIFSGTLSW 636
Cdd:COG0460 67 LYLAALEAGKHVVTANKALLAE---HGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELL-AGDRITRIEGILNGTTNY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 637 LFLQFDGT-VPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAREA-GYNIEPDQVRVESLVpahceegSVDhffen 714
Cdd:COG0460 143 ILTKMEEEgLSFSEALKEAQELGYAEADPTADVEGIDAARKLAILARLAfGTPVELEDVYVEGIT-------RIT----- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 715 gealneqmLQRLEAAREMGLVLRYVARFDANG---KARVGVEAVREEHPLAALLPCDNVFAIESRWYRDnpLVIRGPGAG 791
Cdd:COG0460 211 --------AEDIAAAKELGYVIKLLAIAERTGggvEARVHPTLVPADHPLASVNGVDNAVLVETDAYGE--LMFYGPGAG 280
|
330
....*....|....*....
gi 490994282 792 RDVTAGAIQSDINRLAQLL 810
Cdd:COG0460 281 AEPTASAVLADLLDIARGL 299
|
|
| AAK_AK |
cd04234 |
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ... |
15-298 |
5.72e-74 |
|
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the N-terminal catalytic domain of aspartokinase (4-L-aspartate-4-phosphotransferase;). AK is the first enzyme in the biosynthetic pathway of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. It also catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. One mechanism for the regulation of this pathway is by the production of several isoenzymes of aspartokinase with different repressors and allosteric inhibitors. Pairs of ACT domains are proposed to specifically bind amino acids leading to allosteric regulation of the enzyme. In Escherichia coli, three different aspartokinase isoenzymes are regulated specifically by lysine, methionine, and threonine. AK-HSDHI (ThrA) and AK-HSDHII (MetL) are bifunctional enzymes that consist of an N-terminal AK and a C-terminal homoserine dehydrogenase (HSDH). ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. The third isoenzyme, AKIII (LysC), is monofunctional and is involved in lysine synthesis. The three Bacillus subtilis isoenzymes, AKI (DapG), AKII (LysC), and AKIII (YclM), are feedback-inhibited by meso-diaminopimelate, lysine, and lysine plus threonine, respectively. The E. coli lysine-sensitive AK is described as a homodimer, whereas, the B. subtilis lysine-sensitive AK is described as a heterodimeric complex of alpha- and beta- subunits that are formed from two in-frame overlapping genes. A single AK enzyme type has been described in Pseudomonas, Amycolatopsis, and Corynebacterium. The fungal aspartate pathway is regulated at the AK step, with L-Thr being an allosteric inhibitor of the Saccharomyces cerevisiae AK (Hom3). At least two distinct AK isoenzymes can occur in higher plants, one is a monofunctional lysine-sensitive isoenzyme, which is involved in the overall regulation of the pathway and can be synergistically inhibited by S-adenosylmethionine. The other isoenzyme is a bifunctional, threonine-sensitive AK-HSDH protein. Also included in this CD is the catalytic domain of the Methylomicrobium alcaliphilum ectoine AK, the first enzyme of the ectoine biosynthetic pathway, found in this bacterium, and several other halophilic/halotolerant bacteria.
Pssm-ID: 239767 [Multi-domain] Cd Length: 227 Bit Score: 240.45 E-value: 5.72e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 15 HKFGGSSLADAKCYLRVAGIMTEYS-QAGDMMVVSAAGSTTNQLISwlklsqtdrlsahqvqqslrryqmelisgllspd 93
Cdd:cd04234 4 QKFGGTSVASAERIKRVADIIKAYEkGNRVVVVVSAMGGVTDLLIE---------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 94 aadtliaifiqdlerlaglldggitdavYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSFLRA-ERSAQPQVDEGLS 172
Cdd:cd04234 50 ----------------------------LALLLSFGERLSARLLAAALRDRGIKARSLDARQAGITtDDNHGAARIIEIS 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 173 YPLLQQLIAQHpNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVKDACLLPLL 252
Cdd:cd04234 102 YERLKELLAEI-GKVPVVTGFIGRNEDGEITTLGRGGSDYSAAALAAALGADEVEIWTDVDGIYTADPRIVPEARLIPEI 180
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 490994282 253 RLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRI 298
Cdd:cd04234 181 SYDEALELAYFGAKVLHPRAVEPARKANIPIRVKNTFNPEAPGTLI 226
|
|
| asp_kinases |
TIGR00657 |
aspartate kinase; Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys ... |
16-453 |
4.11e-59 |
|
aspartate kinase; Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys (and its precursor diaminopimelate), Met, and Thr. In E. coli, a distinct isozyme is inhibited by each of the three amino acid products. The Met-sensitive (I) and Thr-sensitive (II) forms are bifunctional enzymes fused to homoserine dehydrogenases and form homotetramers, while the Lys-sensitive form (III) is a monofunctional homodimer.The Lys-sensitive enzyme of Bacillus subtilis resembles the E. coli form but is an alpha 2/beta 2 heterotetramer, where the beta subunit is translated from an in-phase alternative initiator at Met-246. This may be a feature of a number of closely related forms, including a paralog from B. subtilis. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273201 [Multi-domain] Cd Length: 441 Bit Score: 207.59 E-value: 4.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAKCYLRVAGIMTEYSQAGD--MMVVSAAGSTTNQLiswLKLSQtdRLSAHQVQQSLRRYQMELISGLlsPD 93
Cdd:TIGR00657 6 KFGGTSVGNAERIRRVAKIVLKEKKKGNqvVVVVSAMAGVTDAL---VELAE--QASPGPSKDFLEKIREKHIEIL--ER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 94 AADTLIAIFIQDLerLAGLLDGGITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWL-DAR-------SFLRAERSAQP 165
Cdd:TIGR00657 79 LIPQAIAEELKRL--LDAELVLEEKPREMDRILSFGERLSAALLSAALEELGVKAVSLlGGEagiltdsNFGRARVIIEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 166 QVDEGLsyPLLQQliaqhpNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVKD 245
Cdd:TIGR00657 157 LTERLE--PLLEE------GIIPVVAGFQGATEKGETTTLGRGGSDYTAALLAAALKADECEIYTDVDGIYTTDPRIVPD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 246 ACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIERVLASGTGARIVTSHDD----VCLIE 321
Cdd:TIGR00657 229 ARRIDEISYEEMLELASFGAKVLHPRTLEPAMRAKIPIVVKSTFNPEAPGTLIVASTKEMEEPIVKGLSLDrnqaRVTVS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 322 FQVPGGQDFkLAhkELDAILKRAQLRPLAVGVHADRKLLQFCYTSEVADSA---LKLLDEAGLPGELRLRQKLALVAMVG 398
Cdd:TIGR00657 309 GLGMKGPGF-LA--RVFGALAEAGINVDLISQSSSETSISFTVDKEDADQAkelLKSELNLSALSRVEVEKGLAKVSLVG 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 490994282 399 AGVTRNPLHCHRFWQQL--KGQPVEFTWQSEEGISLVAVLRAGptESLIQGLHQSLF 453
Cdd:TIGR00657 386 AGMKSAPGVASKIFEALaqNGINIEMISSSEINISFVVDEKDA--EKAVRLLHNALF 440
|
|
| AAK_AKiii-LysC-EC |
cd04258 |
AAK_AKiii-LysC-EC: Amino Acid Kinase Superfamily (AAK), AKiii-LysC-EC: this CD includes the ... |
16-298 |
5.03e-53 |
|
AAK_AKiii-LysC-EC: Amino Acid Kinase Superfamily (AAK), AKiii-LysC-EC: this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive aspartokinase isoenzyme AKIII. AKIII is a monofunctional class enzyme (LysC) found in some bacteria such as E. coli. Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. In E. coli, LysC is reported to be a homodimer of 50 kD subunits.
