|
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: 1577.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 1 MSVIAQAGAKGRQLHKFGGSSLADVKCYLRVAGIMTEYSQPGDMMVVSAAGSTTNQLISWLKLSQTDRLSAHQVQQSLRR 80
Cdd:PRK09466 1 MSVIAQAGAMGRQLHKFGGSSLADAKCYRRVAGILAEYSQPDDLVVVSAAGKTTNQLISWLKLSQTDRLSAHQVQQTLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 81 YQSELIAGLLPADVADGLISAFTHDLERLAALLDSGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDFLRAE 160
Cdd:PRK09466 81 YQQDLIEGLLPAEQARSLLSRLISDLERLAALLDGGINDAQYAEVVGHGEVWSARLMAALLNQQGLPAAWLDARSFLRAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 161 RAAQPQVDEGLSYPLLQQLLVQHPGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADP 240
Cdd:PRK09466 161 RAAQPQVDEGLSYPLLQQLLAQHPGKRLVVTGFISRNEAGETVLLGRNGSDYSATLIGALAGVERVTIWSDVAGVYSADP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 241 RKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIERVLASGTGARIVTSHDDICLI 320
Cdd:PRK09466 241 RKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYQPEQGSTRIERVLASGTGARIVTSLDDVCLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 321 EFQVPAGQDFKLAHKDIDLVLKRAQVRPLAVGVHNDRQLLQFCYTAEVADSALKILDEAGLPGELRLRQGLALVAMVGAG 400
Cdd:PRK09466 321 ELQVPASHDFKLAQKELDQLLKRAQLRPLAVGVHPDRQLLQLAYTSEVADSALKLLDDAALPGELKLREGLALVALVGAG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 401 VTRNPLHCHRFWQQLKGQPVEFTWQSEEGISLVAVLRKGPTESLIQGLHTSLFRAEKRIGLVLFGKGNIGSRWLELFARE 480
Cdd:PRK09466 401 VTRNPLHCHRFYQQLKDQPVEFIWQSEDGLSLVAVLRQGPTESLIQGLHQSLFRAEKRIGLVLFGKGNIGSRWLELFARE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 481 QVTLSARTGFEFILAGVVDSRRSLLNYEGLDASRALAFFNDEAVEQDEESLFLWMRAHPYDDLVVLDVTASEQLADQYLD 560
Cdd:PRK09466 481 QSTLSARTGFEFVLVGVVDSRRSLLNYDGLDASRALAFFDDEAVEWDEESLFLWLRAHPYDELVVLDVTASEQLALQYPD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 561 FASHGFHVISANKLAGASSTDKYRQIHDAFEKTGRHWLYNATVGAGLPVNHTVRDLIESGDSILALSGIFSGTLSWLFLQ 640
Cdd:PRK09466 561 FASHGFHVISANKLAGSSPSNFYRQIKDAFAKTGRHWLYNATVGAGLPINHTVRDLRNSGDSILAISGIFSGTLSWLFLQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 641 FDGTVPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAREAGYDIEPDAVRVESLVPAGCEEGSVDHFFENGEELNE 720
Cdd:PRK09466 641 FDGSVPFSELVDQAWQQGLTEPDPRDDLSGRDVMRKLVILAREAGYEIEPDDVRVESLVPAHLEDGSLDQFFENGDELDE 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 721 QMVQRLEAANEMGLVLRYVARFEANGKARVGVEAVRPEHPLAALLPCDNVFAIESRWYRDNPLVIRGPGAGRDVTAGAIQ 800
Cdd:PRK09466 721 QMLQRLEAAAEQGKVLRYVARFDANGKARVGVEAVRPDHPLANLLPCDNVFAIESRWYRDNPLVIRGPGAGREVTAGAIQ 800
|
810
....*....|
gi 829777911 801 SDINRLAKLL 810
Cdd:PRK09466 801 SDLNRLAQLL 810
|
|
| thrA |
PRK09436 |
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional |
15-808 |
0e+00 |
|
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional
Pssm-ID: 181856 [Multi-domain] Cd Length: 819 Bit Score: 582.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 15 HKFGGSSLADVKCYLRVAGIMTEYSQPGDMMVV-SAAGSTTNQLISWLKLSQTDRLSAHQVQQSLRRYQSEL--IAGLLP 91
Cdd:PRK09436 4 LKFGGTSVANAERFLRVADIIESNARQEQVAVVlSAPAKVTNHLVAMIEKAAKGDDAYPEILDAERIFHELLdgLAAALP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 92 ADVADGLISAFTHDLERLAALLDsGI------TDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDFLRAERA-AQ 164
Cdd:PRK09436 84 GFDLAQLKAKVDQEFAQLKDILH-GIsllgecPDSVNAAIISRGERLSIAIMAAVLEARGHDVTVIDPRELLLADGHyLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 165 PQVDEGLSYPLLQQLLVQHPgKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVK 244
Cdd:PRK09436 163 STVDIAESTRRIAASFIPAD-HVILMPGFTAGNEKGELVTLGRNGSDYSAAILAACLDADCCEIWTDVDGVYTADPRVVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 245 DACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIERvlASGTGARIV---TSHDDICLIE 321
Cdd:PRK09436 242 DARLLKSLSYQEAMELSYFGAKVLHPRTIAPIAQFQIPCLIKNTFNPQAPGTLIGA--ESDEDSLPVkgiSNLNNMAMFN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 322 FQVP--------AGQDFK-LAHKDIDLVLkraqvrplavgvhndrqLLQ--------FCYTAEVADSALKILDEA----- 379
Cdd:PRK09436 320 VSGPgmkgmvgmASRVFAaLSRAGISVVL-----------------ITQssseysisFCVPQSDAAKAKRALEEEfalel 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 380 --GLPGELRLRQGLALVAMVGAGVTRNPLHCHRFWQQL-----------KGqpveftwQSEEGISLV---AVLRKGptes 443
Cdd:PRK09436 383 keGLLEPLEVEENLAIISVVGDGMRTHPGIAAKFFSALgraninivaiaQG-------SSERSISVVidnDDATKA---- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 444 lIQGLHTSLFRAEKRIGLVLFGKGNIGSRWLELFAREQVTLSARtGFEFILAGVVDSRRSLLNYEGLDASRALAFFNDEA 523
Cdd:PRK09436 452 -LRACHQSFFLSDQVLDVFVIGVGGVGGALLEQIKRQQPWLKKK-NIDLRVCGIANSRKMLLDEHGIDLDNWREELAEAG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 524 VEQDEESLFLWMRAHPYDDLVVLDVTASEQLADQYLDFASHGFHVISANKLAGASSTDKYRQIHDAFEKTGRHWLYNATV 603
Cdd:PRK09436 530 EPFDLDRLIRLVKEYHLLNPVIVDCTSSQAVADQYADFLAAGFHVVTPNKKANTSSYAYYHQLREAARKSRRKFLYETNV 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 604 GAGLPVNHTVRDLIESGDSILALSGIFSGTLSWLFLQFDGTVPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILARE 683
Cdd:PRK09436 610 GAGLPVIETLQNLLNAGDELLKFEGILSGSLSFIFGKLDEGMSFSEATRLAKEKGYTEPDPRDDLSGMDVARKLLILARE 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 684 AGYDIEPDAVRVESLVPAGC-EEGSVDHFFENGEELNEQMVQRLEAANEMGLVLRYVARFEaNGKARVGVEAVRPEHPLA 762
Cdd:PRK09436 690 AGYELELEDIEVESVLPEEFdASGSVDEFMARLPELDAEFAARVAKARAEGKVLRYVGQIE-DGKCRVGIAEVDANHPLY 768
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 829777911 763 ALLPCDNVFAIESRWYRDNPLVIRGPGAGRDVTAGAIQSDINRLAK 808
Cdd:PRK09436 769 KVKGGENALAFYTRYYQPIPLVLRGYGAGNEVTAAGVFADLLRTLS 814
|
|
| AAK_AK-HSDH |
cd04257 |
AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal ... |
13-299 |
1.08e-120 |
|
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: 365.37 E-value: 1.08e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 13 QLHKFGGSSLADVKCYLRVAGIMTEYS-QPGDMMVVSAAGSTTNQLISWLKLSQTDRLSAHQVQQSLRRYQSELIAGLLP 91
Cdd:cd04257 2 KVLKFGGTSLANAERIRRVADIILNAAkQEQVAVVVSAPGKVTDLLLELAELASSGDDAYEDILQELESKHLDLITELLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 92 ADVADGLISAFTHDLERLAALLDSGI-----TDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDFLRAERAAQP- 165