Pssm-ID: 239791 [Multi-domain] Cd Length: 292 Bit Score: 186.03 E-value: 5.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAKCYLRVAGIMTEYSQAGdMMVVSAAGSTTNQLISWLKLSQT-DRLSAHQVQQSLRRYQMELISGLLSPDA 94
Cdd:cd04258 5 KFGGTSVADYAAMLRCAAIVKSDASVR-LVVVSASAGVTNLLVALADAAESgEEIESIPQLHEIRAIHFAILNRLGAPEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 95 ADTLIAIFIQDLERLAG--LLDGGITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSFLRAER---SAQPQVDE 169
Cdd:cd04258 84 LRAKLEELLEELTQLAEgaALLGELSPASRDELLSFGERMSSLLFSEALREQGVPAEWFDVRTVLRTDSrfgRAAPDLNA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 170 glSYPLLQQLIAQHPNKRLVVT-GFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVKDACL 248
Cdd:cd04258 164 --LAELAAKLLKPLLAGTVVVTqGFIGSTEKGRTTTLGRGGSDYSAALLAEALHAEELQIWTDVAGIYTTDPRICPAARA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 490994282 249 LPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRI 298
Cdd:cd04258 242 IKEISFAEAAEMATFGAKVLHPATLLPAIRKNIPVFVGSSKDPEAGGTLI 291
|
|
| PRK09084 |
PRK09084 |
aspartate kinase III; Validated |
16-300 |
6.19e-52 |
|
aspartate kinase III; Validated
Pssm-ID: 236376 [Multi-domain] Cd Length: 448 Bit Score: 187.72 E-value: 6.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAKCYLRVAGIMTEYSQAGdMMVVSAAGSTTNQLISWLKLSQTDRLSAHQVQQsLRRYQMELISGLLSPDAA 95
Cdd:PRK09084 5 KFGGTSVADFDAMNRSADIVLSNPNTR-LVVLSASAGVTNLLVALAEGAEPGDERLALLDE-IRQIQYAILDRLGDPNVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 96 DTLIAIFIQDLERLAGLLDGGITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSFLRAERS---AQPQVDEglS 172
Cdd:PRK09084 83 REEIERLLENITVLAEAASLATSPALTDELVSHGELMSTLLFVELLRERGVQAEWFDVRKVMRTDDRfgrAEPDVAA--L 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 173 YPLLQQLIAQHPNKRLVVT-GFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVKDACLLPL 251
Cdd:PRK09084 161 AELAQEQLLPLLAEGVVVTqGFIGSDEKGRTTTLGRGGSDYSAALLAEALNASRVEIWTDVPGIYTTDPRIVPAAKRIDE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490994282 252 LRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIER 300
Cdd:PRK09084 241 ISFEEAAEMATFGAKVLHPATLLPAVRSNIPVFVGSSKDPEAGGTWICN 289
|
|
| Homoserine_dh |
pfam00742 |
Homoserine dehydrogenase; |
608-803 |
5.19e-50 |
|
Homoserine dehydrogenase;
Pssm-ID: 459921 [Multi-domain] Cd Length: 178 Bit Score: 173.33 E-value: 5.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 608 PVNHTVRdLIDSGDTILALSGIFSGTLSWLFLQFDGT-VPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAREA-G 685
Cdd:pfam00742 1 PIIRTLR-LSLAGDRITRIEGILNGTTNYILTRMEEEgLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAfG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 686 YNIEPDQVRVESLVpahceegsvdhffengeALNEQMlqrLEAAREMGLVLRYVA---RFDANGKARVGVEAVREEHPLA 762
Cdd:pfam00742 80 LDVELEDVEVEGIT-----------------RLTAED---IAYAKELGKVIKLVAsakRDDGGVEARVGPTLVPKDHPLA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490994282 763 ALLPCDNVFAIESRWYrdNPLVIRGPGAGRDVTAGAIQSDI 803
Cdd:pfam00742 140 SVKGVDNAVVIETDRY--GELVFYGPGAGALPTASAVLADL 178
|
|
| PLN02700 |
PLN02700 |
homoserine dehydrogenase family protein |
457-803 |
9.77e-50 |
|
homoserine dehydrogenase family protein
Pssm-ID: 215377 [Multi-domain] Cd Length: 377 Bit Score: 179.58 E-value: 9.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 457 KRIGLVLFGKGNIGSRWLELFAREQTtLSARTGFEFILAGVVDSRRSLL----NYEGLD--------------------- 511
Cdd:PLN02700 2 KKIPVLLLGCGGVGRHLLRHIVSCRS-LHAKQGVRIRVVGVCDSKSLVLaedvLNEELDdallsevclakskgsplsalg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 512 --ASRALAFFNDEAVEQDEESLFLWMRAHPyddLVVLDVTASAQLADQYLDFASHGFHVISANKLAGASSSSKYRQIHDA 589
Cdd:PLN02700 81 alAGGCQVFNNSELSRKVIDIATLLGKSTG---LVVVDCSASMETIGALNEAVDLGCCIVLANKKPLTSTLEDYDKLAAH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 590 FektgRHWLYNATVGAGLPVNHTVRDLIDSGDTILALSGIFSGTLSWLFLQFDGTVPFTDLVDQAWQQGLTEPDPRVDLS 669
Cdd:PLN02700 158 P----RRIRHESTVGAGLPVIASLNRILSSGDPVHRIVGSLSGTLGYVMSELEDGKPFSEVVKQAKSLGYTEPDPRDDLG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 670 GKDVMRKLVILAREAGYNIEPDQVRVESLVPAHCEEG--SVDHFFENGEA-LNEQMLQRLEAAREMGLVLRYVARFDANG 746
Cdd:PLN02700 234 GMDVARKALILARLLGKRINMDSIKVESLYPEEMGPDlmSTDDFLHSGLVeLDLPIEERVKEASLKGCVLRYVCVIEGSS 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490994282 747 kARVGVEAVREEHPLAALLPCDNVFAIESRWYRDNPLVIRGPGAGRDVTAGAIQSDI 803
Cdd:PLN02700 314 -CQVGIRELPKDSALGRLRGSDNVVEIYSRCYSEQPLVIQGAGAGNDTTAAGVLADI 369
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
16-320 |
4.62e-46 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 177.58 E-value: 4.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAKCYLRVAGIMTEYSQAGD--MMVVSAAGSTTNQLIswlKLSQTDRLSAH-QVQQSLRRYQMELISGL-LS 91
Cdd:PRK08961 13 KFGGTSVSRRHRWDTIAKIVRKRLAEGGrvLVVVSALSGVSNELE---AIIAAAGAGDSaSRVAAIRQRHRELLAELgVD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 92 PDAadtLIAifiQDLERLAGLLDG-----GITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSFLRAerSAQPQ 166
Cdd:PRK08961 90 AEA---VLA---ERLAALQRLLDGiraltRASLRWQAEVLGQGELLSTTLGAAYLEASGLDMGWLDAREWLTA--LPQPN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 167 VDEGLSY-----------PLLQQLIAQhPNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGV 235
Cdd:PRK08961 162 QSEWSQYlsvscqwqsdpALRERFAAQ-PAQVLITQGFIARNADGGTALLGRGGSDTSAAYFAAKLGASRVEIWTDVPGM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 236 YSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIERVLASGTGARIVTSHD 315
Cdd:PRK08961 241 FSANPKEVPDARLLTRLDYDEAQEIATTGAKVLHPRSIKPCRDAGIPMAILDTERPDLSGTSIDGDAEPVPGVKAISRKN 320
|
....*
gi 490994282 316 DVCLI 320
Cdd:PRK08961 321 GIVLV 325
|
|
| AAK_AK-LysC-like |
cd04244 |
AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the ... |
16-299 |
2.22e-44 |
|
AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive AK isoenzyme found in higher plants. The lysine-sensitive AK isoenzyme is a monofunctional protein. It is involved in the overall regulation of the aspartate pathway and can be synergistically inhibited by S-adenosylmethionine. Also included in this CD is an uncharacterized LysC-like AK found in Euryarchaeota and some bacteria. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP.
Pssm-ID: 239777 [Multi-domain] Cd Length: 298 Bit Score: 162.16 E-value: 2.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAKCYLRVAGIMTEYSQAGDMMVV-SAAGSTTNQLISWLKLSQTDRLS-AHQVQQSLRRYQMELISGLLSPD 93
Cdd:cd04244 5 KFGGTSVGSAERIRHVADLVGTYAEGHEVVVVvSAMGGVTDRLLLAAEAAVSGRIAgVKDFIEILRLRHIKAAKEAISDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 94 AADTLIAIFIQDLERLAGLLDGgitDAVYAEV--------VGHGEVWSARLMAAVLNHLGVEAAWLDA--------RSFL 157
Cdd:cd04244 85 EIAEVESIIDSLLEELEKLLYG---IAYLGELtprsrdyiVSFGERLSAPIFSAALRSLGIKARALDGgeagiitdDNFG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 158 RAErsAQPQVDEGLSYPLLQQLIAQHPnkrLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYS 237
Cdd:cd04244 162 NAR--PLPATYERVRKRLLPMLEDGKI---PVVTGFIGATEDGAITTLGRGGSDYSATIIGAALDADEIWIWKDVDGVMT 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490994282 238 ADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIE 299
Cdd:cd04244 237 ADPRIVPEARTIPRLSYAEAMELAYFGAKVLHPRTVEPAMEKGIPVRVKNTFNPEAPGTLIT 298
|
|
| asp_kin_monofn |
TIGR00656 |
aspartate kinase, monofunctional class; This model describes a subclass of aspartate kinases. ... |
16-405 |
1.23e-43 |
|
aspartate kinase, monofunctional class; This model describes a subclass of aspartate kinases. These are mostly Lys-sensitive and not fused to homoserine dehydrogenase, unlike some Thr-sensitive and Met-sensitive forms. Homoserine dehydrogenase is part of Thr and Met but not Lys biosynthetic pathways. Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys (and its precursor diaminopimelate), Met, and Thr. In E. coli, a distinct isozyme is inhibited by each of the three amino acid products. The Met-sensitive (I) and Thr-sensitive (II) forms are bifunctional enzymes fused to homoserine dehydrogenases and form homotetramers, while the Lys-sensitive form (III) is a monofunctional homodimer. The Lys-sensitive enzyme of Bacillus subtilis resembles the E. coli form but is an alpha 2/beta 2 heterotetramer, where the beta subunit is translated from an in-phase alternative initiator at Met-246. The protein slr0657 from Synechocystis PCC6803 is extended by a duplication of the C-terminal region corresponding to the beta chain. Incorporation of a second copy of the C-terminal domain may be quite common in this subgroup of aspartokinases. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273200 [Multi-domain] Cd Length: 400 Bit Score: 162.94 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAKCYLRVAGIMTEYSQAGD--MMVVSAAGSTTNQLISwlklsqtdrlsahqvqqslrryqmelisglLSPD 93
Cdd:TIGR00656 6 KFGGTSVGSGERIKNAARIVLKEKMKGHkvVVVVSAMGGVTDELVS------------------------------LAEE 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 94 AadtliaifIQDlerlaglldgGITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARS--------FLRAErsaqp 165
Cdd:TIGR00656 56 A--------ISD----------EISPRERDELVSHGELLSSALFSSALRELGVKAIWLDGGEagirtddnFGNAK----- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 166 qVDEGLSYPLLQQLIAQHpnKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVKD 245
Cdd:TIGR00656 113 -IDIIATEERLLPLLEEG--IIVVVAGFQGATEKGDTTTLGRGGSDYTAALLAAALKADRVDIYTDVPGVYTTDPRVVEA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 246 ACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGsTRIERVLASGTGARIVTSHDDVCLieFQVP 325
Cdd:TIGR00656 190 AKRIDKISYEEALELATFGAKVLHPRTVEPAMRSKVPIEVRSSFDPSEG-TLITNSMENPPLVKGIALRKNVTR--VTVH 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 326 GGqdfKLAHK-----ELDAILKRAQLRPLAVGVHADRKLLQFCYTSEVADSALKLLDEAGLPGELR---LRQKLALVAMV 397
Cdd:TIGR00656 267 GL---GMLGKrgflaEIFGALAERNINVDLISQTPSETSISLTVDTTDADEAVRALKDQSGAAELDrveVEEGLAKVSIV 343
|
....*...
gi 490994282 398 GAGVTRNP 405
Cdd:TIGR00656 344 GAGMVGAP 351
|
|
| AAK_AK-DapDC |
cd04259 |
AAK_AK-DapDC: Amino Acid Kinase Superfamily (AAK), AK-DapDC; this CD includes the N-terminal ... |
16-298 |
2.54e-43 |
|
AAK_AK-DapDC: Amino Acid Kinase Superfamily (AAK), AK-DapDC; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the bifunctional enzyme AK - DAP decarboxylase (DapDC) found in some bacteria. Aspartokinase is the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. DapDC, which is the lysA gene product, catalyzes the decarboxylation of DAP to lysine.
Pssm-ID: 239792 [Multi-domain] Cd Length: 295 Bit Score: 158.86 E-value: 2.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAKCYLRVAGIMTEYSQAGD--MMVVSAAGSTTNQLIswlKLSQTDRLSAHQVQ-QSLRRYQMELISGLLSp 92
Cdd:cd04259 5 KFGGTSVSSRARWDTIAKLAQKHLNTGGqpLIVCSALSGISNKLE---ALIDQALLDEHHSLfNAIQSRHLNLAEQLEV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 93 dAADTLIAifiQDLERLAGLLDG-----GITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSFLRAersAQPQV 167
Cdd:cd04259 81 -DADALLA---NDLAQLQRWLTGisllkQASPRTRAEVLALGELMSTRLGAAYLEAQGLKVKWLDARELLTA---TPTLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 168 DEGLSY-----------PLLQQLIAQhpNKRLVVT-GFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGV 235
Cdd:cd04259 154 GETMNYlsarceseyadALLQKRLAD--GAQLIITqGFIARNAHGETVLLGRGGSDTSAAYFAAKLQAARCEIWTDVPGL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490994282 236 YSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRI 298
Cdd:cd04259 232 FTANPHEVPHARLLKRLDYDEAQEIATMGAKVLHPRCIPPARRANIPMVVRSTERPELSGTLI 294
|
|
| PRK06291 |
PRK06291 |
aspartate kinase; Provisional |
16-320 |
1.49e-36 |
|
aspartate kinase; Provisional
Pssm-ID: 235773 [Multi-domain] Cd Length: 465 Bit Score: 143.91 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAKCYLRVAGIMTEYSQAGD--MMVVSAAGSTTNQLISWLK--LSQTDRLSAHQVQQSLRRYQMELISGLL- 90
Cdd:PRK06291 6 KFGGTSVGDGERIRHVAKLVKRYRSEGNevVVVVSAMTGVTDALLEIAEqaLDVRDIAKVKDFIADLRERHYKAIEEAIk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 91 SPDAADTLIAIFIQDLERLAGLLDG-----GITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDAR--------SFL 157
Cdd:PRK06291 86 DPDIREEVSKTIDSRIEELEKALVGvsylgELTPRSRDYILSFGERLSAPILSGALRDLGIKSVALTGGeagiitdsNFG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 158 RAE--RSAQPQVDEGLSyPLLQQliaqhpNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGV 235
Cdd:PRK06291 166 NARplPKTYERVKERLE-PLLKE------GVIPVVTGFIGETEEGIITTLGRGGSDYSAAIIGAALDADEIWIWTDVDGV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 236 YSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIER-VLASGTGARIVTSH 314
Cdd:PRK06291 239 MTTDPRIVPEARVIPKISYIEAMELSYFGAKVLHPRTIEPAMEKGIPVRVKNTFNPEFPGTLITSdSESSKRVVKAVTLI 318
|
....*.
gi 490994282 315 DDVCLI 320
Cdd:PRK06291 319 KNVALI 324
|
|
| PRK05925 |
PRK05925 |
aspartate kinase; Provisional |
14-461 |
1.08e-34 |
|
aspartate kinase; Provisional
Pssm-ID: 235646 [Multi-domain] Cd Length: 440 Bit Score: 138.02 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 14 LHKFGGSSLADAKCYLRVAGIMTEysQAGDMMVVSAAGSTTNQLISWLKLSQTDRlsaHQVQQSLRRYQMELISGLlspd 93
Cdd:PRK05925 5 VYKFGGTSLGTAESIRRVCDIICK--EKPSFVVVSAVAGVTDLLEEFCRLSKGKR---EALTEKIREKHEEIAKEL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 94 AADTLIAIFIQDLERLAGLLDggITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSFLRAE---RSAQPQVDeg 170
Cdd:PRK05925 76 GIEFSLSPWWERLEHFEDVEE--ISSEDQARILAIGEDISASLICAYCCTYVLPLEFLEARQVILTDdqyLRAVPDLA-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 171 LSYPLLQQLIAQHpNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVKDACLLP 250
Cdd:PRK05925 152 LMQTAWHELALQE-DAIYIMQGFIGANSSGKTTVLGRGGSDFSASLIAELCKAREVRIYTDVNGIYTMDPKIIKDAQLIP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 251 LLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIERVLASGT-GARI----VTSHDDVCLIEFQVP 325
Cdd:PRK05925 231 ELSFEEMQNLASFGAKVLHPPMLKPCVRAGIPIFVTSTFDVTKGGTWIYASDKEVSyEPRIkalsLKQNQALWSVDYNSL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 326 GGQDFklahKELDAILKRAQLRP-------LAVGVHADRKLLqfcyTSEVADSALKLLDEAGLpgeLRLRQKLALVAMVG 398
Cdd:PRK05925 311 GLVRL----EDVLGILRSLGIVPglvmaqnLGVYFTIDDDDI----SEEYPQHLTDALSAFGT---VSCEGPLALITMIG 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490994282 399 AG-----VTRNPLHCHRFWQqlkgQPVeFTW-QSEEGISLVAVLRAGptESLIQGLHQSLFRaEKRIGL 461
Cdd:PRK05925 380 AKlaswkVVRTFTEKLRGYQ----TPV-FCWcQSDMALNLVVNEELA--VAVTELLHNDYVK-QKFSVV 440
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