Cdd:cd04257 82 GDAAAELLSALGNDLEELKDLLEGIYllgelPDSIRAKVLSFGERLSARLLSALLNQQGLDAAWIDARELIVTDGGYLNa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 166 QVDEGLSYPLLQQLLVQHpGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKD 245
Cdd:cd04257 162 VVDIELSKERIKAWFSSN-GKVIVVTGFIASNPQGETTTLGRNGSDYSAAILAALLDADQVEIWTDVDGVYSADPRKVKD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 829777911 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 |
3.78e-114 |
|
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: 348.39 E-value: 3.78e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 13 QLHKFGGSSLADVKCYLRVAGIMTEYSQPGDMMVVSAAGSTTNQLISWLKLSQTDRLSAHQVQQSLRRYQSELIAGLLPA 92
Cdd:cd04243 2 KVLKFGGTSVASAERIRRVADIIKSRASSPVLVVVSALGGVTNRLVALAELAASGDDAQAIVLQEIRERHLDLIKELLSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 93 DVADGLISAFTHDLERLAALLDS-----GITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDFLRAERAA-QPQ 166
Cdd:cd04243 82 ESAAELLAALDSLLERLKDLLEGirllgELSDKTRAEVLSFGELLSSRLMSAYLQEQGLPAAWLDARELLLTDDGFlNAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 167 VDEGLSYPLLQQLLVQHpGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDA 246
Cdd:cd04243 162 VDLKLSKERLAQLLAEH-GKVVVTQGFIASNEDGETTTLGRGGSDYSAALLAALLDAEEVEIWTDVDGVYTADPRKVPDA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 829777911 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 |
9.91e-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: 341.29 E-value: 9.91e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 11 GRQLHKFGGSSLADVKCYLRVAGIMTEYSQPGD--MMVVSAAGSTTNQLISwlklsqtdrlsahqvqqslrryqseliag 88
Cdd:COG0527 2 ALIVQKFGGTSVADAERIKRVADIVKKAKEAGNrvVVVVSAMGGVTDLLIA----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 89 llpadvadglisafthdlerLAALLDSGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDF-LRAERA-AQPQ 166
Cdd:COG0527 53 --------------------LAEELLGEPSPRELDMLLSTGEQLSAALLAMALQELGVPAVSLDGRQAgIITDDNhGKAR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 167 VDEGLSYPLLQQLLvqHPGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDA 246
Cdd:COG0527 113 IDLIETPERIRELL--EEGKVVVVAGFQGVTEDGEITTLGRGGSDTTAVALAAALKADECEIWTDVDGVYTADPRIVPDA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 247 CLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIERVLA-SGTGARIVTSHDDICLIEFQVP 325
Cdd:COG0527 191 RKLPEISYEEMLELAYLGAKVLHPRAVEPAMKYNIPLRVRSTFNPDAPGTLITAEDEmEGPVVKGIASDKDIALITVSGV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 326 AGQDFKLAHKDIDLVLKRAQVRPLAVGVHNDRQLLQFCYTAEVADSALKILDEA---GLPGELRLRQGLALVAMVGAGVT 402
Cdd:COG0527 271 PMVDEPGFAARIFSALAEAGINVDMISQSSSETSISFTVPKSDLEKALEALEEElklEGLEEVEVEEDLAKVSIVGAGMR 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 829777911 403 RNPLHCHRFWQQL--KGQPVEFTWQSEEGISLVAVLRKGPTESLIQGLHTSLFRAE 456
Cdd:COG0527 351 SHPGVAARMFSALaeAGINIRMISQGSSEISISVVVDEEDAEKAVRALHEAFFLDK 406
|
|
| ThrA |
COG0460 |
Homoserine dehydrogenase [Amino acid transport and metabolism]; Homoserine dehydrogenase is ... |
478-810 |
7.52e-89 |
|
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: 282.70 E-value: 7.52e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 478 AREQVTLSARTGFEFILAGVVDSRRSllNYEGLDASRALAFFNDEAVeqdeeslflwMRAHPYDdlVVLDVTA-SEQLAD 556
Cdd:COG0460 1 LENAEELARRLGLDLRVVGVAVRDGM--KPRGIDLPRWLLTTDLEEL----------IKDPEID--VVVELTGgSEPARE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 557 QYLDFASHGFHVISANKLAGAsstDKYRQIHDAFEKTGRHWLYNATVGAGLPVNHTVRDLIeSGDSILALSGIFSGTLSW 636
Cdd:COG0460 67 LYLAALEAGKHVVTANKALLA---EHGKELFELARKNGVDLLFEAAVGGGIPIIKTLRELL-AGDRITRIEGILNGTTNY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 637 LFLQFDGT-VPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAREA-GYDIEPDAVRVESLVpagceegsvdhffen 714
Cdd:COG0460 143 ILTKMEEEgLSFSEALKEAQELGYAEADPTADVEGIDAARKLAILARLAfGTPVELEDVYVEGIT--------------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 715 geELNEQMVqrlEAANEMGLVLRYVARFEANG---KARVGVEAVRPEHPLAALLPCDNVFAIESRWYRDnpLVIRGPGAG 791
Cdd:COG0460 208 --RITAEDI---AAAKELGYVIKLLAIAERTGggvEARVHPTLVPADHPLASVNGVDNAVLVETDAYGE--LMFYGPGAG 280
|
330
....*....|....*....
gi 829777911 792 RDVTAGAIQSDINRLAKLL 810
Cdd:COG0460 281 AEPTASAVLADLLDIARGL 299
|
|
| AAK_AK |
cd04234 |
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ... |
15-298 |
7.21e-73 |
|
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: 237.37 E-value: 7.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 15 HKFGGSSLADVKCYLRVAGIMTEYSQP-GDMMVVSAAGSTTNQLISwlklsqtdrlsahqvqqslrryqseliagllpad 93
Cdd:cd04234 4 QKFGGTSVASAERIKRVADIIKAYEKGnRVVVVVSAMGGVTDLLIE---------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 94 vadglisafthdlerlaalldsgitdavYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDFLRA-ERAAQPQVDEGLS 172
Cdd:cd04234 50 ----------------------------LALLLSFGERLSARLLAAALRDRGIKARSLDARQAGITtDDNHGAARIIEIS 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 173 YPLLQQLLVQHpGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDACLLPLL 252
Cdd:cd04234 102 YERLKELLAEI-GKVPVVTGFIGRNEDGEITTLGRGGSDYSAAALAAALGADEVEIWTDVDGIYTADPRIVPEARLIPEI 180
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 829777911 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 |
1.95e-57 |
|
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: 202.97 E-value: 1.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLADVKCYLRVAGIMTEYSQPGD--MMVVSAAGSTTNQLiswLKLSQtdRLSAHQVQQSLRRYQSELIAGLLPAD 93
Cdd:TIGR00657 6 KFGGTSVGNAERIRRVAKIVLKEKKKGNqvVVVVSAMAGVTDAL---VELAE--QASPGPSKDFLEKIREKHIEILERLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 94 vaDGLISAFTHDLerLAALLDSGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWL-DAR-------DFLRAERAAQP 165
Cdd:TIGR00657 81 --PQAIAEELKRL--LDAELVLEEKPREMDRILSFGERLSAALLSAALEELGVKAVSLlGGEagiltdsNFGRARVIIEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 166 QVDEGLsyPLLQQllvqhpGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKD 245
Cdd:TIGR00657 157 LTERLE--PLLEE------GIIPVVAGFQGATEKGETTTLGRGGSDYTAALLAAALKADECEIYTDVDGIYTTDPRIVPD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 246 ACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIERVLASGTGARIVT-SHDDICLIEFQV 324
Cdd:TIGR00657 229 ARRIDEISYEEMLELASFGAKVLHPRTLEPAMRAKIPIVVKSTFNPEAPGTLIVASTKEMEEPIVKGlSLDRNQARVTVS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 325 PAGQDFKLAHKDIDLVLKRAQVRPLAVGVHNDRQLLQFCYTAEVADSA---LKILDEAGLPGELRLRQGLALVAMVGAGV 401