12-286 |
3.22e-34 |
|
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: 130.95 E-value: 3.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 12 RQLHKFGGSSLADAKCYLRVAGIMTEYSQAG-DMMVVSAAGSTTNQLISWLKLSQtdrlsahqvqqslrryqmelisgll 90
Cdd:pfam00696 2 RVVIKLGGSSLTDKERLKRLADEIAALLEEGrKLVVVHGGGAFADGLLALLGLSP------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 91 spdaadtliaifiqdlERLAGLLDGGITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSFLRAERsaqpqVDEG 170
Cdd:pfam00696 57 ----------------RFARLTDAETLEVATMDALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDD-----VVTR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 171 LSYPLLQQLIAQhpNKRLVVTGFISRNNAGETvllGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVKDACLLP 250
Cdd:pfam00696 116 IDTEALEELLEA--GVVPVITGFIGIDPEGEL---GRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIP 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490994282 251 LLRLDEA-----SELARLAAPVLHARTLQPVSGSDIDLQLR 286
Cdd:pfam00696 191 EISYDELlellaSGLATGGMKVKLPAALEAARRGGIPVVIV 231
|
|
| PLN02551 |
PLN02551 |
aspartokinase |
1-315 |
1.04e-33 |
|
aspartokinase
Pssm-ID: 178166 [Multi-domain] Cd Length: 521 Bit Score: 136.40 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 1 MSVIAQAGAKGRQL---HKFGGSSLADAKCYLRVAGIMTEYSQAGDMMVVSAAGSTTNQLISWLKLS---QTDRLSAHQV 74
Cdd:PLN02551 39 PSETRQGGGTEKQLtvvMKFGGSSVASAERMREVADLILSFPDERPVVVLSAMGKTTNNLLLAGEKAvscGVTNVSEIEE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 75 QQSLRRYQMELISGL-LSPDAADTLiaifiqdLERLAGLLDG-----GITDAVYAEVVGHGEVWSARLMAAVLNHLGVEA 148
Cdd:PLN02551 119 LSAIRELHLRTADELgVDESVVEKL-------LDELEQLLKGiammkELTPRTRDYLVSFGERMSTRIFAAYLNKIGVKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 149 AWLDA--RSFLRAERSAQPQVDEGlSYPLLQQLIAQ---HPNKRLVVTGFISRN-NAGETVLLGRNGSDYSATQIGALAG 222
Cdd:PLN02551 192 RQYDAfdIGFITTDDFTNADILEA-TYPAVAKRLHGdwiDDPAVPVVTGFLGKGwKTGAITTLGRGGSDLTATTIGKALG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 223 ASRVTIWSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRI---- 298
Cdd:PLN02551 271 LREIQVWKDVDGVLTCDPRIYPNAVPVPYLTFDEAAELAYFGAQVLHPQSMRPAREGDIPVRVKNSYNPTAPGTLItktr 350
|
330 340
....*....|....*....|
gi 490994282 299 ---ERVLASGTGARIVTSHD 315
Cdd:PLN02551 351 dmsKAVLTSIVLKRNVTMLD 370
|
|
| AAK_AKiii-YclM-BS |
cd04245 |
AAK_AKiii-YclM-BS: Amino Acid Kinase Superfamily (AAK), AKiii-YclM-BS; this CD includes the ... |
16-298 |
1.36e-33 |
|
AAK_AKiii-YclM-BS: Amino Acid Kinase Superfamily (AAK), AKiii-YclM-BS; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine plus threonine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme found in Bacilli (Bacillus subtilis YclM) and Clostridia species. Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. In Bacillus subtilis (BS), YclM is reported to be a single polypeptide of 50 kD. The Bacillus subtilis 168 AKIII is induced by lysine and repressed by threonine, and it is synergistically inhibited by lysine and threonine.
Pssm-ID: 239778 [Multi-domain] Cd Length: 288 Bit Score: 130.86 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAKCYLRVAGIMTEySQAGDMMVVSAAGSTTNQ-------LISWLKLSQTDRLSAHQVQQSLRRYQmELISG 88
Cdd:cd04245 5 KFGGSSLASAEQFQKVKAIVKA-DPERKIVVVSAPGKRFKDdtkvtdlLILYAEAVLAGEDTESIFEAIVDRYA-EIADE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 89 LLSPDAADTLIAIFIQDLERLagllDGGITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSF--LRAERSAQPQ 166
Cdd:cd04245 83 LGLPMSILEEIAEILENLANL----DYANPDYLLDALKARGEYLNAQLMAAYLNYQGIDARYVIPKDAglVVTDEPGNAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 167 VDEGlSYPLLQQLIAqhPNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVKDA 246
Cdd:cd04245 159 ILPE-SYQKIKKLRD--SDEKLVIPGFYGYSKNGDIKTFSRGGSDITGAILARGFQADLYENFTDVDGIYAANPRIVANP 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490994282 247 CLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRI 298
Cdd:cd04245 236 KPISEMTYREMRELSYAGFSVFHDEALIPAIEAGIPINIKNTNHPEAPGTLI 287
|
|
| AAK_AK-DapG-like |
cd04246 |
AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the ... |
16-298 |
1.70e-33 |
|
AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the diaminopimelate-sensitive aspartokinase isoenzyme AKI (DapG), a monofunctional enzymes found in Bacilli (Bacillus subtilis 168), Clostridia, and Actinobacteria bacterial species, as well as, the catalytic AK domain of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis 168, the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related isoenzymes. In Bacillus subtilis, the regulation of the diaminopimelate-lysine biosynthetic pathway involves dual control by diaminopimelate and lysine, effected through separate diaminopimelate- and lysine-sensitive aspartokinase isoenzymes. The role of the AKI isoenzyme is most likely to provide a constant level of aspartyl-beta-phosphate for the biosynthesis of diaminopimelate for peptidoglycan synthesis and dipicolinate during sporulation. The B. subtilis 168 AKII is induced by methionine, and repressed and inhibited by lysine. In Corynebacterium glutamicum and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and threonine. Also included in this CD are the aspartokinases of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single aspartokinase isoenzyme types found in Pseudomonas, C. glutamicum, and Amycolatopsis lactamdurans. The B. subtilis AKI is tetrameric consisting of two alpha and two beta subunits; the alpha (43 kD) and beta (17 kD) subunit formed by two in-phase overlapping genes. The alpha subunit contains the AK catalytic domain and two ACT domains. The beta subunit contains two ACT domains. The B. subtilis 168 AKII aspartokinase is also described as tetrameric consisting of two alpha and two beta subunits. Some archeal aspartokinases in this group lack recognizable ACT domains.
Pssm-ID: 239779 [Multi-domain] Cd Length: 239 Bit Score: 129.15 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAKCYLRVAGIMTEYSQAGD--MMVVSAAGSTTNQLISWlklsqtdrlsAHQvqqslrryqmelISGLLSPD 93
Cdd:cd04246 5 KFGGTSVADIERIKRVAERIKKAVKKGYqvVVVVSAMGGTTDELIGL----------AKE------------VSPRPSPR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 94 AADTLIAIfiqdlerlaglldggitdavyaevvghGEVWSARLMAAVLNHLGVeaawlDARSFLRAE---------RSAQ 164
Cdd:cd04246 63 ELDMLLST---------------------------GEQISAALLAMALNRLGI-----KAISLTGWQagiltddhhGNAR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 165 -PQVDEGLSYPLLQQliaqhpNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKV 243
Cdd:cd04246 111 iIDIDPKRILEALEE------GDVVVVAGFQGVNEDGEITTLGRGGSDTTAVALAAALKADRCEIYTDVDGVYTADPRIV 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490994282 244 KDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGsTRI 298
Cdd:cd04246 185 PKARKLDVISYDEMLEMASLGAKVLHPRSVELAKKYNVPLRVRSSFSENPG-TLI 238
|
|
| AAK_AKii-LysC-BS |
cd04261 |
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal ... |
15-294 |
5.26e-33 |
|
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis 168, and the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related sequences. In B. subtilis 168, the regulation of the diaminopimelate (Dap)-lysine biosynthetic pathway involves dual control by Dap and lysine, effected through separate Dap- and lysine-sensitive aspartokinase isoenzymes. The B. subtilis 168 AKII is induced by methionine, and repressed and inhibited by lysine. Although Corynebacterium glutamicum is known to contain a single aspartokinase isoenzyme type, both the succinylase and dehydrogenase variant pathways of DAP-lysine synthesis operate simultaneously in this organism. In this organism and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and theronine. Also included in this CD are the aspartokinases of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single aspartokinases found in Pseudomons, C. glutamicum, and Amycolatopsis lactamdurans. B. subtilis 168 AKII, and the C. glutamicum, Streptomyces clavuligerus and A. lactamdurans aspartokinases are described as tetramers consisting of two alpha and two beta subunits; the alpha (44 kD) and beta (18 kD) subunits formed by two in-phase overlapping polypeptides.