Cdd:TIGR00657 309 GLGMKGPGFLARVFGALAEAGINVDLISQSSSETSISFTVDKEDADQAkelLKSELNLSALSRVEVEKGLAKVSLVGAGM 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 829777911 402 TRNPLHCHRFWQQL--KGQPVEFTWQSEEGISLVAVLRKGptESLIQGLHTSLF 453
Cdd:TIGR00657 389 KSAPGVASKIFEALaqNGINIEMISSSEINISFVVDEKDA--EKAVRLLHNALF 440
|
|
| PLN02700 |
PLN02700 |
homoserine dehydrogenase family protein |
457-803 |
4.15e-52 |
|
homoserine dehydrogenase family protein
Pssm-ID: 215377 [Multi-domain] Cd Length: 377 Bit Score: 186.13 E-value: 4.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 457 KRIGLVLFGKGNIGSRWLelfaREQVT---LSARTGFEFILAGVVDSRRSLL----NYEGLD------------------ 511
Cdd:PLN02700 2 KKIPVLLLGCGGVGRHLL----RHIVScrsLHAKQGVRIRVVGVCDSKSLVLaedvLNEELDdallsevclakskgspls 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 512 -----ASRALAFFNDEAVEQDEESLFLWMRAHPyddLVVLDVTASEQLADQYLDFASHGFHVISANKLAGASSTDKYRQI 586
Cdd:PLN02700 78 algalAGGCQVFNNSELSRKVIDIATLLGKSTG---LVVVDCSASMETIGALNEAVDLGCCIVLANKKPLTSTLEDYDKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 587 HDAFektgRHWLYNATVGAGLPVNHTVRDLIESGDSILALSGIFSGTLSWLFLQFDGTVPFTDLVDQAWQQGLTEPDPRV 666
Cdd:PLN02700 155 AAHP----RRIRHESTVGAGLPVIASLNRILSSGDPVHRIVGSLSGTLGYVMSELEDGKPFSEVVKQAKSLGYTEPDPRD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 667 DLSGKDVMRKLVILAREAGYDIEPDAVRVESLVPA--GCEEGSVDHFFENG-EELNEQMVQRLEAANEMGLVLRYVARFE 743
Cdd:PLN02700 231 DLGGMDVARKALILARLLGKRINMDSIKVESLYPEemGPDLMSTDDFLHSGlVELDLPIEERVKEASLKGCVLRYVCVIE 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 744 ANGkARVGVEAVRPEHPLAALLPCDNVFAIESRWYRDNPLVIRGPGAGRDVTAGAIQSDI 803
Cdd:PLN02700 311 GSS-CQVGIRELPKDSALGRLRGSDNVVEIYSRCYSEQPLVIQGAGAGNDTTAAGVLADI 369
|
|
| PRK09084 |
PRK09084 |
aspartate kinase III; Validated |
16-300 |
2.80e-51 |
|
aspartate kinase III; Validated
Pssm-ID: 236376 [Multi-domain] Cd Length: 448 Bit Score: 185.79 E-value: 2.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLADVKCYLRVAGIMTEYSQPGdMMVVSAAGSTTNQLISWLKLSQTDRLSAHQVQQsLRRYQSELIAGLLPADVA 95
Cdd:PRK09084 5 KFGGTSVADFDAMNRSADIVLSNPNTR-LVVLSASAGVTNLLVALAEGAEPGDERLALLDE-IRQIQYAILDRLGDPNVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 96 DGLISAFTHDLERLAALLDSGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDFLRAER---AAQPQVDEglS 172
Cdd:PRK09084 83 REEIERLLENITVLAEAASLATSPALTDELVSHGELMSTLLFVELLRERGVQAEWFDVRKVMRTDDrfgRAEPDVAA--L 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 173 YPLLQQLLVQHPGKRIVVT-GFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDACLLPL 251
Cdd:PRK09084 161 AELAQEQLLPLLAEGVVVTqGFIGSDEKGRTTTLGRGGSDYSAALLAEALNASRVEIWTDVPGIYTTDPRIVPAAKRIDE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 829777911 252 LRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIER 300
Cdd:PRK09084 241 ISFEEAAEMATFGAKVLHPATLLPAVRSNIPVFVGSSKDPEAGGTWICN 289
|
|
| AAK_AKiii-LysC-EC |
cd04258 |
AAK_AKiii-LysC-EC: Amino Acid Kinase Superfamily (AAK), AKiii-LysC-EC: this CD includes the ... |
16-298 |
1.35e-49 |
|
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: 176.40 E-value: 1.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLADVKCYLRVAGIMTEYSQPGdMMVVSAAGSTTNQLISWLKLSQT-DRLSAHQVQQSLRRYQSELIAGLLPADV 94
Cdd:cd04258 5 KFGGTSVADYAAMLRCAAIVKSDASVR-LVVVSASAGVTNLLVALADAAESgEEIESIPQLHEIRAIHFAILNRLGAPEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 95 ADGLISAFTHDLERLAA--LLDSGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDFLRAER---AAQPQVDE 169
Cdd:cd04258 84 LRAKLEELLEELTQLAEgaALLGELSPASRDELLSFGERMSSLLFSEALREQGVPAEWFDVRTVLRTDSrfgRAAPDLNA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 170 glSYPLLQQLLVQHPGKRIVVT-GFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDACL 248
Cdd:cd04258 164 --LAELAAKLLKPLLAGTVVVTqGFIGSTEKGRTTTLGRGGSDYSAALLAEALHAEELQIWTDVAGIYTTDPRICPAARA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 829777911 249 LPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRI 298
Cdd:cd04258 242 IKEISFAEAAEMATFGAKVLHPATLLPAIRKNIPVFVGSSKDPEAGGTLI 291
|
|
| Homoserine_dh |
pfam00742 |
Homoserine dehydrogenase; |
608-803 |
1.70e-49 |
|
Homoserine dehydrogenase;
Pssm-ID: 459921 [Multi-domain] Cd Length: 178 Bit Score: 172.17 E-value: 1.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 608 PVNHTVRdLIESGDSILALSGIFSGTLSWLFLQFDGT-VPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAREA-G 685
Cdd:pfam00742 1 PIIRTLR-LSLAGDRITRIEGILNGTTNYILTRMEEEgLSFSEALKEAQELGYAEADPTDDVEGIDAARKLAILARLAfG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 686 YDIEPDAVRVESLVpagceegsvdhffengeELNEQMVqrlEAANEMGLVLRYVARFEANG---KARVGVEAVRPEHPLA 762
Cdd:pfam00742 80 LDVELEDVEVEGIT-----------------RLTAEDI---AYAKELGKVIKLVASAKRDDggvEARVGPTLVPKDHPLA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 829777911 763 ALLPCDNVFAIESRWYrdNPLVIRGPGAGRDVTAGAIQSDI 803
Cdd:pfam00742 140 SVKGVDNAVVIETDRY--GELVFYGPGAGALPTASAVLADL 178
|
|
| PRK08961 |
PRK08961 |
bifunctional aspartate kinase/diaminopimelate decarboxylase; |
16-320 |
1.40e-45 |
|
bifunctional aspartate kinase/diaminopimelate decarboxylase;
Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 176.04 E-value: 1.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLADVKCYLRVAGI----MTEYSQPgdMMVVSAAGSTTNQLIswlKLSQTDRLSAH-QVQQSLRRYQSELIAGLl 90
Cdd:PRK08961 13 KFGGTSVSRRHRWDTIAKIvrkrLAEGGRV--LVVVSALSGVSNELE---AIIAAAGAGDSaSRVAAIRQRHRELLAEL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 91 paDV-ADGLISAFTHDLERL---AALLDsGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDFLRAerAAQPQ 166
Cdd:PRK08961 87 --GVdAEAVLAERLAALQRLldgIRALT-RASLRWQAEVLGQGELLSTTLGAAYLEASGLDMGWLDAREWLTA--LPQPN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 167 VDEGLSY----------PLLQQLLVQHPGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVY 236
Cdd:PRK08961 162 QSEWSQYlsvscqwqsdPALRERFAAQPAQVLITQGFIARNADGGTALLGRGGSDTSAAYFAAKLGASRVEIWTDVPGMF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 237 SADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIERVLASGTGARIVTSHDD 316
Cdd:PRK08961 242 SANPKEVPDARLLTRLDYDEAQEIATTGAKVLHPRSIKPCRDAGIPMAILDTERPDLSGTSIDGDAEPVPGVKAISRKNG 321
|
....