Pssm-ID: 239794 [Multi-domain] Cd Length: 239 Bit Score: 127.65 E-value: 5.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 15 HKFGGSSLADAKCYLRVAGIMTEYSQAGD--MMVVSAAGSTTNQLISWlklsqtdrlsAHQVQQSLRRYQMelisgllsp 92
Cdd:cd04261 4 QKFGGTSVASIERIKRVAERIKKRKKKGNqvVVVVSAMGGTTDELIEL----------AKEISPRPPAREL--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 93 daaDTLIAIfiqdlerlaglldggitdavyaevvghGEVWSARLMAAVLNHLGVeaawlDARSFLRAE----------RS 162
Cdd:cd04261 65 ---DVLLST---------------------------GEQVSIALLAMALNRLGI-----KAISLTGWQagiltdghhgKA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 163 AQPQVDEGLsyplLQQLIAQhpNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRK 242
Cdd:cd04261 110 RIIDIDPDR----IRELLEE--GDVVIVAGFQGINEDGDITTLGRGGSDTSAVALAAALGADRCEIYTDVDGVYTADPRI 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490994282 243 VKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQG 294
Cdd:cd04261 184 VPKARKLDEISYDEMLEMASLGAKVLHPRSVELAKKYGVPLRVLSSFSEEPG 235
|
|
| PRK06635 |
PRK06635 |
aspartate kinase; Reviewed |
15-400 |
1.43e-31 |
|
aspartate kinase; Reviewed
Pssm-ID: 235843 [Multi-domain] Cd Length: 404 Bit Score: 127.92 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 15 HKFGGSSLADAKCYLRVAGIMTEYSQAGDMM--VVSAAGSTTNQLISWlklsqtdrlsAHQVQQSlrryqmelisgllsP 92
Cdd:PRK06635 6 QKFGGTSVGDVERIKRVAERVKAEVEAGHQVvvVVSAMGGTTDELLDL----------AKEVSPL--------------P 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 93 DAADtliaifiqdlerlaglldggitdavYAEVVGHGEVWSARLMAAVLNHLGVeaawlDARSFL--------------- 157
Cdd:PRK06635 62 DPRE-------------------------LDMLLSTGEQVSVALLAMALQSLGV-----KARSFTgwqagiitdsahgka 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 158 RAErsaqpQVDEGLsyplLQQLIAQhpNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYS 237
Cdd:PRK06635 112 RIT-----DIDPSR----IREALDE--GDVVVVAGFQGVDEDGEITTLGRGGSDTTAVALAAALKADECEIYTDVDGVYT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 238 ADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQG-------STRIERVLASGtgari 310
Cdd:PRK06635 181 TDPRIVPKARKLDKISYEEMLELASLGAKVLHPRSVEYAKKYNVPLRVRSSFSDNPGtlitgeeEEIMEQPVVTG----- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 311 VTSHDDVCLIEF----QVPG--GQDFK-LAHKEL--DAILKraqlrplavGVHADRKL-LQFCYTSEVADSALKLL---- 376
Cdd:PRK06635 256 IAFDKDEAKVTVvgvpDKPGiaAQIFGaLAEANInvDMIVQ---------NVSEDGKTdITFTVPRDDLEKALELLeevk 326
|
410 420
....*....|....*....|....
gi 490994282 377 DEAGLpGELRLRQKLALVAMVGAG 400
Cdd:PRK06635 327 DEIGA-ESVTYDDDIAKVSVVGVG 349
|
|
| PRK06270 |
PRK06270 |
homoserine dehydrogenase; Provisional |
457-803 |
1.87e-30 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235763 [Multi-domain] Cd Length: 341 Bit Score: 123.05 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 457 KRIGLVLFGKGNIGSRWLELFAREQTTLSARTGFEFILAGVVDSRRSLLNYEGLDASRALAF-FNDEAVEQDEESLFLW- 534
Cdd:PRK06270 1 MEMKIALIGFGGVGQGVAELLAEKREYLKKRYGLDLKVVAIADSSGSAIDPDGLDLELALKVkEETGKLADYPEGGGEIs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 535 ----MRAHPYDdlVVLDVT----ASAQLADQYLDFA-SHGFHVISANK--LAGAsssskYRQIHDAFEKTGRHWLYNATV 603
Cdd:PRK06270 81 glevIRSVDAD--VVVEATptniETGEPALSHCRKAlERGKHVVTSNKgpLALA-----YKELKELAKKNGVRFRYEATV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 604 GAGLPVNHTVRDLIdSGDTILALSGIFSGTLSWLFLQFD-GTVPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAR 682
Cdd:PRK06270 154 GGAMPIINLAKETL-AGNDIKSIKGILNGTTNYILTRMEeEGLSYEQALAEAQELGYAEADPTYDVEGIDAALKVVILAN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 683 EA-GYNIEPDQVRVE---SLVPahceegsvdhffengEAlneqmlqrLEAAREMGLVLRYVARFDANGKARVGVEAVREE 758
Cdd:PRK06270 233 SIlGADLTIKDVEVEgitKITP---------------EA--------IELAAKEGYRIKLIGEVSREKDLSVSPRLVPLD 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 490994282 759 HPLA---ALlpcdNVFAIESrwyrD--NPLVIRGPGAGRDVTAGAIQSDI 803
Cdd:PRK06270 290 HPLAvsgTL----NAATFET----DlaGDVTVVGRGAGSIETASAILSDL 331
|
|
| PRK09034 |
PRK09034 |
aspartate kinase; Reviewed |
16-298 |
1.54e-27 |
|
aspartate kinase; Reviewed
Pssm-ID: 236364 [Multi-domain] Cd Length: 454 Bit Score: 116.82 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAKCYLRVAGIMTEysqagD----MMVVSAAGS-------TTNQLISWLKLSQTDRLSAHQVQQSLRRYQmE 84
Cdd:PRK09034 5 KFGGSSLASAEQFKKVLNIVKS-----DperkIVVVSAPGKrfkedtkVTDLLILYAEAVLAGEDYEDIFEAIIARYA-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 85 LISGLLSPDAADTLIAIFIQDLERLAGLLDGGITDAVYAevvgHGEVWSARLMAAVLNHLGVEAAWLDAR---SFLRAEr 161
Cdd:PRK09034 79 IAKELGLDADILEKIEEILEHLANLASRNPDRLLDAFKA----RGEDLNAKLIAAYLNYEGIPARYVDPKeagIIVTDE- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 162 SAQPQVDEGlSYPLLQQLiaQHPNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPR 241
Cdd:PRK09034 154 PGNAQVLPE-SYDNLKKL--RDRDEKLVIPGFFGVTKDGQIVTFSRGGSDITGAILARGVKADLYENFTDVDGIYAANPR 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 490994282 242 KVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRI 298
Cdd:PRK09034 231 IVKNPKSIKEITYREMRELSYAGFSVFHDEALIPAYRGGIPINIKNTNNPEDPGTLI 287
|
|
| PRK08373 |
PRK08373 |
aspartate kinase; Validated |
16-278 |
6.18e-27 |
|
aspartate kinase; Validated
Pssm-ID: 236250 [Multi-domain] Cd Length: 341 Bit Score: 112.84 E-value: 6.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAkcyLRVAGIMTEYSQAGD--MMVVSAAGSTTNQLIswlKLSQT-DRLSAHQVQQSLRRYQMELisgllsp 92
Cdd:PRK08373 9 KFGGSSVRYD---FEEALELVKYLSEENevVVVVSALKGVTDKLL---KLAETfDKEALEEIEEIHEEFAKRL------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 93 daaDTLIAIFIQDLERLAGLLDGGITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSFLRAERS-AQPQVDEGL 171
Cdd:PRK08373 76 ---GIDLEILSPYLKKLFNSRPDLPSEALRDYILSFGERLSAVLFAEALENEGIKGKVVDPWEILEAKGSfGNAFIDIKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 172 SYPLLQQLIAQHPNKRL-VVTGFISRNNaGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVKDACLLP 250
Cdd:PRK08373 153 SKRNVKILYELLERGRVpVVPGFIGNLN-GFRATLGRGGSDYSAVALGVLLNAKAVLIMSDVEGIYTADPKLVPSARLIP 231
|
250 260
....*....|....*....|....*...
gi 490994282 251 LLRLDEASELARLAAPVLHARTLQPVSG 278
Cdd:PRK08373 232 YLSYDEALIAAKLGMKALHWKAIEPVKG 259
|
|
| AAK_AK-Hom3 |
cd04247 |
AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal ... |
16-276 |
4.86e-24 |
|
AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal catalytic domain of the aspartokinase HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae and other related AK domains. Aspartokinase, the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and in fungi, is responsible for the production of threonine, isoleucine and methionine. S. cerevisiae has a single aspartokinase isoenzyme type, which is regulated by feedback, allosteric inhibition by L-threonine. Recent studies show that the allosteric transition triggered by binding of threonine to AK involves a large change in the conformation of the native hexameric enzyme that is converted to an inactive one of different shape and substantially smaller hydrodynamic size.