gi 829777911 317 ICLI 320
Cdd:PRK08961 322 IVLV 325
|
|
| AAK_AK-DapDC |
cd04259 |
AAK_AK-DapDC: Amino Acid Kinase Superfamily (AAK), AK-DapDC; this CD includes the N-terminal ... |
16-298 |
2.74e-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: 2.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLADVKCYLRVAGIMTEYSQPGD--MMVVSAAGSTTNQLIswlKLSQTDRLSAHQVQ-QSLRRYQSELIAGLLPA 92
Cdd:cd04259 5 KFGGTSVSSRARWDTIAKLAQKHLNTGGqpLIVCSALSGISNKLE---ALIDQALLDEHHSLfNAIQSRHLNLAEQLEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 93 dvADGLISAFTHDLERLAA--LLDSGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDFLRAeraAQPQVDEG 170
Cdd:cd04259 82 --ADALLANDLAQLQRWLTgiSLLKQASPRTRAEVLALGELMSTRLGAAYLEAQGLKVKWLDARELLTA---TPTLGGET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 171 LSY-----------PLLQQLLVQhpGKRIVVT-GFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSA 238
Cdd:cd04259 157 MNYlsarceseyadALLQKRLAD--GAQLIITqGFIARNAHGETVLLGRGGSDTSAAYFAAKLQAARCEIWTDVPGLFTA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 239 DPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRI 298
Cdd:cd04259 235 NPHEVPHARLLKRLDYDEAQEIATMGAKVLHPRCIPPARRANIPMVVRSTERPELSGTLI 294
|
|
| asp_kin_monofn |
TIGR00656 |
aspartate kinase, monofunctional class; This model describes a subclass of aspartate kinases. ... |
16-405 |
2.83e-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: 161.79 E-value: 2.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLADVKCYLRVAGIMTEYSQPGD--MMVVSAAGSTTNQLISwlklsqtdrlsahqvqqslrryqseliagllpad 93
Cdd:TIGR00656 6 KFGGTSVGSGERIKNAARIVLKEKMKGHkvVVVVSAMGGVTDELVS---------------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 94 VADGLISafthdlerlaalldSGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARD--------FLRAEraaqp 165
Cdd:TIGR00656 52 LAEEAIS--------------DEISPRERDELVSHGELLSSALFSSALRELGVKAIWLDGGEagirtddnFGNAK----- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 166 qVDEGLSYPLLQQLLVQhpGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKD 245
Cdd:TIGR00656 113 -IDIIATEERLLPLLEE--GIIVVVAGFQGATEKGDTTTLGRGGSDYTAALLAAALKADRVDIYTDVPGVYTTDPRVVEA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 246 ACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGsTRIERVLASGTGARIVTSHDDICLIEFQVP 325
Cdd:TIGR00656 190 AKRIDKISYEEALELATFGAKVLHPRTVEPAMRSKVPIEVRSSFDPSEG-TLITNSMENPPLVKGIALRKNVTRVTVHGL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 326 agqdfKLAHK-----DIDLVLKRAQVRPLAVGVHNDRQLLQFCYTAEVADSALKILDEAGLPGELR---LRQGLALVAMV 397
Cdd:TIGR00656 269 -----GMLGKrgflaEIFGALAERNINVDLISQTPSETSISLTVDTTDADEAVRALKDQSGAAELDrveVEEGLAKVSIV 343
|
....*...
gi 829777911 398 GAGVTRNP 405
Cdd:TIGR00656 344 GAGMVGAP 351
|
|
| AAK_AK-LysC-like |
cd04244 |
AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the ... |
16-299 |
2.60e-42 |
|
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: 155.99 E-value: 2.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLADVKCYLRVAGIMTEYSqPGD--MMVVSAAGSTTNQLISWLKLSQTDRLS-AHQVQQSLRRYQSELIAGLLPA 92
Cdd:cd04244 5 KFGGTSVGSAERIRHVADLVGTYA-EGHevVVVVSAMGGVTDRLLLAAEAAVSGRIAgVKDFIEILRLRHIKAAKEAISD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 93 DVADGLISAFTHDLERLAALLdSGItdAVYAEV--------VGHGEVWSARLMAAVLQHLGVDAAWLDA--------RDF 156
Cdd:cd04244 84 EEIAEVESIIDSLLEELEKLL-YGI--AYLGELtprsrdyiVSFGERLSAPIFSAALRSLGIKARALDGgeagiitdDNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 157 LRAE--RAAQPQVDEGLsYPLLQQllvqhpGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAG 234
Cdd:cd04244 161 GNARplPATYERVRKRL-LPMLED------GKIPVVTGFIGATEDGAITTLGRGGSDYSATIIGAALDADEIWIWKDVDG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 829777911 235 VYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIE 299
Cdd:cd04244 234 VMTADPRIVPEARTIPRLSYAEAMELAYFGAKVLHPRTVEPAMEKGIPVRVKNTFNPEAPGTLIT 298
|
|
| PLN02551 |
PLN02551 |
aspartokinase |
16-315 |
4.20e-34 |
|
aspartokinase
Pssm-ID: 178166 [Multi-domain] Cd Length: 521 Bit Score: 137.55 E-value: 4.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLADVKCYLRVAGIMTEYSQPGDMMVVSAAGSTTNQLISWLKLS---QTDRLSAHQVQQSLRRYQSELIAGL-LP 91
Cdd:PLN02551 57 KFGGSSVASAERMREVADLILSFPDERPVVVLSAMGKTTNNLLLAGEKAvscGVTNVSEIEELSAIRELHLRTADELgVD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 92 ADVADGLisafthdLERLAALLdSGI------TDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDA--------RDFL 157
Cdd:PLN02551 137 ESVVEKL-------LDELEQLL-KGIammkelTPRTRDYLVSFGERMSTRIFAAYLNKIGVKARQYDAfdigfittDDFT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 158 RAERAAQpqvdeglSYPLLQQLLVQHPGKRI---VVTGFISRS-NAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVA 233
Cdd:PLN02551 209 NADILEA-------TYPAVAKRLHGDWIDDPavpVVTGFLGKGwKTGAITTLGRGGSDLTATTIGKALGLREIQVWKDVD 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 234 GVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRI-------ERVLASGT 306
Cdd:PLN02551 282 GVLTCDPRIYPNAVPVPYLTFDEAAELAYFGAQVLHPQSMRPAREGDIPVRVKNSYNPTAPGTLItktrdmsKAVLTSIV 361
|
....*....
gi 829777911 307 GARIVTSHD 315
Cdd:PLN02551 362 LKRNVTMLD 370
|
|
| PRK06291 |
PRK06291 |
aspartate kinase; Provisional |
16-300 |
2.47e-33 |
|
aspartate kinase; Provisional
Pssm-ID: 235773 [Multi-domain] Cd Length: 465 Bit Score: 134.28 E-value: 2.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLADVKCYLRVAGIMTEYSQPGD--MMVVSAAGSTTNQLISWLK--LSQTDRLSAHQVQQSLRRYQSELIAGLLP 91
Cdd:PRK06291 6 KFGGTSVGDGERIRHVAKLVKRYRSEGNevVVVVSAMTGVTDALLEIAEqaLDVRDIAKVKDFIADLRERHYKAIEEAIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 92 A-DVADGLISAFTHDLERLAALLdSGI------TDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARD--------F 156
Cdd:PRK06291 86 DpDIREEVSKTIDSRIEELEKAL-VGVsylgelTPRSRDYILSFGERLSAPILSGALRDLGIKSVALTGGEagiitdsnF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 157 LRAE--RAAQPQVDEGLSyPLLQQLLVqhPgkriVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAG 234
Cdd:PRK06291 165 GNARplPKTYERVKERLE-PLLKEGVI--P----VVTGFIGETEEGIITTLGRGGSDYSAAIIGAALDADEIWIWTDVDG 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 829777911 235 VYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIER 300
Cdd:PRK06291 238 VMTTDPRIVPEARVIPKISYIEAMELSYFGAKVLHPRTIEPAMEKGIPVRVKNTFNPEFPGTLITS 303
|
|
| AA_kinase |
pfam00696 |
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
12-286 |
3.22e-33 |
|
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: 127.87 E-value: 3.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 12 RQLHKFGGSSLADVKCYLRVAGIMTEYSQPG-DMMVVSAAGSTTNQLISWLKLSQtdrlsahqvqqslrryqseliagll 90
Cdd:pfam00696 2 RVVIKLGGSSLTDKERLKRLADEIAALLEEGrKLVVVHGGGAFADGLLALLGLSP------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 91 padvadglisafthdlERLAALLDSGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDFLRAERaaqpqVDEG 170
Cdd:pfam00696 57 ----------------RFARLTDAETLEVATMDALGSLGERLNAALLAAGLPAVGLPAAQLLATEAGFIDD-----VVTR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 171 LSYPLLQQLLvqHPGKRIVVTGFISRSNAGETvllGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDACLLP 250
Cdd:pfam00696 116 IDTEALEELL--EAGVVPVITGFIGIDPEGEL---GRGSSDTLAALLAEALGADKLIILTDVDGVYTADPRKVPDAKLIP 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 829777911 251 LLRLDEA-----SELARLAAPVLHARTLQPVSGSDIDLQLR 286
Cdd:pfam00696 191 EISYDELlellaSGLATGGMKVKLPAALEAARRGGIPVVIV 231
|
|
| AAK_AKiii-YclM-BS |
cd04245 |
AAK_AKiii-YclM-BS: Amino Acid Kinase Superfamily (AAK), AKiii-YclM-BS; this CD includes the ... |
16-298 |
1.12e-31 |
|
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: 125.08 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLADVKCYLRVAGIMTeySQPG-DMMVVSAAGSTTNQ-------LISWLKLSQTDRLSAHQVQQSLRRYQSELIA 87
Cdd:cd04245 5 KFGGSSLASAEQFQKVKAIVK--ADPErKIVVVSAPGKRFKDdtkvtdlLILYAEAVLAGEDTESIFEAIVDRYAEIADE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 88 GLLPADVADgLISAFTHDLERLaallDSGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDF--LRAERAAQP 165
Cdd:cd04245 83 LGLPMSILE-EIAEILENLANL----DYANPDYLLDALKARGEYLNAQLMAAYLNYQGIDARYVIPKDAglVVTDEPGNA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 166 QVDEGlSYPLLQQLLvqHPGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKD 245
Cdd:cd04245 158 QILPE-SYQKIKKLR--DSDEKLVIPGFYGYSKNGDIKTFSRGGSDITGAILARGFQADLYENFTDVDGIYAANPRIVAN 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 829777911 246 ACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRI 298
Cdd:cd04245 235 PKPISEMTYREMRELSYAGFSVFHDEALIPAIEAGIPINIKNTNHPEAPGTLI 287
|
|
| AAK_AKii-LysC-BS |
cd04261 |
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal ... |
15-294 |
1.40e-31 |
|
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: 123.41 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 15 HKFGGSSLADVKCYLRVAGIMTEYSQPGD--MMVVSAAGSTTNQLISWlklsqtdrlsAHQVqqSLRRYQSELiagllpa 92
Cdd:cd04261 4 QKFGGTSVASIERIKRVAERIKKRKKKGNqvVVVVSAMGGTTDELIEL----------AKEI--SPRPPAREL------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 93 dvaDGLISAfthdlerlaalldsgitdavyaevvghGEVWSARLMAAVLQHLGVDA-AWLDARDFLRAE----RAAQPQV 167
Cdd:cd04261 65 ---DVLLST---------------------------GEQVSIALLAMALNRLGIKAiSLTGWQAGILTDghhgKARIIDI 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 168 DEGLsyplLQQLLVQhpGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDAC 247
Cdd:cd04261 115 DPDR----IRELLEE--GDVVIVAGFQGINEDGDITTLGRGGSDTSAVALAAALGADRCEIYTDVDGVYTADPRIVPKAR 188
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 829777911 248 LLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQG 294
Cdd:cd04261 189 KLDEISYDEMLEMASLGAKVLHPRSVELAKKYGVPLRVLSSFSEEPG 235
|
|
| PRK05925 |
PRK05925 |
aspartate kinase; Provisional |
14-461 |
3.05e-31 |
|
aspartate kinase; Provisional
Pssm-ID: 235646 [Multi-domain] Cd Length: 440 Bit Score: 127.62 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 14 LHKFGGSSLADVKCYLRVAGIMTEySQPgDMMVVSAAGSTTNQLISWLKLSQTDRlsaHQVQQSLRRYQSELIAGLlpad 93
Cdd:PRK05925 5 VYKFGGTSLGTAESIRRVCDIICK-EKP-SFVVVSAVAGVTDLLEEFCRLSKGKR---EALTEKIREKHEEIAKEL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 94 vadGLISAFTHDLERLAALLDSG-ITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDAR-------DFLRAEraaqP 165
Cdd:PRK05925 76 ---GIEFSLSPWWERLEHFEDVEeISSEDQARILAIGEDISASLICAYCCTYVLPLEFLEARqviltddQYLRAV----P 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 166 QVDegLSYPLLQQLLVQHPGKRIVvTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKD 245
Cdd:PRK05925 149 DLA--LMQTAWHELALQEDAIYIM-QGFIGANSSGKTTVLGRGGSDFSASLIAELCKAREVRIYTDVNGIYTMDPKIIKD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 246 ACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRIERVLASGT-GARI----VTSHDDICLI 320
Cdd:PRK05925 226 AQLIPELSFEEMQNLASFGAKVLHPPMLKPCVRAGIPIFVTSTFDVTKGGTWIYASDKEVSyEPRIkalsLKQNQALWSV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 321 EFQVPAGQDFklahKDIDLVLKRAQVRP-------LAVGVHNDRQLLqfcyTAEVADSALKILDEAGLpgeLRLRQGLAL 393
Cdd:PRK05925 306 DYNSLGLVRL----EDVLGILRSLGIVPglvmaqnLGVYFTIDDDDI----SEEYPQHLTDALSAFGT---VSCEGPLAL 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 829777911 394 VAMVGAG-----VTRNPLHCHRFWQqlkgQPVeFTW-QSEEGISLvaVLRKGPTESLIQGLHTSLFRaEKRIGL 461
Cdd:PRK05925 375 ITMIGAKlaswkVVRTFTEKLRGYQ----TPV-FCWcQSDMALNL--VVNEELAVAVTELLHNDYVK-QKFSVV 440
|
|
| AAK_AK-DapG-like |
cd04246 |
AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the ... |
16-298 |
5.61e-31 |
|
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: 121.83 E-value: 5.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLADVKCYLRVAGIMTEYSQPGD--MMVVSAAGSTTNQLISWlklsqtdrlsAHQVqqSLRRYQSELiagllpad 93
Cdd:cd04246 5 KFGGTSVADIERIKRVAERIKKAVKKGYqvVVVVSAMGGTTDELIGL----------AKEV--SPRPSPREL-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 94 vaDGLISAfthdlerlaalldsgitdavyaevvghGEVWSARLMAAVLQHLGVDA-AWLDAR-------DFLRAERAaqp 165
Cdd:cd04246 65 --DMLLST---------------------------GEQISAALLAMALNRLGIKAiSLTGWQagiltddHHGNARII--- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 166 QVDEGLSYPLLQQllvqhpGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKD 245
Cdd:cd04246 113 DIDPKRILEALEE------GDVVVVAGFQGVNEDGEITTLGRGGSDTTAVALAAALKADRCEIYTDVDGVYTADPRIVPK 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 829777911 246 ACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGsTRI 298
Cdd:cd04246 187 ARKLDVISYDEMLEMASLGAKVLHPRSVELAKKYNVPLRVRSSFSENPG-TLI 238
|
|
| PRK06270 |
PRK06270 |
homoserine dehydrogenase; Provisional |
457-803 |
1.17e-28 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235763 [Multi-domain] Cd Length: 341 Bit Score: 117.66 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 457 KRIGLVLFGKGNIGSRWLELFAREQVTLSARTGFEFILAGVVDSRRSLLNYEGLDASRALAF-FNDEAVEQDEESLFLW- 534
Cdd:PRK06270 1 MEMKIALIGFGGVGQGVAELLAEKREYLKKRYGLDLKVVAIADSSGSAIDPDGLDLELALKVkEETGKLADYPEGGGEIs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 535 ----MRAHPYDdlVVLDVTASE----QLADQYLDFA-SHGFHVISANK--LAGAsstdkYRQIHDAFEKTGRHWLYNATV 603
Cdd:PRK06270 81 glevIRSVDAD--VVVEATPTNietgEPALSHCRKAlERGKHVVTSNKgpLALA-----YKELKELAKKNGVRFRYEATV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 604 GAGLPVNHTVRDLIeSGDSILALSGIFSGTLSWLFLQFD-GTVPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAR 682
Cdd:PRK06270 154 GGAMPIINLAKETL-AGNDIKSIKGILNGTTNYILTRMEeEGLSYEQALAEAQELGYAEADPTYDVEGIDAALKVVILAN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 683 EA-GYDIEPDAVRVE---SLVPagceegsvdhffengeelneqmvQRLEAANEMGLVLRYVARFEANGKARVGVEAVRPE 758
Cdd:PRK06270 233 SIlGADLTIKDVEVEgitKITP-----------------------EAIELAAKEGYRIKLIGEVSREKDLSVSPRLVPLD 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 829777911 759 HPLA---ALlpcdNVFAIESrwyrD--NPLVIRGPGAGRDVTAGAIQSDI 803
Cdd:PRK06270 290 HPLAvsgTL----NAATFET----DlaGDVTVVGRGAGSIETASAILSDL 331
|
|
| PRK06635 |
PRK06635 |
aspartate kinase; Reviewed |
15-400 |
2.50e-28 |
|
aspartate kinase; Reviewed
Pssm-ID: 235843 [Multi-domain] Cd Length: 404 Bit Score: 118.29 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 15 HKFGGSSLADVKCYLRVAGIMTEYSQPGDMM--VVSAAGSTTNQLISWlklsqtdrlsAHQvqqslrryqseliagllpa 92
Cdd:PRK06635 6 QKFGGTSVGDVERIKRVAERVKAEVEAGHQVvvVVSAMGGTTDELLDL----------AKE------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 93 dvadglISAFTHDLErlaalldsgitdavYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARD--------FLRAeRAAQ 164
Cdd:PRK06635 57 ------VSPLPDPRE--------------LDMLLSTGEQVSVALLAMALQSLGVKARSFTGWQagiitdsaHGKA-RITD 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 165 pqVDEGLsyplLQQLLVQhpGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVK 244
Cdd:PRK06635 116 --IDPSR----IREALDE--GDVVVVAGFQGVDEDGEITTLGRGGSDTTAVALAAALKADECEIYTDVDGVYTTDPRIVP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 245 DACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQG-------STRIERVLASGtgariVTSHDDI 317
Cdd:PRK06635 188 KARKLDKISYEEMLELASLGAKVLHPRSVEYAKKYNVPLRVRSSFSDNPGtlitgeeEEIMEQPVVTG-----IAFDKDE 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 318 CLIEF-QVP-----AGQDFK-LAHKDI--DLVLKraqvrplavGVHNDRQL-LQFCYTAEVADSALKIL----DEAGLpG 383
Cdd:PRK06635 263 AKVTVvGVPdkpgiAAQIFGaLAEANInvDMIVQ---------NVSEDGKTdITFTVPRDDLEKALELLeevkDEIGA-E 332
|
410
....*....|....*..