Pssm-ID: 239780 [Multi-domain] Cd Length: 306 Bit Score: 103.28 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLAdaKCYLRVAG-IMTEYSQAGDMMVVSAAGS-------TTNQLISWLKLSQTDRLSA-HQVQQSLRRYQMELI 86
Cdd:cd04247 6 KFGGTSVG--KFPDNIADdIVKAYLKGNKVAVVCSARStgtkaegTTNRLLQAADEALDAQEKAfHDIVEDIRSDHLAAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 87 -SGLLSPDAADTLIAIFIQDLERLAGLLD-----GGITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARSFLRAE 160
Cdd:cd04247 84 rKFIKNPELQAELEEEINKECELLRKYLEaakilSEISPRTKDLVISTGEKLSCRFMAAVLRDRGVDAEYVDLSHIVDLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 161 RSAQpQVDEGLSYPLLQQL---IAQHPNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYS 237
Cdd:cd04247 164 FSIE-ALDQTFYDELAQVLgekITACENRVPVVTGFFGNVPGGLLSQIGRGYTDLCAALCAVGLNADELQIWKEVDGIFT 242
|
250 260 270
....*....|....*....|....*....|....*....
gi 490994282 238 ADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPV 276
Cdd:cd04247 243 ADPRKVPTARLLPSITPEEAAELTYYGSEVIHPFTMEQV 281
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
16-310 |
7.21e-24 |
|
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: 101.36 E-value: 7.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAKCYLRVAGIMTEY-SQAGDMMVVSAAGSTTNQLISwlklsqtdrlsahqvqqslrryqmelisgllspda 94
Cdd:cd02115 3 KFGGSSVSSEERLRNLARILVKLaSEGGRVVVVHGAGPQITDELL----------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 95 adtliaifiqDLERLAGLLDG-GITDAVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDARS--FLRAERSAQPQVDEgL 171
Cdd:cd02115 48 ----------AHGELLGYARGlRITDRETDALAAMGEGMSNLLIAAALEQHGIKAVPLDLTQagFASPNQGHVGKITK-V 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 172 SYPLLQQLIAQhpNKRLVVTGFISRNNAGETVLlGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVKDACLLPL 251
Cdd:cd02115 117 STDRLKSLLEN--GILPILSGFGGTDEKETGTL-GRGGSDSTAALLAAALKADRLVILTDVDGVYTADPRKVPDAKLLSE 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 490994282 252 LRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQgstrIERVLASGTGARI 310
Cdd:cd02115 194 LTYEEAAELAYAGAMVLKPKAADPAARAGIPVRIANTENPGA----LALFTPDGGGTLI 248
|
|
| AAK_AKi-DapG-BS |
cd04260 |
AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the ... |
16-298 |
7.29e-23 |
|
AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the diaminopimelate-sensitive aspartokinase isoenzyme AKI (DapG), a monofunctional class enzyme found in Bacilli (Bacillus subtilis 168), Clostridia, and Actinobacteria bacterial species. In Bacillus subtilis, the regulation of the diaminopimelate-lysine biosynthetic pathway involves dual control by diaminopimelate and lysine, effected through separate diaminopimelate- and lysine-sensitive aspartokinase isoenzymes. AKI activity is invariant during the exponential and stationary phases of growth and is not altered by addition of amino acids to the growth medium. The role of this isoenzyme is most likely to provide a constant level of aspartyl-beta-phosphate for the biosynthesis of diaminopimelate for peptidoglycan synthesis and dipicolinate during sporulation. The B. subtilis AKI is tetrameric consisting of two alpha and two beta subunits; the alpha (43 kD) and beta (17 kD) subunit formed by two in-phase overlapping genes. The alpha subunit contains the AK catalytic domain and two ACT domains. The beta subunit contains two ACT domains.
Pssm-ID: 239793 [Multi-domain] Cd Length: 244 Bit Score: 98.23 E-value: 7.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAKCYLRVAGIMTEYSQAGD--MMVVSAAGSttnqliswlklsqtdrlsahqvqqslrryqmeliSGllSPD 93
Cdd:cd04260 5 KFGGTSVSTKERREQVAKKVKQAVDEGYkpVVVVSAMGR----------------------------------KG--DPY 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 94 AADTLIAIFIQDLERLAGL-LDggitdavyaEVVGHGEVWSARLMAAVLNHLGVEAAWL---DArSFLRAERSAQPQVDE 169
Cdd:cd04260 49 ATDTLINLVYAENSDISPReLD---------LLMSCGEIISAVVLTSTLRAQGLKAVALtgaQA-GILTDDNYSNAKIIK 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 170 GLSYPLLQQLIAqhpNKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKVKDACLL 249
Cdd:cd04260 119 VNPKKILSALKE---GDVVVVAGFQGVTEDGEVTTLGRGGSDTTAAALGAALNAEYVEIYTDVDGIMTADPRVVPNARIL 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490994282 250 PLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGsTRI 298
Cdd:cd04260 196 DVVSYNEVFQMAHQGAKVIHPRAVEIAMQANIPIRIRSTMSENPG-TLI 243
|
|
| NAD_binding_3 |
pfam03447 |
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ... |
465-600 |
1.55e-22 |
|
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model.
Pssm-ID: 281446 [Multi-domain] Cd Length: 116 Bit Score: 93.14 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 465 GKGNIGSRWLELFAREQTTLSARtgfefiLAGVVDSRrsllnyegLDASRALAFFNDEAVEQDEESLFLWMRAhpydDLV 544
Cdd:pfam03447 1 GCGAIGSGVLEQLLRQQSEIPLE------LVAVADRD--------LLSKDPLALLPDEPLTLDLDDLIAHPDP----DVV 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 490994282 545 VlDVTASAQLADQYLDFASHGFHVISANKLAGAsSSSKYRQIHDAFEKTGRHWLYN 600
Cdd:pfam03447 63 V-ECASSEAVAELVLDALKAGKDVVTASKGALA-DLALYEELREAAEANGARIYVE 116
|
|
| PRK08374 |
PRK08374 |
homoserine dehydrogenase; Provisional |
457-807 |
2.08e-21 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 169409 [Multi-domain] Cd Length: 336 Bit Score: 96.41 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 457 KRIGLVLFGKGNIGSRWLELFAREQTTLSARTGFEFILAGVVDSRRSLLNYEGLDASRAL----------AFFND-EAVE 525
Cdd:PRK08374 1 MEVKVSIFGFGNVGRAVAEVLAEKSRVFKERYGVELKVVSITDTSGTIWLPEDIDLREAKevkenfgklsNWGNDyEVYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 526 QDEESLFLWMRAHpyddlVVLDVTASAQLADQYLDFASHGFHVISANKLAGASSsskYRQIHDAFEKTGRHWLYNATVGA 605
Cdd:PRK08374 81 FSPEEIVEEIDAD-----IVVDVTNDKNAHEWHLEALKEGKSVVTSNKPPIAFH---YDELLDLANERNLPYLFEATVMA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 606 GLPVNHTVRDLIdSGDTILALSGIFSGTLSWLFLQFDGTVPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAREAG 685
Cdd:PRK08374 153 GTPIIGLLRENL-LGDTVKRIEAVVNATTTFILTRMEQGKTFEEALKEAQTLGIAERDPSKDIDGIDAGYKATILHWVAF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 686 YNIEPDQVRVESLVPAHCEEgsvdhffengealneqmlqrLEAAREMGLVLRYVARFDaNGKARVGVEAVREEHPLAaLL 765