gi 829777911 384 ELRLRQGLALVAMVGAG 400
Cdd:PRK06635 333 SVTYDDDIAKVSVVGVG 349
|
|
| PRK08373 |
PRK08373 |
aspartate kinase; Validated |
16-278 |
8.35e-27 |
|
aspartate kinase; Validated
Pssm-ID: 236250 [Multi-domain] Cd Length: 341 Bit Score: 112.46 E-value: 8.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSladVKCYLRVAGIMTEYSQPGD--MMVVSAAGSTTNQLIswlKLSQT-DRLSAHQVQQSLRRYQSELIAGLLPa 92
Cdd:PRK08373 9 KFGGSS---VRYDFEEALELVKYLSEENevVVVVSALKGVTDKLL---KLAETfDKEALEEIEEIHEEFAKRLGIDLEI- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 93 dvadglisaFTHDLERLAALLDSGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDFLRAE----------RA 162
Cdd:PRK08373 82 ---------LSPYLKKLFNSRPDLPSEALRDYILSFGERLSAVLFAEALENEGIKGKVVDPWEILEAKgsfgnafidiKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 163 AQPQVdeGLSYPLLQQllvqhpGKRIVVTGFISRSNaGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRK 242
Cdd:PRK08373 153 SKRNV--KILYELLER------GRVPVVPGFIGNLN-GFRATLGRGGSDYSAVALGVLLNAKAVLIMSDVEGIYTADPKL 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 829777911 243 VKDACLLPLLRLDEASELARLAAPVLHARTLQPVSG 278
Cdd:PRK08373 224 VPSARLIPYLSYDEALIAAKLGMKALHWKAIEPVKG 259
|
|
| AAK_AK-Hom3 |
cd04247 |
AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal ... |
16-276 |
2.82e-25 |
|
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: 107.13 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLAdvKCYLRVAG-IMTEYSQPGDMMVVSAAGS-------TTNQLISWLKLSQTDRLSAhqVQQSLRRYQSELIA 87
Cdd:cd04247 6 KFGGTSVG--KFPDNIADdIVKAYLKGNKVAVVCSARStgtkaegTTNRLLQAADEALDAQEKA--FHDIVEDIRSDHLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 88 G----LLPADVADGLISAFTHDLERL-----AALLDSGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDFLR 158
Cdd:cd04247 82 AarkfIKNPELQAELEEEINKECELLrkyleAAKILSEISPRTKDLVISTGEKLSCRFMAAVLRDRGVDAEYVDLSHIVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 159 AERAAQpQVDEGLSYPLLQQL--LVQHPGKRI-VVTGFISRSNAGETVLLGRNGSDYSAtqigALAGV----SRVTIWSD 231
Cdd:cd04247 162 LDFSIE-ALDQTFYDELAQVLgeKITACENRVpVVTGFFGNVPGGLLSQIGRGYTDLCA----ALCAVglnaDELQIWKE 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 829777911 232 VAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPV 276
Cdd:cd04247 237 VDGIFTADPRKVPTARLLPSITPEEAAELTYYGSEVIHPFTMEQV 281
|
|
| AAK |
cd02115 |
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
16-310 |
4.00e-25 |
|
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: 105.22 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLADVKCYLRVAGIMTEYSQPGD--MMVVSAAGSTTNQLiswlklsqtdrlsahqvqqslrryqseliagllpad 93
Cdd:cd02115 3 KFGGSSVSSEERLRNLARILVKLASEGGrvVVVHGAGPQITDEL------------------------------------ 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 94 vadglisafTHDLERLAALLDSGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARDFLRAeRAAQPQVDE--GL 171
Cdd:cd02115 47 ---------LAHGELLGYARGLRITDRETDALAAMGEGMSNLLIAAALEQHGIKAVPLDLTQAGFA-SPNQGHVGKitKV 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 172 SYPLLQQLLVQhpGKRIVVTGFISRSNAGETVLlGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDACLLPL 251
Cdd:cd02115 117 STDRLKSLLEN--GILPILSGFGGTDEKETGTL-GRGGSDSTAALLAAALKADRLVILTDVDGVYTADPRKVPDAKLLSE 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 829777911 252 LRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQgstrIERVLASGTGARI 310
Cdd:cd02115 194 LTYEEAAELAYAGAMVLKPKAADPAARAGIPVRIANTENPGA----LALFTPDGGGTLI 248
|
|
| PRK09034 |
PRK09034 |
aspartate kinase; Reviewed |
16-298 |
1.01e-24 |
|
aspartate kinase; Reviewed
Pssm-ID: 236364 [Multi-domain] Cd Length: 454 Bit Score: 108.35 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLADVKCYLRVAGIMTEysqpgD----MMVVSAAGS-------TTNQLISWLKLSQTDRLSAHQVQQSLRRYQsE 84
Cdd:PRK09034 5 KFGGSSLASAEQFKKVLNIVKS-----DperkIVVVSAPGKrfkedtkVTDLLILYAEAVLAGEDYEDIFEAIIARYA-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 85 LIAGL-LPADvadgLISAFTHDLERLAALlDSGITDAVYAEVVGHGEVWSARLMAAVLQHLGVDAAWLDARD--FLRAER 161
Cdd:PRK09034 79 IAKELgLDAD----ILEKIEEILEHLANL-ASRNPDRLLDAFKARGEDLNAKLIAAYLNYEGIPARYVDPKEagIIVTDE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 162 AAQPQVDEGlSYPLLQQLlvQHPGKRIVVTGFISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPR 241
Cdd:PRK09034 154 PGNAQVLPE-SYDNLKKL--RDRDEKLVIPGFFGVTKDGQIVTFSRGGSDITGAILARGVKADLYENFTDVDGIYAANPR 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 829777911 242 KVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRI 298
Cdd:PRK09034 231 IVKNPKSIKEITYREMRELSYAGFSVFHDEALIPAYRGGIPINIKNTNNPEDPGTLI 287
|
|
| NAD_binding_3 |
pfam03447 |
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ... |
465-600 |
7.70e-24 |
|
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: 96.99 E-value: 7.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 465 GKGNIGSRWLELFAREQVTLSARtgfefiLAGVVDSRrsllnyegLDASRALAFFNDEAVEQDEESLFLWMRAhpydDLV 544
Cdd:pfam03447 1 GCGAIGSGVLEQLLRQQSEIPLE------LVAVADRD--------LLSKDPLALLPDEPLTLDLDDLIAHPDP----DVV 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 829777911 545 VlDVTASEQLADQYLDFASHGFHVISANKLAGASStDKYRQIHDAFEKTGRHWLYN 600
Cdd:pfam03447 63 V-ECASSEAVAELVLDALKAGKDVVTASKGALADL-ALYEELREAAEANGARIYVE 116
|
|
| PRK08210 |
PRK08210 |
aspartate kinase I; Reviewed |
129-402 |
3.31e-21 |
|
aspartate kinase I; Reviewed
Pssm-ID: 236188 [Multi-domain] Cd Length: 403 Bit Score: 96.85 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 129 GEVWSARLMAAVLQHLGVDAAWL---DA-----RDFLRAE-RAAQPQvdeglsypLLQQLLVQhpGKRIVVTGFISRSNA 199
Cdd:PRK08210 78 GEIISSVVFSNMLNENGIKAVALtggQAgiitdDNFTNAKiIEVNPD--------RILEALEE--GDVVVVAGFQGVTEN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 200 GETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGS 279
Cdd:PRK08210 148 GDITTLGRGGSDTTAAALGVALKAEYVDIYTDVDGIMTADPRIVEDARLLDVVSYNEVFQMAYQGAKVIHPRAVEIAMQA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 280 DIDLQLRCSYTPDQGsTRIERVLASGTGA----RIVT--SH-DDIclIEFQVPAGQDFKLAHKDIDLVLKRAQVRPLAVG 352