Cdd:PRK08374 232 PPITFEEVGIRGIKDVTEGE--------------------IERAKAKGRNVRLVATVE-EGRISVKPKKLPENSPLA-VE 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 490994282 766 PCDNVFAIESrwyrDN--PLVIRGPGAGRDVTAGAIQSDINRLA 807
Cdd:PRK08374 290 GVENAAVIKT----DLlgELVLKGPGAGGKETASGVVTDIIKAA 329
|
|
| PRK08210 |
PRK08210 |
aspartate kinase I; Reviewed |
1-402 |
3.63e-21 |
|
aspartate kinase I; Reviewed
Pssm-ID: 236188 [Multi-domain] Cd Length: 403 Bit Score: 96.85 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 1 MSVIAQagakgrqlhKFGGSSLADAKCYLRVAGIMTEYSQAGDM--MVVSAAGS-----TTNQLISWLKLSQTDrlsahq 73
Cdd:PRK08210 1 MKIIVQ---------KFGGTSVSTEERRKMAVNKIKKALKEGYKvvVVVSAMGRkgdpyATDTLLSLVGEEFSE------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 74 vqqslrryqmelisglLSPDAADTLIAIfiqdlerlaglldggitdavyaevvghGEVWSARLMAAVLNHLGVEAAWL-- 151
Cdd:PRK08210 66 ----------------ISKREQDLLMSC---------------------------GEIISSVVFSNMLNENGIKAVALtg 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 152 ------------DARsFLRAErsaqPQvdeglsypLLQQLIAQHpnKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGA 219
Cdd:PRK08210 103 gqagiitddnftNAK-IIEVN----PD--------RILEALEEG--DVVVVAGFQGVTENGDITTLGRGGSDTTAAALGV 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 220 LAGASRVTIWSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGsTRIE 299
Cdd:PRK08210 168 ALKAEYVDIYTDVDGIMTADPRIVEDARLLDVVSYNEVFQMAYQGAKVIHPRAVEIAMQANIPLRIRSTYSDSPG-TLIT 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 300 RVLASGTGA----RIVT--SH-DDVclIEFQVPGGQDFKLAHKELDAILKRAQLRPLAVGVHADRKLlqFCYTSEVADSA 372
Cdd:PRK08210 247 SLGDAKGGIdveeRLITgiAHvSNV--TQIKVKAKENAYDLQQEVFKALAEAGISVDFINIFPTEVV--FTVSDEDSEKA 322
|
410 420 430
....*....|....*....|....*....|
gi 490994282 373 LKLLDEAGLpgELRLRQKLALVAMVGAGVT 402
Cdd:PRK08210 323 KEILENLGL--KPSVRENCAKVSIVGAGMA 350
|
|
| PRK07431 |
PRK07431 |
aspartate kinase; Provisional |
1-298 |
2.33e-20 |
|
aspartate kinase; Provisional
Pssm-ID: 236018 [Multi-domain] Cd Length: 587 Bit Score: 95.76 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 1 MSVIAQagakgrqlhKFGGSSLADAKCYLRVAGIMTEYSQAGD--MMVVSAAGSTTNQLiswLKLsqtdrlsAHQVQQSL 78
Cdd:PRK07431 1 MALIVQ---------KFGGTSVGSVERIQAVAQRIARTKEAGNdvVVVVSAMGKTTDEL---VKL-------AKEISSNP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 79 RRYQMELisgLLSPdaadtliaifiqdlerlaglldggitdavyaevvghGEVWSARLMAAVLNHLGVEAAWLDA----- 153
Cdd:PRK07431 62 PRREMDM---LLST------------------------------------GEQVSIALLSMALHELGQPAISLTGaqvgi 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 154 ---RSFLRAE-RSAQPQvdeglsypLLQQLIAQhpNKRLVVTGF--ISRNNAGETVLLGRNGSDYSATQIGALAGASRVT 227
Cdd:PRK07431 103 vteSEHGRARiLEIKTD--------RIQRHLDA--GKVVVVAGFqgISLSSNLEITTLGRGGSDTSAVALAAALGADACE 172
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490994282 228 IWSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTpDQGSTRI 298
Cdd:PRK07431 173 IYTDVPGVLTTDPRLVPEAQLMDEISCDEMLELASLGASVLHPRAVEIARNYGVPLVVRSSWS-DAPGTLV 242
|
|
| AspKin_pair |
TIGR02078 |
Pyrococcus aspartate kinase subunit, putative; This family consists of proteins restricted to ... |
16-281 |
1.40e-18 |
|
Pyrococcus aspartate kinase subunit, putative; This family consists of proteins restricted to and found as paralogous pairs (typically close together) in species of Pyrococcus, a hyperthermophilic archaeal genus. Members are always found close to other genes of threonine biosynthesis and appear to represent the Pyrococcal form of aspartate kinase. Alignment to aspartokinase III from E. coli shows that 300 N-terminal and 20 C-terminal amino acids are homologous, but the form in Pyrococcus lacks ~ 100 amino acids in between. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 131133 Cd Length: 327 Bit Score: 87.54 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSL-ADAKCYLRVAGIMTEYSQAgdMMVVSAAGSTTNQLIswlKLSQT-DRLSAHQVQQSLRRYQMELISGL--LS 91
Cdd:TIGR02078 5 KFGGSSVrYAFEEALELVKSLSEEKRV--IVVVSALKGITDCLI---RYANTfDKSAALEIEEIYEEFAKELGVDLniLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 92 PdaadtliaiFIQDLERLAGLLDGGITDavyaEVVGHGEVWSARLMAAvlnhlGVEAAWLDARSFLRAERS-AQPQVD-- 168
Cdd:TIGR02078 80 P---------YLKELFNPPDLPKEALRD----YILSLGERLSAVIFAE-----GINGKVVDPWDIFFAKGDfGNAFIDik 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 169 -----EGLSYPLLQQliaqhpNKRLVVTGFISRNNaGETVLLGRNGSDYSATQIGALAGASRVTIWSDVAGVYSADPRKV 243
Cdd:TIGR02078 142 kskrnAKILYEVLES------GKIPVIPGFYGNLN-GYRVTLGRGGSDYSAVALGVLLNSKLVAIMSDVEGIFTADPKLV 214
|
250 260 270
....*....|....*....|....*....|....*...
gi 490994282 244 KDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDI 281
Cdd:TIGR02078 215 PSARLIPYLSYEEIKIAAKLGMKALQWKAADLAKEYKI 252
|
|
| PRK06392 |
PRK06392 |
homoserine dehydrogenase; Provisional |
459-681 |
1.41e-18 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 102354 [Multi-domain] Cd Length: 326 Bit Score: 87.62 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 459 IGLVLFGKGNIGSRWLEL---FAREQttlsaRTGFEFILAGVVDSRRSLLNYEGLDASRALAFFNDEAVEQDEESLFLWM 535
Cdd:PRK06392 1 IRISIIGLGNVGLNVLRIiksRNDDR-----RNNNGISVVSVSDSKLSYYNERGLDIGKIISYKEKGRLEEIDYEKIKFD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 536 RAHPYDDLVVLDVTASAQLADQ----YLDFASHGFHVISANKlagASSSSKYRQIHDAFEKTGRHWLYNATVGAGLPVnH 611
Cdd:PRK06392 76 EIFEIKPDVIVDVTPASKDGIReknlYINAFEHGIDVVTANK---SGLANHWHDIMDSASKNRRIIRYEATVAGGVPL-F 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 612 TVRDLIDSGDTILALSGIFSGTLSWLFLQFDGTVPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILA 681
Cdd:PRK06392 152 SLRDYSTLPSRIKNFRGIVSSTINYVIRQEANGRGFLDVVKIAQKMGIAETNYSDDLMGLDAARKSVILA 221
|
|
| PRK08841 |
PRK08841 |
aspartate kinase; Validated |
129-295 |
1.10e-13 |
|
aspartate kinase; Validated
Pssm-ID: 181563 [Multi-domain] Cd Length: 392 Bit Score: 73.63 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 129 GEVWSARLMAAVLNHLGVEAAWLDA-RSFLRAERSAQPQVDEGLSYPLLQQLIAQhpNKRLVVTGFISRNNAGETVLLGR 207
Cdd:PRK08841 73 GEQVSMALLAMTLNKLGYAARSLTGaQANIVTDNQHNDATIKHIDTSTITELLEQ--DQIVIVAGFQGRNENGDITTLGR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 208 NGSDYSATqigALAGASRVT---IWSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQ 284
Cdd:PRK08841 151 GGSDTTAV---ALAGALNADecqIFTDVDGVYTCDPRVVKNARKLDVIDFPSMEAMARKGAKVLHLPSVQHAWKHSVPLR 227
|
170
....*....|.