Cdd:PRK08210 228 NIPLRIRSTYSDSPG-TLITSLGDAKGGIdveeRLITgiAHvSNV--TQIKVKAKENAYDLQQEVFKALAEAGISVDFIN 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 829777911 353 VHNDRQLlqFCYTAEVADSALKILDEAGLpgELRLRQGLALVAMVGAGVT 402
Cdd:PRK08210 305 IFPTEVV--FTVSDEDSEKAKEILENLGL--KPSVRENCAKVSIVGAGMA 350
|
|
| PRK08374 |
PRK08374 |
homoserine dehydrogenase; Provisional |
457-807 |
1.10e-20 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 169409 [Multi-domain] Cd Length: 336 Bit Score: 94.10 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 457 KRIGLVLFGKGNIGSRWLELFAREQVTLSARTGFEFILAGVVDSRRSLLNYEGLDASRAL----------AFFND-EAVE 525
Cdd:PRK08374 1 MEVKVSIFGFGNVGRAVAEVLAEKSRVFKERYGVELKVVSITDTSGTIWLPEDIDLREAKevkenfgklsNWGNDyEVYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 526 QDEESLFLWMRAHpyddlVVLDVTASEQLADQYLDFASHGFHVISANKLAGASStdkYRQIHDAFEKTGRHWLYNATVGA 605
Cdd:PRK08374 81 FSPEEIVEEIDAD-----IVVDVTNDKNAHEWHLEALKEGKSVVTSNKPPIAFH---YDELLDLANERNLPYLFEATVMA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 606 GLPVNHTVRDLIeSGDSILALSGIFSGTLSWLFLQFDGTVPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAREAG 685
Cdd:PRK08374 153 GTPIIGLLRENL-LGDTVKRIEAVVNATTTFILTRMEQGKTFEEALKEAQTLGIAERDPSKDIDGIDAGYKATILHWVAF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 686 YDIEPDAVRVEslvpagceegsvdhffengeELNEQMVQRLEAANEMGLVLRYVARFEaNGKARVGVEAVRPEHPLAaLL 765
Cdd:PRK08374 232 PPITFEEVGIR--------------------GIKDVTEGEIERAKAKGRNVRLVATVE-EGRISVKPKKLPENSPLA-VE 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 829777911 766 PCDNVFAIESrwyrDN--PLVIRGPGAGRDVTAGAIQSDINRLA 807
Cdd:PRK08374 290 GVENAAVIKT----DLlgELVLKGPGAGGKETASGVVTDIIKAA 329
|
|
| AspKin_pair |
TIGR02078 |
Pyrococcus aspartate kinase subunit, putative; This family consists of proteins restricted to ... |
16-281 |
1.26e-20 |
|
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: 93.70 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSL-ADVKCYLRVAGIMTEYSQPgdMMVVSAAGSTTNQLIswlKLSQT-DRLSAHQVQQSLRRYQSELiagllpaD 93
Cdd:TIGR02078 5 KFGGSSVrYAFEEALELVKSLSEEKRV--IVVVSALKGITDCLI---RYANTfDKSAALEIEEIYEEFAKEL-------G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 94 VADGLISAFTHDLERLAALLDSGITDavyaEVVGHGEVWSARLMAAvlqhlGVDAAWLDARDFLRAE-RAAQPQVD---- 168
Cdd:TIGR02078 73 VDLNILSPYLKELFNPPDLPKEALRD----YILSLGERLSAVIFAE-----GINGKVVDPWDIFFAKgDFGNAFIDikks 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 169 ---EGLSYPLLQQllvqhpGKRIVVTGFISRSNaGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKD 245
Cdd:TIGR02078 144 krnAKILYEVLES------GKIPVIPGFYGNLN-GYRVTLGRGGSDYSAVALGVLLNSKLVAIMSDVEGIFTADPKLVPS 216
|
250 260 270
....*....|....*....|....*....|....*.
gi 829777911 246 ACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDI 281
Cdd:TIGR02078 217 ARLIPYLSYEEIKIAAKLGMKALQWKAADLAKEYKI 252
|
|
| AAK_AKi-DapG-BS |
cd04260 |
AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the ... |
129-298 |
4.05e-20 |
|
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: 90.52 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 129 GEVWSARLMAAVLQHLGVDAAWLDARD--FLRAERAAQPQVDEGLSYPLLQQLlvqHPGKRIVVTGFISRSNAGETVLLG 206
Cdd:cd04260 76 GEIISAVVLTSTLRAQGLKAVALTGAQagILTDDNYSNAKIIKVNPKKILSAL---KEGDVVVVAGFQGVTEDGEVTTLG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 207 RNGSDYSATQIGALAGVSRVTIWSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLR 286
Cdd:cd04260 153 RGGSDTTAAALGAALNAEYVEIYTDVDGIMTADPRVVPNARILDVVSYNEVFQMAHQGAKVIHPRAVEIAMQANIPIRIR 232
|
170
....*....|..
gi 829777911 287 CSYTPDQGsTRI 298
Cdd:cd04260 233 STMSENPG-TLI 243
|
|
| PRK07431 |
PRK07431 |
aspartate kinase; Provisional |
1-405 |
8.45e-20 |
|
aspartate kinase; Provisional
Pssm-ID: 236018 [Multi-domain] Cd Length: 587 Bit Score: 94.22 E-value: 8.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 1 MSVIAQagakgrqlhKFGGSSLADVKCYLRVAGIMTEYSQPGD--MMVVSAAGSTTNQLiswLKLSQtdrlsahqvQQSL 78
Cdd:PRK07431 1 MALIVQ---------KFGGTSVGSVERIQAVAQRIARTKEAGNdvVVVVSAMGKTTDEL---VKLAK---------EISS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 79 RRYQSELiagllpadvaDGLISAfthdlerlaalldsgitdavyaevvghGEVWSARLMAAVLQHLGVDAAWLDA----- 153
Cdd:PRK07431 60 NPPRREM----------DMLLST---------------------------GEQVSIALLSMALHELGQPAISLTGaqvgi 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 154 ---RDFLRAeRAAQPQVDEglsyplLQQLLVQhpGKRIVVTGF--ISRSNAGETVLLGRNGSDYSATQIGALAGVSRVTI 228
Cdd:PRK07431 103 vteSEHGRA-RILEIKTDR------IQRHLDA--GKVVVVAGFqgISLSSNLEITTLGRGGSDTSAVALAAALGADACEI 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 229 WSDVAGVYSADPRKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTpDQGSTRI------ERVL 302
Cdd:PRK07431 174 YTDVPGVLTTDPRLVPEAQLMDEISCDEMLELASLGASVLHPRAVEIARNYGVPLVVRSSWS-DAPGTLVtsppprPRSL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 303 ASGTGARIVtshDDICLIEFQ-------VP-----AGQDFK-LAHK--DIDLVlkraqVRPLAVGVHNDrqlLQFCYTAE 367
Cdd:PRK07431 253 GGLELGKPV---DGVELDEDQakvallrVPdrpgiAAQLFEeLAAQgvNVDLI-----IQSIHEGNSND---IAFTVAEN 321
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 829777911 368 VADSAL----KILDEAGlPGELRLRQGLALVAMVGAGVTRNP 405
Cdd:PRK07431 322 ELKKAEavaeAIAPALG-GAEVLVETNVAKLSISGAGMMGRP 362
|
|
| PRK06392 |
PRK06392 |
homoserine dehydrogenase; Provisional |
459-681 |
2.32e-18 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 102354 [Multi-domain] Cd Length: 326 Bit Score: 87.23 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 459 IGLVLFGKGNIGSRWLEL---FAREQvtlsaRTGFEFILAGVVDSRRSLLNYEGLDASRALAFFNDEAVEQDEESLFLWM 535
Cdd:PRK06392 1 IRISIIGLGNVGLNVLRIiksRNDDR-----RNNNGISVVSVSDSKLSYYNERGLDIGKIISYKEKGRLEEIDYEKIKFD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 536 RAHPYDDLVVLDVTASEQLADQ----YLDFASHGFHVISANKlagASSTDKYRQIHDAFEKTGRHWLYNATVGAGLPVnH 611