gi 490994282 285 LRCSYTPDQGS 295
Cdd:PRK08841 228 VLSSFEVGEGT 238
|
|
| PRK06349 |
PRK06349 |
homoserine dehydrogenase; Provisional |
457-803 |
1.84e-13 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235783 [Multi-domain] Cd Length: 426 Bit Score: 73.18 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 457 KRIGLVLFGKGNIGSRWLELFAREQTTLSARTGFEFILAGVVDsrRSLLNYEGLDASRALaFFND-EAVEQDEESlflwm 535
Cdd:PRK06349 2 KPLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAV--RDLEKDRGVDLPGIL-LTTDpEELVNDPDI----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 536 rahpydDLVVlDVTASAQLADQYLDFA-SHGFHVISANK--LAgassssKYRQ-IHDAFEKTGRHWLYNATVGAGLPVNH 611
Cdd:PRK06349 74 ------DIVV-ELMGGIEPARELILKAlEAGKHVVTANKalLA------VHGAeLFAAAEEKGVDLYFEAAVAGGIPIIK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 612 TVRD-LidSGDTILALSGIFSGT----LSWLFLqfDGTvPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAREA-G 685
Cdd:PRK06349 141 ALREgL--AANRITRVMGIVNGTtnyiLTKMTE--EGL-SFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAfG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 686 YNIEPDQVRVE---SLVPAhceegsvDhffengealneqmlqrLEAAREMGLVLRY--VARFDANG-KARVGVEAVREEH 759
Cdd:PRK06349 216 TRVDFDDVYVEgisKITAE-------D----------------IAYAKELGYRIKLlgIAERTEEGiELRVHPTLIPKSH 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 490994282 760 PLAALlpcDNVF---AIESrwyrDN--PLVIRGPGAGRDVTAGAIQSDI 803
Cdd:PRK06349 273 PLANV---NGVMnavFVEG----DAvgETMFYGPGAGGLPTASAVVADL 314
|
|
| AAK_AK-Ectoine |
cd04248 |
AAK_AK-Ectoine: Amino Acid Kinase Superfamily (AAK), AK-Ectoine; this CD includes the ... |
16-298 |
1.32e-05 |
|
AAK_AK-Ectoine: Amino Acid Kinase Superfamily (AAK), AK-Ectoine; this CD includes the N-terminal catalytic domain of the aspartokinase of the ectoine (1,4,5,6-tetrahydro-2-methyl pyrimidine-4-carboxylate) biosynthetic pathway found in Methylomicrobium alcaliphilum, Vibrio cholerae, and other various halotolerant or halophilic bacteria. Bacteria exposed to hyperosmotic stress accumulate organic solutes called 'compatible solutes' of which ectoine, a heterocyclic amino acid, is one. Apart from its osmotic function, ectoine also exhibits a protective effect on proteins, nucleic acids and membranes against a variety of stress factors. de novo synthesis of ectoine starts with the phosphorylation of L-aspartate and shares its first two enzymatic steps with the biosynthesis of amino acids of the aspartate family: aspartokinase and L-aspartate-semialdehyde dehydrogenase. The M. alcaliphilum and the V. cholerae aspartokinases are encoded on the ectABCask operon.
Pssm-ID: 239781 [Multi-domain] Cd Length: 304 Bit Score: 47.83 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 16 KFGGSSLADAKCYLRVAGIMTEYSQAGDMMVVSAAGSTTNQLISWLKLSQTD------------RLSAHQVQQSLRRYQM 83
Cdd:cd04248 5 KIGGTSMSAFGAVLDNIILKPDSDLYGRVFVVSAYSGVTNALLEHKKTGAPGiyqhfvdadeawREALSALKQAMLKINE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 84 ELISGLLSPDAADTLIAIFIQD----LERLAGLLDGGITD------AVYAEVVGHGEVWSARLMAAVLNHLGVEAAWLDA 153
Cdd:cd04248 85 AFADIGLDVEQADAFIGARIQDaracLHDLARLCSSGYFSlaehllAARELLASLGEAHSAFNTALLLQNRGVNARFVDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 154 rSFLRAERsaQPQVDEGLSypllQQLIAQHPNKRL-VVTGFiSRNNAGETVLLGRNGSDYSATQIGALAGASRVTIWSDV 232
Cdd:cd04248 165 -SGWRDSG--DMTLDERIS----EAFRDIDPRDELpIVTGY-AKCAEGLMREFDRGYSEMTFSRIAVLTGASEAIIHKEF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994282 233 AgVYSADPRKVKDACLLPLLR--LDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRI 298
Cdd:cd04248 237 H-LSSADPKLVGEDKARPIGRtnYDVADQLANLGMEAIHPKAAKGLRQAGIPLRVKNTFEPDHPGTLI 303
|
|
| ACT_AK-like_2 |
cd04892 |
ACT domains C-terminal to the catalytic domain of aspartokinase (AK; ... |
392-453 |
1.34e-05 |
|
ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase); This CD includes the second of two ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). The exception in this group, is the inclusion of the first ACT domain of the bifunctional aspartokinase - homoserine dehydrogenase-like enzyme group (ACT_AKi-HSDH-ThrA-like_1) which includes the monofunctional, threonine-sensitive, aspartokinase found in Methanococcus jannaschii and other related archaeal species. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. AK is the first enzyme in the pathway of the biosynthesis of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. One mechanism for the regulation of this pathway is by the production of several isoenzymes of AK with different repressors and allosteric inhibitors. Pairs of ACT domains are proposed to specifically bind amino acids leading to allosteric regulation of the enzyme. In Escherichia coli (EC), three different AK isoenzymes are regulated specifically by lysine, methionine, and threonine. AK-HSDHI (ThrA) and AK-HSDHII (MetL) are bifunctional enzymes that consist of an N-terminal AK and a C-terminal homoserine dehydrogenase (HSDH). ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. The third isoenzyme, AKIII (LysC), is monofunctional and is involved in lysine synthesis. The three Bacillus subtilis (BS) isoenzymes, AKI (DapG), AKII (LysC), and AKIII (YclM), are feedback inhibited by meso-diaminopimelate, lysine, and lysine plus threonine, respectively. The E. coli lysine-sensitive AK is described as a homodimer, whereas, the B. subtilis lysine-sensitive AK is described as is a heterodimeric complex of alpha- and beta- subunits that are formed from two in-frame overlapping genes. A single AK enzyme type has been described in Pseudomonas, Amycolatopsis, and Corynebacterium, and apparently, unique to cyanobacteria, are AKs with two tandem pairs of ACT domains, C-terminal to the catalytic domain. The fungal aspartate pathway is regulated at the AK step, with L-Thr being an allosteric inhibitor of the Saccharomyces cerevisiae AK (Hom3). At least two distinct AK isoenzymes can occur in higher plants, a monofunctional lysine-sensitive isoenzyme, which is involved in the overall regulation of the pathway and can be synergistically inhibited by S-adenosylmethionine. The other isoenzyme is a bifunctional, threonine-sensitive AK-HSDH protein. Also included in this CD are the ACT domains of the Methylomicrobium alcaliphilum AK; the first enzyme of the ectoine biosynthetic pathway found in this bacterium and several other halophilic/halotolerant bacteria. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153164 [Multi-domain] Cd Length: 65 Bit Score: 43.25 E-value: 1.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490994282 392 ALVAMVGAGVTRNPLHCHRFWQQL--KGQPVEFTWQSEEGISLVAVLRAGPTESLIQGLHQSLF 453
Cdd:cd04892 1 ALVSVVGAGMRGTPGVAARIFSALaeAGINIIMISQGSSEVNISFVVDEDDADKAVKALHEEFF 64
|
|
| pyrH_bact |
TIGR02075 |
uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a ... |
136-257 |
1.14e-03 |
|
uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a phosphate from ATP. It is the first step in pyrimidine biosynthesis. GTP is an allosteric activator. In a large fraction of all bacterial genomes, the gene tends to be located immediately downstream of elongation factor Ts and upstream of ribosome recycling factor. A related protein family, believed to be equivalent in function and found in the archaea and in spirochetes, is described by a separate model, TIGR02076. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 213681 [Multi-domain] Cd Length: 232 Bit Score: 41.46 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 136 LMAAVLNHLGVEAAWLDARSFlraersaqPQVDEglsyPLLQQLIAQHPNKRLVVtgfisrnnagetVLLGRNGS----- 210
Cdd:TIGR02075 82 ALRDALEKLGLKTRVLSAISM--------PQICE----SYIRRKAIKHLEKGKVV------------IFSGGTGNpfftt 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 490994282 211 DYSATQIGALAGASRVTIWSDVAGVYSADPRKVKDACLLPLLRLDEA 257
Cdd:TIGR02075 138 DTAAALRAIEINADVILKGTNVDGVYTADPKKNKDAKKYDTITYNEA 184
|
|
| AAK_UMPK-like |
cd04239 |
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ... |
134-260 |
2.11e-03 |
|
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays a key role in pyrimidine nucleotide biosynthesis. Regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinases of E. coli (Ec) and Pyrococcus furiosus (Pf) are known to function as homohexamers, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Also included in this CD are the alpha and beta subunits of the Mo storage protein (MosA and MosB) characterized as an alpha4-beta4 octamer containing an ATP-dependent, polynuclear molybdenum-oxide cluster. These and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK).
Pssm-ID: 239772 [Multi-domain] Cd Length: 229 Bit Score: 40.60 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994282 134 ARLMAAVLNHLGVEAAWLDARSFlraersaqPQVDEGLSYpllqQLIAQHPNK-RLVVTGFISRNnAGETvllgrngSDY 212
Cdd:cd04239 77 ALALQDALEKLGVKTRVMSAIPM--------QGVAEPYIR----RRAIRHLEKgRIVIFGGGTGN-PGFT-------TDT 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 490994282 213 SATQIGALAGASRVTIWSDVAGVYSADPRKVKDACLLPLLRLDEASEL 260
Cdd:cd04239 137 AAALRAEEIGADVLLKATNVDGVYDADPKKNPDAKKYDRISYDELLKK 184
|
|
| |