Cdd:PRK06392 76 EIFEIKPDVIVDVTPASKDGIReknlYINAFEHGIDVVTANK---SGLANHWHDIMDSASKNRRIIRYEATVAGGVPL-F 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 612 TVRDLIESGDSILALSGIFSGTLSWLFLQFDGTVPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILA 681
Cdd:PRK06392 152 SLRDYSTLPSRIKNFRGIVSSTINYVIRQEANGRGFLDVVKIAQKMGIAETNYSDDLMGLDAARKSVILA 221
|
|
| PRK06349 |
PRK06349 |
homoserine dehydrogenase; Provisional |
457-810 |
3.32e-12 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235783 [Multi-domain] Cd Length: 426 Bit Score: 69.33 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 457 KRIGLVLFGKGNIGSRWLELFAREQVTLSARTGFEFILAGVVDsrRSLLNYEGLDASRALaFFND-EAVEQDEESlflwm 535
Cdd:PRK06349 2 KPLKVGLLGLGTVGSGVVRILEENAEEIAARAGRPIEIKKVAV--RDLEKDRGVDLPGIL-LTTDpEELVNDPDI----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 536 rahpydDLVVlDVTASEQLADQYLDFA-SHGFHVISANK--LAgasstdKYRQ-IHDAFEKTGRHWLYNATVGAGLPVnh 611
Cdd:PRK06349 74 ------DIVV-ELMGGIEPARELILKAlEAGKHVVTANKalLA------VHGAeLFAAAEEKGVDLYFEAAVAGGIPI-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 612 tVRDLIES--GDSILALSGIFSGT----LSWLFLqfDGTvPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAREA- 684
Cdd:PRK06349 139 -IKALREGlaANRITRVMGIVNGTtnyiLTKMTE--EGL-SFEDALKEAQRLGYAEADPTFDVEGIDAAHKLAILASLAf 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 685 GYDIEPDAVRVE---SLVPAgceegsvDhffengeelneqmvqrLEAANEMGLVLRY--VARFEANgkarvGVEA-VRP- 757
Cdd:PRK06349 215 GTRVDFDDVYVEgisKITAE-------D----------------IAYAKELGYRIKLlgIAERTEE-----GIELrVHPt 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 829777911 758 ----EHPLAALlpcDNVF---AIESrwyrDN--PLVIRGPGAGRDVTAGAIQSDINRLAKLL 810
Cdd:PRK06349 267 lipkSHPLANV---NGVMnavFVEG----DAvgETMFYGPGAGGLPTASAVVADLVDIARNL 321
|
|
| PRK08841 |
PRK08841 |
aspartate kinase; Validated |
175-295 |
1.81e-11 |
|
aspartate kinase; Validated
Pssm-ID: 181563 [Multi-domain] Cd Length: 392 Bit Score: 66.70 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 175 LLQQLLVQhpGKRIVVTGFISRSNAGETVLLGRNGSDYSATqigALAGVSRVT---IWSDVAGVYSADPRKVKDACLLPL 251
Cdd:PRK08841 120 TITELLEQ--DQIVIVAGFQGRNENGDITTLGRGGSDTTAV---ALAGALNADecqIFTDVDGVYTCDPRVVKNARKLDV 194
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 829777911 252 LRLDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGS 295
Cdd:PRK08841 195 IDFPSMEAMARKGAKVLHLPSVQHAWKHSVPLRVLSSFEVGEGT 238
|
|
| PRK06813 |
PRK06813 |
homoserine dehydrogenase; Validated |
458-810 |
8.37e-08 |
|
homoserine dehydrogenase; Validated
Pssm-ID: 168683 [Multi-domain] Cd Length: 346 Bit Score: 54.87 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 458 RIGLVLFGKGNIGSRWLELFAREQVTLSARTGFEFILAGVVDSRRSLLNYEGLDASRALAFFN-DEAVEQDEESLFLWMR 536
Cdd:PRK06813 2 KIKVVLSGYGTVGREFIKLLNEKYLYINETYGIDLVVSGVLGRNVAIHNEDGLSIHHLLRYGGgSCAIEKYIEHHPEERA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 537 AHPYDDLVVLDVTAS----EQLADQYLDFA-SHGFHVISANKlaGASSTDkYRQIHDAFEKTGRHWLYNATVGAGLPVNH 611
Cdd:PRK06813 82 TDNISGTVLVESTVTnlkdGNPGKQYIKQAiEKKMDIVAISK--GALVTN-WREINEAAKIANVRIRYSGATAAALPTLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 612 TVRdLIESGDSILALSGIFSGTLSWLFLQ-FDGTVPFTDLVDQAWQQGLTEPDPRVDLSGKDVMRKLVILAreagydiep 690
Cdd:PRK06813 159 IGQ-FSLAGCHIEKIEGILNGTTNYILTKmNEEDITFEEALKEAQSKGIAETNPILDVSGSDSACKLLLLT--------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 691 davrvESLVpaGCEEGSVDHFFENGEELNEQMVQRleaANEMGLVLRYVAR--FEANGKARVGVEA--VRPEHPLAALLP 766
Cdd:PRK06813 229 -----NSLM--GTENKLTDIHIKGIEHVTKQQIRN---AKEQNKIIKLIASayKDNEGNVNLNVEPykIEKNHPLANVNG 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 829777911 767 CDN--VFAIESrwyRDNPLVIRGPGAGRDVTAGAIQSDINRLAKLL 810
Cdd:PRK06813 299 TEKgiTFFTDT---MGQVTTIGGASNPRGAAAAALKDIINLYRKDL 341
|
|
| AAK_AK-Ectoine |
cd04248 |
AAK_AK-Ectoine: Amino Acid Kinase Superfamily (AAK), AK-Ectoine; this CD includes the ... |
16-298 |
1.95e-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: 47.44 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 16 KFGGSSLADVKCYLRVAGIMTEYSQPGDMMVVSAAGSTTNQLISWLKLSQTD------------RLSAHQVQQSLRRYQS 83
Cdd:cd04248 5 KIGGTSMSAFGAVLDNIILKPDSDLYGRVFVVSAYSGVTNALLEHKKTGAPGiyqhfvdadeawREALSALKQAMLKINE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 84 ELIAGLLPADVADGLISAFTHD----LERLAALLDSGITD------AVYAEVVGHGEVWSARLMAAVLQHLGVDA----- 148
Cdd:cd04248 85 AFADIGLDVEQADAFIGARIQDaracLHDLARLCSSGYFSlaehllAARELLASLGEAHSAFNTALLLQNRGVNArfvdl 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 149 -AWLDARDFLRAERAAQPQVDEGLSYPLlqqllvqhpgkrIVVTGFiSRSNAGETVLLGRNGSDYSATQIGALAGVSRVT 227
Cdd:cd04248 165 sGWRDSGDMTLDERISEAFRDIDPRDEL------------PIVTGY-AKCAEGLMREFDRGYSEMTFSRIAVLTGASEAI 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 829777911 228 IWSDVAgVYSADPRKVKDACLLPLLR--LDEASELARLAAPVLHARTLQPVSGSDIDLQLRCSYTPDQGSTRI 298
Cdd:cd04248 232 IHKEFH-LSSADPKLVGEDKARPIGRtnYDVADQLANLGMEAIHPKAAKGLRQAGIPLRVKNTFEPDHPGTLI 303
|
|
| ACT_AK-like_2 |
cd04892 |
ACT domains C-terminal to the catalytic domain of aspartokinase (AK; ... |
392-453 |
5.41e-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: 41.71 E-value: 5.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 829777911 392 ALVAMVGAGVTRNPLHCHRFWQQL--KGQPVEFTWQSEEGISLVAVLRKGPTESLIQGLHTSLF 453
Cdd:cd04892 1 ALVSVVGAGMRGTPGVAARIFSALaeAGINIIMISQGSSEVNISFVVDEDDADKAVKALHEEFF 64
|
|
| AAK_UMPK-like |
cd04239 |
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ... |
134-260 |
3.80e-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: 39.83 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777911 134 ARLMAAVLQHLGVDAAWLDArdflraerAAQPQVDEGLSYPLLQQLLVQHpgkRIVVTGFISRsNAGETvllgrngSDYS 213
Cdd:cd04239 77 ALALQDALEKLGVKTRVMSA--------IPMQGVAEPYIRRRAIRHLEKG---RIVIFGGGTG-NPGFT-------TDTA 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 829777911 214 ATQIGALAGVSRVTIWSDVAGVYSADPRKVKDACLLPLLRLDEASEL 260
Cdd:cd04239 138 AALRAEEIGADVLLKATNVDGVYDADPKKNPDAKKYDRISYDELLKK 184
|
|
| |
